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Conserved domains on  [gi|22328940|ref|NP_194324|]
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ENTH/ANTH/VHS superfamily protein [Arabidopsis thaliana]

Protein Classification

ANTH domain-containing protein( domain architecture ID 10541692)

ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; similar to Homo sapiens phosphatidylinositol-binding clathrin assembly protein and clathrin coat assembly protein AP180

CATH:  1.20.58.150|1.25.40.90
Gene Ontology:  GO:0030276|GO:0048268|GO:0072583
PubMed:  12740367|12742163|22748146|14657269
SCOP:  4000571|4000581

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 31-314 1.03e-118

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


:

Pssm-ID: 400137  Cd Length: 272  Bit Score: 353.14  E-value: 1.03e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940    31 DLDVAIVKATNHVESAPKERHIRRIFSATSvvqPRADVAYCIHALAKRLSKTRNWVVAIKVLIVIHRTLREGDPTFREEL 110
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTS---SSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940   111 LNYSHRG-HILRISNFkddtsPLAWDCSAWIRTYALFLEERLECYRVLKYD-IEAERLPKGSgassknvdFNASQTYRTR 188
Cdd:pfam07651  78 LRARRRIsSLLRISSF-----SLSWDYGAFIRAYAKYLDERLDFHRKLPRDpGTFERVEYGS--------LVAVGDPNER 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940   189 --MLSDEELLEQLPALQQLLYRLIGCQPEGSAYSNYLIQYALALVLKESFKIYCAINDGIINLVDMFFEMSRHDAVKALN 266
Cdd:pfam07651 145 ylTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALG 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 22328940   267 IYKRAGQQAENLADFYEYCKGLELARNFQFPTLRQPPPSFLATMEDYI 314
Cdd:pfam07651 225 IYKRFVKQFERLKEFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 31-314 1.03e-118

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 353.14  E-value: 1.03e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940    31 DLDVAIVKATNHVESAPKERHIRRIFSATSvvqPRADVAYCIHALAKRLSKTRNWVVAIKVLIVIHRTLREGDPTFREEL 110
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTS---SSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940   111 LNYSHRG-HILRISNFkddtsPLAWDCSAWIRTYALFLEERLECYRVLKYD-IEAERLPKGSgassknvdFNASQTYRTR 188
Cdd:pfam07651  78 LRARRRIsSLLRISSF-----SLSWDYGAFIRAYAKYLDERLDFHRKLPRDpGTFERVEYGS--------LVAVGDPNER 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940   189 --MLSDEELLEQLPALQQLLYRLIGCQPEGSAYSNYLIQYALALVLKESFKIYCAINDGIINLVDMFFEMSRHDAVKALN 266
Cdd:pfam07651 145 ylTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALG 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 22328940   267 IYKRAGQQAENLADFYEYCKGLELARNFQFPTLRQPPPSFLATMEDYI 314
Cdd:pfam07651 225 IYKRFVKQFERLKEFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 32-154 2.96e-62

ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.


Pssm-ID: 340767  Cd Length: 120  Bit Score: 201.35  E-value: 2.96e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940  32 LDVAIVKATNHVESAPKERHIRRIFSATSVVQPRADVAYCIHALAKRLSKtRNWVVAIKVLIVIHRTLREGDPTFREELL 111
Cdd:cd03564   1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHALAKRLHK-KNWIVVLKTLIVIHRLLREGSPSFLEELL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 22328940 112 NYshRGHILRISNFKDDTSPLAWDCSAWIRTYALFLEERLECY 154
Cdd:cd03564  80 RY--SGHIFNLSNFKDDSSPEAWDLSAFIRRYARYLEERLECF 120
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
31-160 1.80e-38

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 137.76  E-value: 1.80e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940     31 DLDVAIVKATNHVESAPKERHIRRIFSATSvvQPRADVAYCIHALAKRLSKTRNWVVAIKVLIVIHRTLREGDPtfrEEL 110
Cdd:smart00273   2 DLEVKVRKATNNDEWGPKGKHLREIIQGTH--NEKSSFAEIMAVLWRRLNDTKNWRVVYKALILLHYLLRNGSP---RVI 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 22328940    111 LN-YSHRGHILRISNFKDDtSPLAWDCSAWIRTYALFLEERLECYRVLKYD 160
Cdd:smart00273  77 LEaLRNRNRILNLSDFQDI-DSRGKDQGANIRTYAKYLLERLEDDRRLKEE 126
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 31-314 1.03e-118

