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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400827  31 LEVAIVKATSHDDDPASEKYIREILNLTSLSRGYILACVTSVSRRLSKTRDWVVALKALMLVHRLLNEGDPIFQEEILYS 110
Cdd:cd16987   1 LEVAVVKATSHDDAPPDEKYVREILSLGSSSRAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGSPILEQELSLA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18400827 111 TRRGTRMLNMSDFRDEAHSSSWDHSAFVRTYAGYLDQRLELA 152
Cdd:cd16987  81 PSGGRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 122

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400827  31 LEVAIVKATSHDDDPASEKYIREILNLTSLSRGYILACVTSVSRRLSKTRDWVVALKALMLVHRLLNEGDPIFQEEILYS 110
Cdd:cd16987   1 LEVAVVKATSHDDAPPDEKYVREILSLGSSSRAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGSPILEQELSLA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18400827 111 TRRGTRMLNMSDFRDEAHSSSWDHSAFVRTYAGYLDQRLELA 152
Cdd:cd16987  81 PSGGRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 122

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400827  31 LEVAIVKATSHDDDPASEKYIREILNLTSLSRGY--ILACVTSVSRRLSKtRDWVVALKALMLVHRLLNEGDPIFQEEIL 108
Cdd:cd03564   1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNGGGRadVAYIVHALAKRLHK-KNWIVVLKTLIVIHRLLREGSPSFLEELL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18400827 109 ystRRGTRMLNMSDFRDEAHSSSWDHSAFVRTYAGYLDQRLE 150
Cdd:cd03564  80 ---RYSGHIFNLSNFKDDSSPEAWDLSAFIRRYARYLEERLE 118

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400827  34 AIVKATSHDDDPASEKYIREILNLTSLSRGYILACVTSVSRRlSKTRDWVVALKALMLVHRLLNEGDPIFqeeILYSTRR 113
Cdd:cd16985   4 AVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFER-TQNSSWVVVFKALITTHHLMVYGNERF---IQYLASR 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 18400827 114 GTRMlNMSDFRDEAHSSSWDHSAFVRTYAGYLDQRL 149
Cdd:cd16985  80 NSLF-NLSNFLDKSGSQGYDMSTFIRRYAKYLNEKA 114

Epsin N-Terminal Homology (ENTH)-like domain of AP-4 complex accessory subunit Tepsin and similar domains; This family is composed of proteins containing an ENTH-like domain including vertebrate AP-4 complex accessory subunit Tepsin and Arabidopsis thaliana VHS domain-containing protein At3g16270. Tepsin is also called ENTH Domain-containing protein 2 (ENTHD2), Epsin for AP-4, or Tetra-epsin. It associates with the adapter-like complex 4 (AP-4), a heterotetramer composed of two large adaptins (epsilon and beta), a medium adaptin (mu) and a small adaptin (sigma), which forms a non-clathrin coat on vesicles departing the Trans-Golgi Network. The Epsin N-Terminal Homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18400827  37 KATSHDDDPASeKYI-REILNLTSLSRGYILACVTSVSRRLSKTrDWVVALKALMLVHRLLNEGDPIFQEEI 107
Cdd:cd03572   7 KATSDDDEPTP-GYLlEEIAKLTRSSPGSCQELLDYLLKRLKKS-SPHVKLKALRIIKHLCQKGSPEFRREL 76