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Conserved domains on  [gi|2024343508|ref|XP_025002382|]
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protein Shroom2 isoform X1 [Gallus gallus]

Protein Classification

shroom family protein( domain architecture ID 10098759)

shroom family protein is a PDZ (PSD-95, Dlg, and ZO-1/2) domain-containing protein that functions in cell morphology by coordinating the assembly of both microtubule and actin cytoskeletons

CATH:  2.30.42.10
Gene Ontology:  GO:0003779|GO:0005515
SCOP:  4001790

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASD2 pfam08687
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which ...
1454-1749 3.76e-144

Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure.


:

Pssm-ID: 462561 [Multi-domain]  Cd Length: 290  Bit Score: 445.94  E-value: 3.76e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508 1454 ELAREIVGRDKSLADILDPNVKIKTAMDLMVGIFPKDEHLLEEAQQRRKllpkvpSPKISEEKKEEQNAPSAISLTTNST 1533
Cdd:pfam08687    1 ELVKELVPKDKSLADILDPKPSRKTTMDLMEGLFPEDTLRAMKPDLGEA------YKKAPSEEGSEEEASGTSSLSSCSA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508 1534 YYSTSAPKAELLIKMKDMQEQQQQQQSEDDSEDELDHDLSEKKQELIDSISRKLQVLREARETLLEDIHANNILGEEVEA 1613
Cdd:pfam08687   75 YYTTSAPKAELLTKMKDLTTLPSPDQPEEQGEEELDNDLQQKKVELIESLQRKLQVLREEQEALQEEIQANAALGAEVEA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508 1614 IVKEVCKPNEFDKFKMFIGDLDKVVNLLLSLSGRLARVENALNNLDENTSPEERRTLVEKQKLLTQQHEDAKELKENLDR 1693
Cdd:pfam08687  155 LVQEVCKPNELEKYRMFIGDLEKVVSLLLSLSGRLARVENALSSLDSDADAEERQSLLEKRRLLLRQLEDAKELKENLDR 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343508 1694 RERIVFDILANYLSEENLADYEHFVKMKSALIIEQRELEDKIKLGEEQLKCLTDSL 1749
Cdd:pfam08687  235 RERVVSGILARYLTAEQLQDYRHFVKMKAALLIEQRELDEKIKLGEEQLKALKESL 290
ASD1 pfam08688
Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which ...
724-903 2.94e-57

Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure. ASD1 has been implicated directly in F-actin binding.


:

Pssm-ID: 462562 [Multi-domain]  Cd Length: 179  Bit Score: 196.02  E-value: 2.94e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508  724 KLQKSRSTATLIGSSETEEcseNGKPDAAENVNASPDTNFTSTYKDHLKEAQARVLRATSFKRRDLEPS--PAEYPPRSP 801
Cdd:pfam08688    1 LLQRSKSTFQLEGEDEAEW---SWRRPRGDEPMSDADGSFNRAYREKLKDAQSRVLRATSFRRRDLQPSvpPVPWHLSSR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508  802 ERKAGSYNSSLLALVSEDVSGFL--EATQAKPNPTGSGTHHVSRIGARKRFTTEQKLKSYSEPEKMNEVGMSEDECRAHC 879
Cdd:pfam08688   78 PRPASAHLRSPEAPISASPSPHTprERHSVTPGDRLAGPPAVRRIGGRKRLTAEQKKRSYSEPEKMNEVGVSPEPEPAPA 157
                          170       180
                   ....*....|....*....|....
gi 2024343508  880 HPETSEEalGSFADRWKFFEETSK 903
Cdd:pfam08688  158 PHFMFPE--GSVADRRKFFERRGK 179
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
35-116 2.84e-49

PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of shroom2, shroom3, shroom4, and related domains. Shroom family proteins shroom2 (also known as apical-like protein; protein APXL), shroom3 (also known as shroom-related protein), and shroom4 (also known as second homolog of apical protein) are essential regulators of cell morphology during animal development; they regulate cell architecture by directing the subcellular distribution and activation of Rho kinase (ROCK), which results in the localized activation of non-muscle myosin. The interaction between shroom and ROCK is mediated by the shroom domain 2 (SD2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This shroom2,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


:

Pssm-ID: 467232 [Multi-domain]  Cd Length: 82  Bit Score: 169.44  E-value: 2.84e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   35 RLVEVLLTGGAPWGFTLKGGREHGEPLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGFRQEAICLVKGSHKTLKLVV 114
Cdd:cd06750      1 QLIEVQLQGGAPWGFTLKGGLEHGEPLVISKIEEGGKAASVGKLQVGDEVVNINGVPLSGSRQEAIQLVKGSHKTLKLVV 80

                   ..
gi 2024343508  115 KR 116
Cdd:cd06750     81 RR 82
 
Name Accession Description Interval E-value
ASD2 pfam08687
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which ...
1454-1749 3.76e-144

Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure.