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 353.14  E-value: 1.03e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940    31 DLDVAIVKATNHVESAPKERHIRRIFSATSvvqPRADVAYCIHALAKRLSKTRNWVVAIKVLIVIHRTLREGDPTFREEL 110
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTS---SSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940   111 LNYSHRG-HILRISNFkddtsPLAWDCSAWIRTYALFLEERLECYRVLKYD-IEAERLPKGSgassknvdFNASQTYRTR 188
Cdd:pfam07651  78 LRARRRIsSLLRISSF-----SLSWDYGAFIRAYAKYLDERLDFHRKLPRDpGTFERVEYGS--------LVAVGDPNER 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940   189 --MLSDEELLEQLPALQQLLYRLIGCQPEGSAYSNYLIQYALALVLKESFKIYCAINDGIINLVDMFFEMSRHDAVKALN 266
Cdd:pfam07651 145 ylTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALG 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 22328940   267 IYKRAGQQAENLADFYEYCKGLELARNFQFPTLRQPPPSFLATMEDYI 314
Cdd:pfam07651 225 IYKRFVKQFERLKEFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 32-154 2.96e-62

ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.


Pssm-ID: 340767  Cd Length: 120  Bit Score: 201.35  E-value: 2.96e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940  32 LDVAIVKATNHVESAPKERHIRRIFSATSVVQPRADVAYCIHALAKRLSKtRNWVVAIKVLIVIHRTLREGDPTFREELL 111
Cdd:cd03564   1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHALAKRLHK-KNWIVVLKTLIVIHRLLREGSPSFLEELL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 22328940 112 NYshRGHILRISNFKDDTSPLAWDCSAWIRTYALFLEERLECY 154
Cdd:cd03564  80 RY--SGHIFNLSNFKDDSSPEAWDLSAFIRRYARYLEERLECF 120
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 32-154 4.32e-49

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly protein AP180 and similar proteins; This subfamily is composed of plant clathrin coat assembly protein AP180 and other ANTH domain containing proteins that are yet to be characterized. Arabidopsis thaliana AP180 (At-AP180) is a binding partner of plant alphaC-adaptin; it functions as a clathrin assembly protein that promotes the formation of cages with an almost uniform size distribution. In addition to At-AP180, Arabidopsis thaliana contains many ANTH domain containing proteins labelled as putative clathrin assembly proteins included in this subfamily such as At4g02650, At5g10410, At2g25430, and At1g33340, among others. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of plant clathrin coat assembly protein AP180 and similar proteins.


Pssm-ID: 340784  Cd Length: 122  Bit Score: 166.65  E-value: 4.32e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940  32 LDVAIVKATNHVESAPKERHIRRIFSATSVVqpRADVAYCIHALAKRLSKTRNWVVAIKVLIVIHRTLREGDPTFREELL 111
Cdd:cd16987   1 LEVAVVKATSHDDAPPDEKYVREILSLGSSS--RAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGSPILEQELS 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 22328940 112 NYSHRGH-ILRISNFKDDTSPLAWDCSAWIRTYALFLEERLECY 154
Cdd:cd16987  79 LAPSGGRnPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 122
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
31-160 1.80e-38

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 137.76  E-value: 1.80e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940     31 DLDVAIVKATNHVESAPKERHIRRIFSATSvvQPRADVAYCIHALAKRLSKTRNWVVAIKVLIVIHRTLREGDPtfrEEL 110
Cdd:smart00273   2 DLEVKVRKATNNDEWGPKGKHLREIIQGTH--NEKSSFAEIMAVLWRRLNDTKNWRVVYKALILLHYLLRNGSP---RVI 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 22328940    111 LN-YSHRGHILRISNFKDDtSPLAWDCSAWIRTYALFLEERLECYRVLKYD 160
Cdd:smart00273  77 LEaLRNRNRILNLSDFQDI-DSRGKDQGANIRTYAKYLLERLEDDRRLKEE 126
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 33-154 8.99e-18

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins; This subfamily includes yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins. There are two YAP180 proteins in Saccharomyces cerevisiae, AP180A (yAP180A or YAP1801) and AP180B (yAP180B or YAP1802). They are involved in endocytosis and clathrin cage assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of plant clathrin coat assembly protein AP180 and similar proteins.


Pssm-ID: 340785  Cd Length: 117  Bit Score: 79.15  E-value: 8.99e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940  33 DVAIVKATNHVESAPKERHIRRIFSATSvvQPRADVAYCIHALAKRLSKTrNWVVAIKVLIVIHRTLREGDPtfREELLN 112
Cdd:cd16988   2 EKLVKGATKIKLAPPKAKYLDPILLATY--SSDASFGEIVRALSRRLRDN-SWTVVFKSLIVLHLMIREGET--DDVLLY 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 22328940 113 YSHRGHILRISNFKDDTSPLAWDCSAwIRTYALFLEERLECY 154
Cdd:cd16988  77 YLSRPDFLDLRKIRNGSSAGSGQLQN-IQRYAAYLKERVKEY 117
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
 34-152 3.52e-14

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.


