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Conserved domains on  [gi|1958751928|ref|XP_038958736|]
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PDZ domain-containing protein GIPC2 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH2_GIPC cd21180
GIPC-homology 2 (GH2) domain found in the GIPC family; The GIPC family includes PDZ ...
 160-224 7.69e-38

GIPC-homology 2 (GH2) domain found in the GIPC family; The GIPC family includes PDZ domain-containing proteins, GIPC1 (also called GAIP C-terminus-interacting protein, RGS-GAIP-interacting protein, RGS19-interacting protein 1, RGS19IP1, synectin, tax interaction protein 2, or TIP-2), GIPC2, and GIPC3, which may act as scaffold proteins linking heterotrimeric G-proteins to seven-transmembrane-type WNT receptor or to receptor tyrosine kinases. They might play key roles in carcinogenesis and embryogenesis through modulation of growth factor signaling and cell adhesion. GIPCs are proteins with a GIPC homology 1 (GH1) domain, a central PDZ domain and a GH2 domain. This model corresponds to the GH2 domain, which mediates the interaction with myosin VI and is involved in homodimerization in the autoinhibited state.


:

Pssm-ID: 409666  Cd Length: 65  Bit Score: 126.12  E-value: 7.69e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958751928 160 KAKAIEKVDDLLELYMGIRDIDLATTMFEAGKDKSNPDEFAVALDETLGDFAFPDEFMFDVWGAI 224
Cdd:cd21180     1 EEKAIEKIDDLLESYMGIRDDELAQTIVELGKDKSNPDEFAEALDESLGDFAFPDEFVFDVWGAI 65
PDZ_canonical super family cl49608
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 59-119 2.16e-29

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.


The actual alignment was detected with superfamily member cd23078:

Pssm-ID: 483948  Cd Length: 93  Bit Score: 105.38  E-value: 2.16e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958751928  59 QRIKDGSTIDSVKTICVGDHIECINGENIVGWRHFEVAKKLKELKKEELFTLQLIEPKKAF 119
Cdd:cd23078    33 KRIKDGSVIDSVKTICVGDHIECINGENIVGWRHYEVAKKLKELKKEELFTLKLIEPKKAF 93
 
Name Accession Description Interval E-value
GH2_GIPC cd21180
GIPC-homology 2 (GH2) domain found in the GIPC family; The GIPC family includes PDZ ...
 160-224 7.69e-38

GIPC-homology 2 (GH2) domain found in the GIPC family; The GIPC family includes PDZ domain-containing proteins, GIPC1 (also called GAIP C-terminus-interacting protein, RGS-GAIP-interacting protein, RGS19-interacting protein 1, RGS19IP1, synectin, tax interaction protein 2, or TIP-2), GIPC2, and GIPC3, which may act as scaffold proteins linking heterotrimeric G-proteins to seven-transmembrane-type WNT receptor or to receptor tyrosine kinases. They might play key roles in carcinogenesis and embryogenesis through modulation of growth factor signaling and cell adhesion. GIPCs are proteins with a GIPC homology 1 (GH1) domain, a central PDZ domain and a GH2 domain. This model corresponds to the GH2 domain, which mediates the interaction with myosin VI and is involved in homodimerization in the autoinhibited state.


Pssm-ID: 409666  Cd Length: 65  Bit Score: 126.12  E-value: 7.69e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958751928 160 KAKAIEKVDDLLELYMGIRDIDLATTMFEAGKDKSNPDEFAVALDETLGDFAFPDEFMFDVWGAI 224
Cdd:cd21180     1 EEKAIEKIDDLLESYMGIRDDELAQTIVELGKDKSNPDEFAEALDESLGDFAFPDEFVFDVWGAI 65
PDZ_GIPC2 cd23078
PDZ domain of PDZ domain-containing protein GIPC2, and related domains; PDZ (PSD-95 ...
 59-119 2.16e-29