Pssm-ID: 462561 [Multi-domain]  Cd Length: 290  Bit Score: 445.94  E-value: 3.76e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508 1454 ELAREIVGRDKSLADILDPNVKIKTAMDLMVGIFPKDEHLLEEAQQRRKllpkvpSPKISEEKKEEQNAPSAISLTTNST 1533
Cdd:pfam08687    1 ELVKELVPKDKSLADILDPKPSRKTTMDLMEGLFPEDTLRAMKPDLGEA------YKKAPSEEGSEEEASGTSSLSSCSA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508 1534 YYSTSAPKAELLIKMKDMQEQQQQQQSEDDSEDELDHDLSEKKQELIDSISRKLQVLREARETLLEDIHANNILGEEVEA 1613
Cdd:pfam08687   75 YYTTSAPKAELLTKMKDLTTLPSPDQPEEQGEEELDNDLQQKKVELIESLQRKLQVLREEQEALQEEIQANAALGAEVEA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508 1614 IVKEVCKPNEFDKFKMFIGDLDKVVNLLLSLSGRLARVENALNNLDENTSPEERRTLVEKQKLLTQQHEDAKELKENLDR 1693
Cdd:pfam08687  155 LVQEVCKPNELEKYRMFIGDLEKVVSLLLSLSGRLARVENALSSLDSDADAEERQSLLEKRRLLLRQLEDAKELKENLDR 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343508 1694 RERIVFDILANYLSEENLADYEHFVKMKSALIIEQRELEDKIKLGEEQLKCLTDSL 1749
Cdd:pfam08687  235 RERVVSGILARYLTAEQLQDYRHFVKMKAALLIEQRELDEKIKLGEEQLKALKESL 290
ASD1 pfam08688
Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which ...
724-903 2.94e-57

Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure. ASD1 has been implicated directly in F-actin binding.


Pssm-ID: 462562 [Multi-domain]  Cd Length: 179  Bit Score: 196.02  E-value: 2.94e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508  724 KLQKSRSTATLIGSSETEEcseNGKPDAAENVNASPDTNFTSTYKDHLKEAQARVLRATSFKRRDLEPS--PAEYPPRSP 801
Cdd:pfam08688    1 LLQRSKSTFQLEGEDEAEW---SWRRPRGDEPMSDADGSFNRAYREKLKDAQSRVLRATSFRRRDLQPSvpPVPWHLSSR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508  802 ERKAGSYNSSLLALVSEDVSGFL--EATQAKPNPTGSGTHHVSRIGARKRFTTEQKLKSYSEPEKMNEVGMSEDECRAHC 879
Cdd:pfam08688   78 PRPASAHLRSPEAPISASPSPHTprERHSVTPGDRLAGPPAVRRIGGRKRLTAEQKKRSYSEPEKMNEVGVSPEPEPAPA 157
                          170       180
                   ....*....|....*....|....
gi 2024343508  880 HPETSEEalGSFADRWKFFEETSK 903
Cdd:pfam08688  158 PHFMFPE--GSVADRRKFFERRGK 179
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
35-116 2.84e-49

PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of shroom2, shroom3, shroom4, and related domains. Shroom family proteins shroom2 (also known as apical-like protein; protein APXL), shroom3 (also known as shroom-related protein), and shroom4 (also known as second homolog of apical protein) are essential regulators of cell morphology during animal development; they regulate cell architecture by directing the subcellular distribution and activation of Rho kinase (ROCK), which results in the localized activation of non-muscle myosin. The interaction between shroom and ROCK is mediated by the shroom domain 2 (SD2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This shroom2,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467232 [Multi-domain]  Cd Length: 82  Bit Score: 169.44  E-value: 2.84e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   35 RLVEVLLTGGAPWGFTLKGGREHGEPLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGFRQEAICLVKGSHKTLKLVV 114
Cdd:cd06750      1 QLIEVQLQGGAPWGFTLKGGLEHGEPLVISKIEEGGKAASVGKLQVGDEVVNINGVPLSGSRQEAIQLVKGSHKTLKLVV 80

