Protein Domain : IPR003164

Type:  Domain Name:  Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain
Description:  Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins (such as clathrin or coatomer) that are important for cargo selection and direction of transport []. Clathrin coats contain both clathrin (acts as a scaffold) and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The two major types of clathrin adaptor complexes are the heterotetrameric adaptor protein (AP) complexes, and the monomeric GGA (Golgi-localising, Gamma-adaptin ear domain homology, ARF-binding proteins) adaptors [, ].AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and lipids to clathrin at vesicle budding sites, as well as binding accessory proteins that regulate coat assembly and disassembly (such as AP180, epsins and auxilin). There are different AP complexes in mammals. AP1 is responsible for the transport of lysosomal hydrolases between the TGN and endosomes []. AP2 associates with the plasma membrane and is responsible for endocytosis []. AP3 is responsible for protein trafficking to lysosomes and other related organelles []. AP4 is less well characterised. AP complexes are heterotetramers composed of two large subunits (adaptins), a medium subunit (mu) and a small subunit (sigma). For example, in AP1 these subunits are gamma-1-adaptin, beta-1-adaptin, mu-1 and sigma-1, while in AP2 they are alpha-adaptin, beta-2-adaptin, mu-2 and sigma-2. Each subunit has a specific function. Adaptins recognise and bind to clathrin through their hinge region (clathrin box), and recruit accessory proteins that modulate AP function through their C-terminal ear (appendage) domains. Mu recognises tyrosine-based sorting signals within the cytoplasmic domains of transmembrane cargo proteins []. One function of clathrin and AP2 complex-mediated endocytosis is to regulate the number of GABA(A) receptors available at the cell surface []. AP adaptor alpha-adaptin can be divided into a trunk domain and the C-terminal appendage domain (or ear domain), separated by a linker region. The C-terminal appendage domain regulates translocation of endocytic accessory proteins to the bud site [].This entry represents a subdomain of the appendage (ear) domain of alpha-adaptin from AP clathrin adaptor complexes. This domain has a three-layer arrangement, alpha-beta-alpha, with a bifurcated antiparallel beta-sheet []. Short Name:  Clathrin_a-adaptin_app_sub_C

0 Child Features

0 Contains

1 Cross References

Identifier
PF02296

1 Found In

DB identifier Type Name
IPR017104 Family Adaptor protein complex AP-2, alpha subunit

3 GO Annotations

GO Term Gene Name
GO:0006886 IPR003164
GO:0016192 IPR003164
GO:0030131 IPR003164

3 Ontology Annotations

GO Term Gene Name
GO:0006886 IPR003164
GO:0016192 IPR003164
GO:0030131 IPR003164

1 Parent Features

DB identifier Type Name
IPR015873 Domain Clathrin alpha-adaptin/coatomer adaptor, appendage, C-terminal subdomain

682 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
233268 D8S746 PAC:15421058 Selaginella moellendorffii 861  
230624 D8R188 PAC:15415405 Selaginella moellendorffii 997  
evm.model.supercontig_47.59 PAC:16420664 Carica papaya 958  
29991.m000630 B9SN68 PAC:16815248 Ricinus communis 1018  
Cucsa.385480.1 PAC:16982576 Cucumis sativus 1019  
orange1.1g001845m A0A067DS13 PAC:18099867 Citrus sinensis 1006  
AT5G22770.1 Q8LPL6 PAC:19666783 Arabidopsis thaliana 1012  
AT5G22770.2 Q8LPL6 PAC:19666784 Arabidopsis thaliana 1012  
AT5G22770.3 Q8LPL6 PAC:19666785 Arabidopsis thaliana 1012  
AT5G22780.1 Q8LPK4 PAC:19672998 Arabidopsis thaliana 1013  
Thhalv10012556m V4LET6 PAC:20206102 Eutrema salsugineum 1012  
Thhalv10012557m V4LQV3 PAC:20206103 Eutrema salsugineum 1011  
Ciclev10027737m V4SKJ1 PAC:20813496 Citrus clementina 1014  
Lus10005371 PAC:23148515 Linum usitatissimum 1018  
Lus10043363 PAC:23168291 Linum usitatissimum 1020  
Lus10020522 PAC:23172283 Linum usitatissimum 1021  
Lus10019520 PAC:23181546 Linum usitatissimum 1023  
Potri.009G150300.2 PAC:26985791 Populus trichocarpa 946  
Potri.009G150300.1 B9HQK6 PAC:26985788 Populus trichocarpa 1018  
Potri.009G150300.5 PAC:26985792 Populus trichocarpa 735  
Potri.009G150300.4 PAC:26985790 Populus trichocarpa 952  
Potri.004G189700.2 A0A2K2AWX1 PAC:26991579 Populus trichocarpa 1014  
Potri.004G189700.1 A0A2K2AWX0 PAC:26991578 Populus trichocarpa 1015  
Gorai.004G008000.1 A0A0D2RRC7 PAC:26776072 Gossypium raimondii 1019  
Gorai.006G108500.2 A0A0D2RTQ9 PAC:26832254 Gossypium raimondii 1022  
Gorai.006G108500.1 A0A0D2RTQ9 PAC:26832255 Gossypium raimondii 1022  
Gorai.006G108500.3 A0A0D2SVC0 PAC:26832256 Gossypium raimondii 1001  
52285 I0Z6J0 PAC:27393399 Coccomyxa subellipsoidea C-169 1023  
194640 C1MZK0 PAC:27344166 Micromonas pusilla CCMP1545 1107  
104856 C1E889 PAC:27401989 Micromonas sp RCC299 1016  

10 Publications

First Author Title Year Journal Volume Pages PubMed ID
            15261670
            17449236
            11598180
            11080148
            15107467
            12952931
            16542748
            17254016
            12057195
            10430869