PDZ domain of PDZ domain-containing protein GIPC2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GIPC2, and related domains. GIPC2 belongs to the GIPC family, members of which contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC proteins function as adaptor molecules that assemble RTKs, GPCRs, integrins, transmembrane proteins and cytoplasmic signaling regulators as cargoes of MYO6-dependent endocytic transport. Mutations in the Gipc2 gene have been linked to cancer. 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 GIPC2 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: 467291  Cd Length: 93  Bit Score: 105.38  E-value: 2.16e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958751928  59 QRIKDGSTIDSVKTICVGDHIECINGENIVGWRHFEVAKKLKELKKEELFTLQLIEPKKAF 119
Cdd:cd23078    33 KRIKDGSVIDSVKTICVGDHIECINGENIVGWRHYEVAKKLKELKKEELFTLKLIEPKKAF 93
 
Name Accession Description Interval E-value
GH2_GIPC cd21180
GIPC-homology 2 (GH2) domain found in the GIPC family; The GIPC family includes PDZ ...
 160-224 7.69e-38

GIPC-homology 2 (GH2) domain found in the GIPC family; The GIPC family includes PDZ domain-containing proteins, GIPC1 (also called GAIP C-terminus-interacting protein, RGS-GAIP-interacting protein, RGS19-interacting protein 1, RGS19IP1, synectin, tax interaction protein 2, or TIP-2), GIPC2, and GIPC3, which may act as scaffold proteins linking heterotrimeric G-proteins to seven-transmembrane-type WNT receptor or to receptor tyrosine kinases. They might play key roles in carcinogenesis and embryogenesis through modulation of growth factor signaling and cell adhesion. GIPCs are proteins with a GIPC homology 1 (GH1) domain, a central PDZ domain and a GH2 domain. This model corresponds to the GH2 domain, which mediates the interaction with myosin VI and is involved in homodimerization in the autoinhibited state.


Pssm-ID: 409666  Cd Length: 65  Bit Score: 126.12  E-value: 7.69e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958751928 160 KAKAIEKVDDLLELYMGIRDIDLATTMFEAGKDKSNPDEFAVALDETLGDFAFPDEFMFDVWGAI 224
Cdd:cd21180     1 EEKAIEKIDDLLESYMGIRDDELAQTIVELGKDKSNPDEFAEALDESLGDFAFPDEFVFDVWGAI 65
PDZ_GIPC2 cd23078
PDZ domain of PDZ domain-containing protein GIPC2, and related domains; PDZ (PSD-95 ...
 59-119 2.16e-29

PDZ domain of PDZ domain-containing protein GIPC2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GIPC2, and related domains. GIPC2 belongs to the GIPC family, members of which contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC proteins function as adaptor molecules that assemble RTKs, GPCRs, integrins, transmembrane proteins and cytoplasmic signaling regulators as cargoes of MYO6-dependent endocytic transport. Mutations in the Gipc2 gene have been linked to cancer. 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 GIPC2 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: 467291  Cd Length: 93  Bit Score: 105.38  E-value: 2.16e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958751928  59 QRIKDGSTIDSVKTICVGDHIECINGENIVGWRHFEVAKKLKELKKEELFTLQLIEPKKAF 119
Cdd:cd23078    33 KRIKDGSVIDSVKTICVGDHIECINGENIVGWRHYEVAKKLKELKKEELFTLKLIEPKKAF 93
PDZ_GIPC cd06707
PDZ domain of GIPC family proteins; GIPC1/GIPC (GAIP/RGS19-interacting protein), GIPC2, and ...
 60-117 5.92e-22

PDZ domain of GIPC family proteins; GIPC1/GIPC (GAIP/RGS19-interacting protein), GIPC2, and GIPC3 (also known as C19orf64) constitute the GIPC family. These proteins contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC proteins function as adaptor molecules that assemble RTKs, GPCRs, integrins, transmembrane proteins and cytoplasmic signaling regulators as cargoes of MYO6-dependent endocytic transport. Mutations in the Gipc1 and Gipc2 genes have been linked to cancer, while mutations in the Gipc3 gene cause nonsyndromic hearing loss. 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 GIPC 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: 467191 [Multi-domain]  Cd Length: 89  Bit Score: 86.13  E-value: 5.92e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958751928  60 RIKDGSTIDSVKTICVGDHIECINGENIVGWRHFEVAKKLKELKKEELFTLQLIEPKK 117
Cdd:cd06707    32 RIKEGSIMDKVPAICVGDHIEKINGESLVGCRHYEVARMLKEIPIGETFTLRLVEPKK 89
PDZ_GIPC3 cd23079
PDZ domain of PDZ domain-containing protein GIPC3, and related domains; PDZ (PSD-95 ...
 59-117 2.76e-19