                   ..
gi 2024343508  115 KR 116
Cdd:cd06750     81 RR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
35-118 2.35e-13

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 67.02  E-value: 2.35e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508    35 RLVEVLLTGGaPWGFTLKGGREHGEPLIITKIEDGSkAASVDKLLAGDEIVGINDVGLSGFRQ-EAICLVKGSHKTLKLV 113
Cdd:smart00228    3 RLVELEKGGG-GLGFSLVGGKDEGGGVVVSSVVPGS-PAAKAGLRVGDVILEVNGTSVEGLTHlEAVDLLKKAGGKVTLT 80

                    ....*
gi 2024343508   114 VKRRN 118
Cdd:smart00228   81 VLRGG 85
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
36-115 1.92e-10

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 58.83  E-value: 1.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   36 LVEVLLTGGAPWGFTLKGGREHGE-PLIITKIEDGSkAASVDKLLAGDEIVGINDVGLSGFRQE-AICLVKGSHKTLKLV 113
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSDQGDpGIFVSEVLPGG-AAEAGGLKVGDRILSINGQDVENMTHEeAVLALKGSGGKVTLT 79

                   ..
gi 2024343508  114 VK 115
Cdd:pfam00595   80 IL 81
 
Name Accession Description Interval E-value
ASD2 pfam08687
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which ...
1454-1749 3.76e-144

Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure.


Pssm-ID: 462561 [Multi-domain]  Cd Length: 290  Bit Score: 445.94  E-value: 3.76e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508 1454 ELAREIVGRDKSLADILDPNVKIKTAMDLMVGIFPKDEHLLEEAQQRRKllpkvpSPKISEEKKEEQNAPSAISLTTNST 1533
Cdd:pfam08687    1 ELVKELVPKDKSLADILDPKPSRKTTMDLMEGLFPEDTLRAMKPDLGEA------YKKAPSEEGSEEEASGTSSLSSCSA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508 1534 YYSTSAPKAELLIKMKDMQEQQQQQQSEDDSEDELDHDLSEKKQELIDSISRKLQVLREARETLLEDIHANNILGEEVEA 1613
Cdd:pfam08687   75 YYTTSAPKAELLTKMKDLTTLPSPDQPEEQGEEELDNDLQQKKVELIESLQRKLQVLREEQEALQEEIQANAALGAEVEA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508 1614 IVKEVCKPNEFDKFKMFIGDLDKVVNLLLSLSGRLARVENALNNLDENTSPEERRTLVEKQKLLTQQHEDAKELKENLDR 1693
Cdd:pfam08687  155 LVQEVCKPNELEKYRMFIGDLEKVVSLLLSLSGRLARVENALSSLDSDADAEERQSLLEKRRLLLRQLEDAKELKENLDR 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343508 1694 RERIVFDILANYLSEENLADYEHFVKMKSALIIEQRELEDKIKLGEEQLKCLTDSL 1749
Cdd:pfam08687  235 RERVVSGILARYLTAEQLQDYRHFVKMKAALLIEQRELDEKIKLGEEQLKALKESL 290
ASD1 pfam08688
Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which ...
724-903 2.94e-57

Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure. ASD1 has been implicated directly in F-actin binding.


Pssm-ID: 462562 [Multi-domain]  Cd Length: 179  Bit Score: 196.02  E-value: 2.94e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508  724 KLQKSRSTATLIGSSETEEcseNGKPDAAENVNASPDTNFTSTYKDHLKEAQARVLRATSFKRRDLEPS--PAEYPPRSP 801
Cdd:pfam08688    1 LLQRSKSTFQLEGEDEAEW---SWRRPRGDEPMSDADGSFNRAYREKLKDAQSRVLRATSFRRRDLQPSvpPVPWHLSSR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508  802 ERKAGSYNSSLLALVSEDVSGFL--EATQAKPNPTGSGTHHVSRIGARKRFTTEQKLKSYSEPEKMNEVGMSEDECRAHC 879
Cdd:pfam08688   78 PRPASAHLRSPEAPISASPSPHTprERHSVTPGDRLAGPPAVRRIGGRKRLTAEQKKRSYSEPEKMNEVGVSPEPEPAPA 157
                          170       180
                   ....*....|....*....|....
gi 2024343508  880 HPETSEEalGSFADRWKFFEETSK 903
Cdd:pfam08688  158 PHFMFPE--GSVADRRKFFERRGK 179
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
35-116 2.84e-49

PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of shroom2, shroom3, shroom4, and related domains. Shroom family proteins shroom2 (also known as apical-like protein; protein APXL), shroom3 (also known as shroom-related protein), and shroom4 (also known as second homolog of apical protein) are essential regulators of cell morphology during animal development; they regulate cell architecture by directing the subcellular distribution and activation of Rho kinase (ROCK), which results in the localized activation of non-muscle myosin. The interaction between shroom and ROCK is mediated by the shroom domain 2 (SD2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This shroom2,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467232 [Multi-domain]  Cd Length: 82  Bit Score: 169.44  E-value: 2.84e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   35 RLVEVLLTGGAPWGFTLKGGREHGEPLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGFRQEAICLVKGSHKTLKLVV 114
Cdd:cd06750      1 QLIEVQLQGGAPWGFTLKGGLEHGEPLVISKIEEGGKAASVGKLQVGDEVVNINGVPLSGSRQEAIQLVKGSHKTLKLVV 80

                   ..
gi 2024343508  115 KR 116
Cdd:cd06750     81 RR 82
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
38-116 4.54e-18

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 80.27  E-value: 4.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   38 EVLLTGGAPWGFTLKGGREHGEPLIITKIEDGSKAASVDkLLAGDEIVGINDVGLSGFRQ-EAICLVKGSHKTLKLVVKR 116
Cdd:cd06753      1 SVTLSGPAPWGFRLQGGKDFNQPLTISRVTPGGKAAQAN-LRPGDVILAINGESTEGMTHlEAQNKIKAATGSLSLTLER 79
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
39-115 2.55e-16

PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNPO2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467264 [Multi-domain]  Cd Length: 78  Bit Score: 75.42  E-value: 2.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   39 VLLTGGAPWGFTLKGGREHGEPLIITKIEDGSKAASVdKLLAGDEIVGINDV---GLSgfRQEAICLVKGSHKTLKLVVK 115
Cdd:cd10820      2 VTLTGGAPWGFRLQGGSEQKKPLQVAKIRKKSKAALA-GLCEGDELLSINGKpcaDLS--HSEAMDLIDSSGDTLQLLIK 78
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
36-115 1.55e-13

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 67.57  E-value: 1.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   36 LVEVLLTGGAPWGFTLKGGREHGEPLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGF-RQEAICLVKGSHKTLKLVV 114
Cdd:cd00136      1 TVTLEKDPGGGLGFSIRGGKDGGGGIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLtHEEAVELLKSAGGEVTLTV 80

                   .
gi 2024343508  115 K 115
Cdd:cd00136     81 R 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
35-118 2.35e-13

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 67.02  E-value: 2.35e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508    35 RLVEVLLTGGaPWGFTLKGGREHGEPLIITKIEDGSkAASVDKLLAGDEIVGINDVGLSGFRQ-EAICLVKGSHKTLKLV 113
Cdd:smart00228    3 RLVELEKGGG-GLGFSLVGGKDEGGGVVVSSVVPGS-PAAKAGLRVGDVILEVNGTSVEGLTHlEAVDLLKKAGGKVTLT 80

                    ....*
gi 2024343508   114 VKRRN 118
Cdd:smart00228   81 VLRGG 85
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
46-116 5.71e-12

PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Drosophila melanogaster Zasp52 and related domains. Drosophila melanogaster Zasp52 (also known as Z band alternatively spliced PDZ-motif protein or Zasp) colocalizes with integrins at myotendinous junctions and with alpha-actinin at Z-disks and is required for muscle attachment as well as Z-disk assembly and maintenance. The Zasp52 actin-binding site includes the extended PDZ domain and the ZM region. The Zasp52-PDZ domain is required for myofibril assembly. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Zasp52-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 62.93  E-value: 5.71e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024343508   46 PWGFTLKGGREHGEPLIITKIEDGSKAASVdKLLAGDEIVGINDVGLSGFR-QEAICLVKGSHKTLKLVVKR 116
Cdd:cd23068     12 PWGFRLQGGADFGQPLSIQKVNPGSPADKA-GLRRGDVILRINGTDTSNLThKQAQDLIKRAGNDLQLTVQR 82
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
36-115 1.92e-10