Pssm-ID: 340783  Cd Length: 117  Bit Score: 68.95  E-value: 3.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940  34 VAIVKATNHVESAPKERHIRRIFSATSvvqPRADVAYCIHALAKRLSKTrNWVVAIKVLIVIHRTLREGDPtfREELLNY 113
Cdd:cd16986   3 KAVNKATNKTDSPPKPKHVRTIIVKSW---THQKGPQFYEELSKRLLLN-NPVVQFKALVTLHKVLRDGPP--ELSLLGG 76

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 22328940 114 SHRGHILRISNFKDDTSPLAWDCSAWIRTYALFLEERLE 152
Cdd:cd16986  77 YLDAWLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVV 115
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 35-154 4.40e-13

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) subfamily; The Adaptor Protein 180 (AP180) subfamily members are phosphatidylinositol-binding clathrin assembly proteins, including mammalian clathrin coat assembly protein AP180 and Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), Drosophila LAP (also called Like-AP180 or AP180), and Caenorhabditis elegans Uncoordinated protein 11 (unc-11, also called AP180-like adaptor protein). They are components of the adaptor complexes which link clathrin to receptors in coated vesicles. AP180 and CALM play important roles in clathrin-mediated endocytosis. AP180, also called 91 kDa synaptosomal-associated protein (SNAP91) or phosphoprotein F1-20, is a brain-specific clathrin-binding protein which stimulates clathrin assembly during the recycling of synaptic vesicles. CALM, also called phosphatidylinositol binding clathrin assembly protein (PICALM), is ubiquitously expressed. Members of this subfamily contain ANTH domains, which bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of the Adaptor Protein 180 (AP180) subfamily.


Pssm-ID: 340782  Cd Length: 117  Bit Score: 65.91  E-value: 4.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940  35 AIVKATNHVESAPKERHIRRIFSATSvvQPRADVAYCIHALAKRlSKTRNWVVAIKVLIVIHRTLREGDPTFREELlnyS 114
Cdd:cd16985   4 AVCKATTHEVMGPKKKHLDYLVQCTN--EPNVNIPQLADLLFER-TQNSSWVVVFKALITTHHLMVYGNERFIQYL---A 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 22328940 115 HRGHILRISNFKDDTSPLAWDCSAWIRTYALFLEERLECY 154
Cdd:cd16985  78 SRNSLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKAISY 117
ANTH_N_HIP1_like cd17006
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 34-152 1.70e-07

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.


Pssm-ID: 340803  Cd Length: 114  Bit Score: 49.97  E-value: 1.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940  34 VAIVKATNHVESAPKERHIRRIFSATSvvqpRADVAYCIHALAKRLSKTRNWVVAIKVLIVIHRTLREGDPT-FREellN 112
Cdd:cd17006   3 ISINKAINPQEVPVKEKHVRSIIIGTH----QEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSvLRD---S 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 22328940 113 YSHRGHILRISNF----KDDTSPLawdcsawIRTYALFLEERLE 152
Cdd:cd17006  76 QRYRSRLKELGKLwghlKDGYGKL-------IAQYCKLLITKLE 112
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
 32-106 7.14e-07

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.


Pssm-ID: 340804  Cd Length: 115  Bit Score: 48.07  E-value: 7.14e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328940  32 LDVAIVKATNHVESAPKERHIRRIFSATSVVQPRADVAYCIhalaKRLSKTRNWVVAIKVLIVIHRTLREGDPTF 106
Cdd:cd17007   1 LQVAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNAL----KTQPLLSDEVQCFKALITIHKVLQEGHPSA 71
ANTH_N_HIP1R cd17014
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 34-113 6.05e-04

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.


Pssm-ID: 340811  Cd Length: 114  Bit Score: 39.85  E-value: 6.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940  34 VAIVKATNHVESAPKERHIRRIFSATSvvqpRADVAYCIHALAKRLSKTRNWVVAIKVLIVIHRTLREGDPTFREELLNY 113
Cdd:cd17014   3 ISISKAINTQEAPVKEKHARRIILGTH----HEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRY 78
ANTH_N_HIP1 cd17013
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 34-113 7.04e-03

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.


Pssm-ID: 340810  Cd Length: 114  Bit Score: 36.94  E-value: 7.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328940  34 VAIVKATNHVESAPKERHIRRIFSATSvvqpRADVAYCIHALAKRLSKTRNWVVAIKVLIVIHRTLREGDPTFREELLNY 113
Cdd:cd17013   3 VSINKAINTQEVAVKEKHARTCILGTH----HEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRY 78
 
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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