PDZ domain of PDZ domain-containing protein GIPC3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GIPC3, and related domains. GIPC3 (also known as C19orf64) belongs to the GIPC family, members of which contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC proteins function as adaptor molecules that assemble RTKs, GPCRs, integrins, transmembrane proteins and cytoplasmic signaling regulators as cargoes of MYO6-dependent endocytic transport. Mutations in the Gipc3 gene cause nonsyndromic hearing loss. 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 GIPC3 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: 467292 [Multi-domain]  Cd Length: 89  Bit Score: 79.19  E-value: 2.76e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958751928  59 QRIKDGSTIDSVKTICVGDHIECINGENIVGWRHFEVAKKLKELKKEELFTLQLIEPKK 117
Cdd:cd23079    31 KRIKEGSIIDRIKAVCVGDHIEAINDQSIVGCRHYEVAKMLRELPKSQPFTLRLVEPKR 89
GH2_like cd21690
GIPC homology 2 (GH2) domain-like family; The GIPC (GAIP C-terminus-interacting protein) ...
 162-224 9.03e-19

GIPC homology 2 (GH2) domain-like family; The GIPC (GAIP C-terminus-interacting protein) family of proteins mediate endocytosis by tethering cargo proteins to the motor myosin VI. This model represents the C-terminal GIPC homology 2 or GH2 domain (plus the linker to the PDZ domain located N-terminally of GH2), which mediates the interaction with myosin VI and is involved in homodimerization in the autoinhibited state. The family also includes DEAH box protein 8 (DHX8) and similar proteins. DHX8 (a human homolog of yeast Prp22), also called RNA helicase HRH1, is an ATP-dependent RNA helicase involved in pre-mRNA splicing as a component of the spliceosome. It facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 contains a GH2-like domain at the N-terminus, which shows high sequence similarity with the GH2 domain found in GIPC proteins.


Pssm-ID: 409667  Cd Length: 62  Bit Score: 77.13  E-value: 9.03e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958751928 162 KAIEKVDDLLELYMGIRDIDLATTMFEAGKDKSNPDEFAVALDEtlGDFAFPDEFMFDVWGAI 224
Cdd:cd21690     2 SAIEKVDDLLKNYLGIDDPELAEFVISLAKKKKNPDEFAEALDE--NDAAFPDEFVFDLYRAI 62
PDZ_GIPC1 cd23077
PDZ domain of PDZ domain-containing protein GIPC1; PDZ (PSD-95 (Postsynaptic density protein ...
 59-120 3.13e-16

PDZ domain of PDZ domain-containing protein GIPC1; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GIPC1, and related domains. GIPC1 (also known as GIPC, GAIP/RGS19-interacting protein or Tax-interacting protein 2) belongs to the GIPC family, members of which contain an N-terminal GIPC-homology 1 (GH1) domain, a central PDZ domain, and a C-terminal GH2 domain. GIPC1 functions as an adaptor molecule for loading PDZ-target cargoes on the MYO6 motor protein. The GIPC1 PDZ domain interacts with a variety of ligands, such as RGS19, NRP1, GLUT1, SEMA4C, SDC4 and IGF1R. 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 GIPC1 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: 467290 [Multi-domain]  Cd Length: 94  Bit Score: 71.38  E-value: 3.13e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958751928  59 QRIKDGSTIDSVKTICVGDHIECINGENIVGWRHFEVAKKLKELKKEELFTLQLIEPKKAFE 120
Cdd:cd23077    33 KRIKEGSVIDRIQLISVGDMIEAINGQSLLGCRHYEVARLLKELPRGRTFTLKLTEPRKAFD 94
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 59-96 6.76e-05

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: 40.22  E-value: 6.76e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958751928  59 QRIKDGSTIDSVKTICVGDHIECINGENIVGWRHFEVA 96
Cdd:cd00136    29 SRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAV 66
 
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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