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 58.83  E-value: 1.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   36 LVEVLLTGGAPWGFTLKGGREHGE-PLIITKIEDGSkAASVDKLLAGDEIVGINDVGLSGFRQE-AICLVKGSHKTLKLV 113
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSDQGDpGIFVSEVLPGG-AAEAGGLKVGDRILSINGQDVENMTHEeAVLALKGSGGKVTLT 79

                   ..
gi 2024343508  114 VK 115
Cdd:pfam00595   80 IL 81
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
35-116 2.58e-10

PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467219 [Multi-domain]  Cd Length: 85  Bit Score: 58.42  E-value: 2.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   35 RLVEVLLTGGAPWGFTLKGGREHGEPLIITKIEDGSKAASVDkLLAGDEIVGINDVGLSGF-RQEAICLVKgSHKTLKLV 113
Cdd:cd06737      3 RLVRLDRRGPESLGFSVRGGLEHGCGLFVSHVSPGSQADNKG-LRVGDEIVRINGYSISQCtHEEVINLIK-TKKTVSLK 80

                   ...
gi 2024343508  114 VKR 116
Cdd:cd06737     81 VRH 83
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
48-115 2.35e-08

PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntrophin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467262 [Multi-domain]  Cd Length: 83  Bit Score: 52.96  E-value: 2.35e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343508   48 GFTLKGGREHGEPLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGFR-QEAICLVKGSHKTLKLVVK 115
Cdd:cd06801     14 GISIKGGAEHKMPILISKIFKGQAADQTGQLFVGDAILSVNGENLEDAThDEAVQALKNAGDEVTLTVK 82
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
39-116 8.17e-08

PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467217 [Multi-domain]  Cd Length: 84  Bit Score: 51.43  E-value: 8.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   39 VLLTGGAPWGFTLKGGREHGE-PLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGF-RQEAICLVKGSHKTLKLVVKR 116
Cdd:cd06735      5 ELERGPKGFGFSIRGGREYNNmPLYVLRLAEDGPAQRDGRLRVGDQILEINGESTQGMtHAQAIELIRSGGSVVRLLLRR 84
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
48-116 1.57e-07

PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the first PDZ domain of the canonical isoform of PDZD7- isoform 1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD7-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467269 [Multi-domain]  Cd Length: 84  Bit Score: 50.51  E-value: 1.57e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343508   48 GFTLKGGREHGEPLIITKIEDGSkAASVDKLLAGDEIVGINDVGLSGFRQEAICLVKGSHKTLKLVVKR 116
Cdd:cd10833     15 GFSVRGGSEHGLGIFVSKVEEGS-AAERAGLCVGDKITEVNGVSLENITMSSAVKVLTGSNRLRMVVRR 82
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
35-115 4.12e-06

PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Lin-7-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467258 [Multi-domain]  Cd Length: 86  Bit Score: 46.66  E-value: 4.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   35 RLVEvLLTGGAPWGFTLKGGREHGEPLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGFRQE-AICLVKGSHKTLKLV 113
Cdd:cd06796      3 RVVE-LPKTEEGLGFNVMGGKEQNSPIYISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEkAVELLKAAQGSVKLV 81

                   ..
gi 2024343508  114 VK 115
Cdd:cd06796     82 VR 83
PDZ7_PDZD2-PDZ4_hPro-IL-16-like cd06763
PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 ...
37-104 1.54e-05

PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of PDZD2, also known as KIAA0300, PIN-1, PAPIN, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family include the PDZ domain of the secreted mature form of human interleukin-16 (IL-16); this is the fourth PDZ domain (PDZ4) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467244 [Multi-domain]  Cd Length: 86  Bit Score: 44.91  E-value: 1.54e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024343508   37 VEvLLTGGAPWGFTLKGGRE--HGE-PLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGF-RQEAICLVK 104
Cdd:cd06763      4 VE-LEKGSAGLGFSLEGGKGspLGDrPLTIKRIFKGGAAEQSGVLQVGDEILQINGTSLQGLtRFEAWNIIK 74
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
47-115 2.08e-05

PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467222 [Multi-domain]  Cd Length: 82  Bit Score: 44.28  E-value: 2.08e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024343508   47 WGFTLKGGREHGEPLIITKIEDGSKAasvDK--LLAGDEIVGINDVGLSGF-RQEAICLVKGShKTLKLVVK 115
Cdd:cd06740     15 LGFSIRGGAEHGVGIYVSLVEPGSLA---EKegLRVGDQILRVNDVSFEKVtHAEAVKILRVS-KKLVLSVR 82
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
48-92 3.14e-05

PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GOPC and related domains. GOPC, also known as PIST (PDZ domain protein interacting specifically with TC10), FIG (fused in glioblastoma), and CAL (CFTR-associated ligand), regulates the trafficking of a wide array of proteins, including small GTPases, receptors, and cell surface molecules such as cadherin 23 and CFTR. It may regulate CFTR chloride currents and acid-sensing ASIC3 currents by modulating cell surface expression of both channels, and may play a role in autophagy. Interaction partners of the GOPC PDZ domains include: FZD5, FZD8, ASIC3, CFTR, MUC3, ARFRP1, Ggamma13, neuroligin, and Stargazin. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GOPC-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467261 [Multi-domain]  Cd Length: 83  Bit Score: 43.90  E-value: 3.14e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2024343508   48 GFTLKGGREHGEPLIITKIEDGSKAASVDKLLAGDEIVGINDVGL 92
Cdd:cd06800     14 GISITGGKEHGVPILISEIHEGQPADRCGGLYVGDAILSVNGIDL 58
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
48-116 4.65e-05

PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467187 [Multi-domain]  Cd Length: 92  Bit Score: 43.79  E-value: 4.65e-05
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gi 2024343508   48 GFTLKGGREH-----GEPLI-ITKIEDGSKAASVDKLLAGDEIVGINDVGLSGFRQ-EAICLVKGSHKTLKLVVKR 116
Cdd:cd06703     15 GFSIAGGKGStpfrdGDEGIfISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHdQAVALLTSSSPTITLVVER 90
PDZ1_Dlg1-2-4-like cd06723
PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
39-117 4.77e-05

PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467206 [Multi-domain]  Cd Length: 89  Bit Score: 43.46  E-value: 4.77e-05
                           10        20        30        40        50        60        70        80
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gi 2024343508   39 VLLTGGAPWGFTLKGGREH----GEPLI-ITKIEDGSKAASVDKLLAGDEIVGINDVGLSGF-RQEAICLVKGSHKTLKL 112
Cdd:cd06723      5 TLERGNSGLGFSIAGGTDNphigDDPSIyITKIIPGGAAAADGRLRVNDIILRVNDVDVRNVtHSVAVEALKEAGSIVRL 84

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gi 2024343508  113 VVKRR 117
Cdd:cd06723     85 YVKRR 89
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
35-116 5.09e-05

PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467223 [Multi-domain]  Cd Length: 84  Bit Score: 43.41  E-value: 5.09e-05
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gi 2024343508   35 RLVEVLLTGGAPWGFTLKGGREHGEPLIITKIEDGSkAASVDKLLAGDEIVGINDVGLSGF-RQEAICLVKgSHKTLKLV 113
Cdd:cd06741      2 RKVNLVVEDGQSLGLMIRGGAEYGLGIYVTGVDPGS-VAENAGLKVGDQILEVNGRSFLDItHDEAVKILK-SSKHLIMT 79

                   ...
gi 2024343508  114 VKR 116
Cdd:cd06741     80 VKD 82
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
37-116 5.71e-05

PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ6 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467171 [Multi-domain]  Cd Length: 85  Bit Score: 43.45  E-value: 5.71e-05
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gi 2024343508   37 VEVLLTGGaPWGFTLKGGREHGEPLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGFR-QEAICLVKGSHKTLKLVVK 115
Cdd:cd06683      6 VELKRYGG-PLGITISGTEEPFDPIVISGLTEGGLAERTGAIHVGDRILAINGESLRGKPlSEAIHLLQNAGDTVTLKIS 84

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gi 2024343508  116 R 116
Cdd:cd06683     85 R 85
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
48-115 4.41e-04

PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein phosphatase non-receptor type 4 (PTNP4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PTPN3, PTPN4 and related domains. PTPN3 (also known as protein-tyrosine phosphatase H1, PTP-H1) has a tumor-suppressive or a tumor-promoting role in many cancers. It serves as a specific phosphatase for the MAP kinase p38gamma; the two interact via their PDZ domains and cooperate to promote Ras-induced oncogenesis. Interaction partners of the PTPN3 PDZ domain include p38gamma and human papillomavirus E6 oncoprotein. PTPN4 (also known as protein-tyrosine phosphatase MEG1) plays a role in immunity, learning, synaptic plasticity or cell homeostasis. p38gamma is also an interaction partner of the PTPN4 PDZ domain: PTPN4 regulates neuronal cell homeostasis by protecting neurons against apoptosis; binding of the C terminus of p38gamma to the PDZ domain of PTPN4, antagonizes the catalytic autoinhibition of PTPN4, leading to cell apoptosis. Other interaction partners of the PTPN4 PDZ domain include glutamate receptor subunit GluN2A, and RABV strain G protein, among others. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467190 [Multi-domain]  Cd Length: 90  Bit Score: 40.76  E-value: 4.41e-04
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gi 2024343508   48 GFTLKGGREHGEPLIITKIEDGSKAA-SVDKLLAGDEIVGINDVGLSGFRQE-AICLVKGSHKT----LKLVVK 115
Cdd:cd06706     17 GFNVKGGVDQKMPVIVSRVAPGTPADlCIPRLNEGDQVLLINGRDISEHTHDqVVMFIKASRERhsgeLVLLVR 90
PDZ1_GRIP1-2-like cd06687
PDZ domain 1 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
36-115 4.69e-04

PDZ domain 1 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467175 [Multi-domain]  Cd Length: 83  Bit Score: 40.47  E-value: 4.69e-04
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gi 2024343508   36 LVEVLLTGGAPWGFTLKGGREHGEPLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGFRQ-EAICLVKGSHKTLKLVV 114
Cdd:cd06687      2 VVELIKKEGSTLGLTVSGGIDKDGKPRVSNLRPGGIAARSDQLNVGDYIKSVNGIRTTKLRHdEIISLLKNVGERVVLEV 81

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gi 2024343508  115 K 115
Cdd:cd06687     82 E 82
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
45-104 6.20e-04

PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange factor 6, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Rap guanine nucleotide exchange factor 2 (RapGEF2, also named RA-GEF-1, PDZ-GEF1, CNrasGEF and nRapGEP) and Rap guanine nucleotide exchange factor 6 (RapGEF6, also named RA-GEF-2 and PDZ-GEF2). RapGEF2 and RapGEF6 constitute a subfamily of guanine nucleotide exchange factors (GEFs) for RAP small GTPases that is characterized by the possession of the PDZ and Ras/Rap-associating domains. They activate Rap small GTPases, by catalyzing the release of GDP from the inactive GDP-bound forms, thereby accelerating GTP loading to yield the active GTP-bound forms. The PDZ domain of RapGEF6 (also known as PDZ-GEF2) binds junctional adhesion molecule A (JAM-A). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RapGEF2 and RapGEF6 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467237 [Multi-domain]  Cd Length: 83  Bit Score: 40.33  E-value: 6.20e-04
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gi 2024343508   45 APWGFTLKGGREHGEPLIITKIEDGSKAASVDkLLAGDEIVGINdvglsGFRQEAICLVK 104
Cdd:cd06755     12 SPLHFSLLGGSEKGFGIFVSKVEKGSKAAEAG-LKRGDQILEVN-----GQNFENITLKK 65
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
35-114 6.85e-04

PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467169 [Multi-domain]  Cd Length: 89  Bit Score: 40.29  E-value: 6.85e-04
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gi 2024343508   35 RLVEVLLT--GGAPwGFTLKGGReHGE-----PLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGF-RQEAICLVKGS 106
Cdd:cd06681      1 KTVEVTLEkeGNSF-GFVIRGGA-HEDrnksrPLTVTHVRPGGPADREGTIKPGDRLLSVDGISLHGAtHAEAMSILKQC 78

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gi 2024343508  107 HKTLKLVV 114
Cdd:cd06681     79 GQEATLLI 86
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
48-117 7.57e-04

PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains, and is expressed at exceptionally high levels in the pancreas and certain cancer tissues such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467239 [Multi-domain]  Cd Length: 88  Bit Score: 40.03  E-value: 7.57e-04
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gi 2024343508   48 GFTLKGGR-----EHGepLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGF-RQEAICLVKGSHKTLKLVVKRR 117
Cdd:cd06758     15 GIQITGGKgskrgDIG--IFVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLsHQEAVAILRSSASPVQLVIASK 88
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
40-116 9.26e-04

PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467155 [Multi-domain]  Cd Length: 80  Bit Score: 39.57  E-value: 9.26e-04
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gi 2024343508   40 LLTGGAPWGFTLKGGREHGepLIITKIEDGSKAASVDKLLAGDEIVGINDVGLSGFRQEAICLV-KGSHKTLKLVVKR 116
Cdd:cd06667      5 LVNDGSGLGFGIVGGKSTG--VVVKTILPGGVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVlRQCGSHVRLVVAR 80
PDZ1_DLG5-like cd06764
PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
48-117 1.18e-03

PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467245 [Multi-domain]  Cd Length: 95  Bit Score: 39.69  E-value: 1.18e-03
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gi 2024343508   48 GFTLKGGRE----HGEP-LIITKIEDGSKAASvdKLLAGDEIVGINDVGL-SGFRQEAICLVKGSHKTLKLVVKRR 117
Cdd:cd06764     22 GFDIAGGVNdpqfPGDCsIFVTKVDKGSIADG--RLRVNDCLLRINDVDLtNKDKKQAIQAVLNGGGVINMVVRRR 95
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
42-115 4.08e-03

PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZD11, and related domains. PDZD11 (also known as ATPase-interacting PDZ protein, plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PISP) is involved in the dynamic assembly of apical junctions (AJs). It is recruited by PLEKHA7 to AJs to promote the efficient junctional recruitment and stabilization of nectins, and the efficient early phases of assembly of AJs in epithelial cells. The PDZD11 PDZ domain binds nectin-1 and nectin-3. PDZD11 also binds to a PDZ binding motif located in the C-terminal tail of the human sodium-dependent multivitamin transporter, to the cytoplasmic tail of the Menkes copper ATPase ATP7A, and to the cytoplasmic tail of all plasma membrane Ca2+-ATPase b-splice variants. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD11-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467234 [Multi-domain]  Cd Length: 83  Bit Score: 38.06  E-value: 4.08e-03
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gi 2024343508   42 TGGAPWGFTLKGGREHGEPLIITKIEDGSKAASVDkLLAGDEIVGINDVGLSGF-RQEAICLVKGShKTLKLVVK 115
Cdd:cd06752      8 PPGEQLGFNIRGGKASGLGIFISKVIPDSDAHRLG-LKEGDQILSVNGVDFEDIeHSEAVKVLKTA-REIQMRVR 80
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
48-90 4.27e-03

PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This rhophilin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467196 [Multi-domain]  Cd Length: 78  Bit Score: 37.56  E-value: 4.27e-03
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                   ....*....|....*....|....*....|....*....|...
gi 2024343508   48 GFTLKGGrehgEPLIITKIEDGSKAASvDKLLAGDEIVGINDV 90
Cdd:cd06712     14 GFTLRGD----SPVQVASVDPGSCAAE-AGLKEGDYIVSVGGV 51
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
28-116 6.65e-03

PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467176 [Multi-domain]  Cd Length: 102  Bit Score: 38.00  E-value: 6.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   28 QRAAEGyRLVEVL-----LTGGApwGFTLKGGRE--HGEPLI-ITKIEDGSKAASVDKLLAGDEIVGIN----DVGLSgf 95
Cdd:cd06689      7 QSMAQG-RQVEYIelekpESGGL--GFSVVGLKSenRGELGIfVQEIQPGSVAARDGRLKENDQILAINgqplDQSIS-- 81
                           90       100
                   ....*....|....*....|.
gi 2024343508   96 RQEAICLVKGSHKTLKLVVKR 116
Cdd:cd06689     82 HQQAIAILQQAKGSVELVVAR 102
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
35-114 8.53e-03

PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467194 [Multi-domain]  Cd Length: 76  Bit Score: 36.84  E-value: 8.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343508   35 RLVEVLlTGGAPWGFTLKGGRehgePLIITKIEDGSKAASVDkLLAGDEIVGINDVGLSGFRQE-AICLVKGSHKTLKLV 113
Cdd:cd06710      1 RTVEIA-RGRAGYGFTISGQA----PCVLSCVVRGSPADVAG-LKAGDQILAVNGINVSKASHEdVVKLIGKCTGVLRLV 74

                   .
gi 2024343508  114 V 114
Cdd:cd06710     75 I 75
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
48-114 9.31e-03

PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 13 of MUPP1. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ13 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ13 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467164 [Multi-domain]  Cd Length: 83  Bit Score: 36.93  E-value: 9.31e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024343508   48 GFTLKGG--REHGEPLIITKIEDGSKAASVD-KLLAGDEIVGINDVGLSGF-RQEAICLVKGSHKTLKLVV 114
Cdd:cd06676     12 GFSIVGGfgSPHGDLPIYVKTVFEKGAAAEDgRLKRGDQILAVNGESLEGVtHEEAVNILKKTKGTVTLTV 82
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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