Protein Domain : IPR002553

Type:  Domain Name:  Clathrin/coatomer adaptor, adaptin-like, N-terminal
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. This traffic is bidirectional, to ensure that proteins required to form vesicles are recycled. Vesicles have specific coat proteins (such as clathrin or coatomer) that are important for cargo selection and direction of transfer []. Clathrin coats contain both clathrin 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 []. All AP complexes are heterotetramers composed of two large subunits (adaptins), a medium subunit (mu) and a small subunit (sigma). Each subunit has a specific function. Adaptin subunits recognise and bind to clathrin through their hinge region (clathrin box), and recruit accessory proteins that modulate AP function through their C-terminal appendage domains. By contrast, GGAs are monomers composed of four domains, which have functions similar to AP subunits: an N-terminal VHS (Vps27p/Hrs/Stam) domain, a GAT (GGA and Tom1) domain, a hinge region, and a C-terminal GAE (gamma-adaptin ear) domain. The GAE domain is similar to the AP gamma-adaptin ear domain, being responsible for the recruitment of accessory proteins that regulate clathrin-mediated endocytosis [].While clathrin mediates endocytic protein transport from ER to Golgi, coatomers (COPI, COPII) primarily mediate intra-Golgi transport, as well as the reverse Golgi to ER transport of dilysine-tagged proteins []. Coatomers reversibly associate with Golgi (non-clathrin-coated) vesicles to mediate protein transport and for budding from Golgi membranes []. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunits. This entry represents the N-terminal domain of various adaptins from different AP clathrin adaptor complexes (including AP1, AP2, AP3 and AP4), and from the beta and gamma subunits of various coatomer (COP) adaptors. This domain has a 2-layer alpha/alpha fold that forms a right-handed superhelix, and is a member of the ARM repeat superfamily []. The N-terminal region of the various AP adaptor proteins share strong sequence identity; by contrast, the C-terminal domains of different adaptins share similar structural folds, but have little sequence identity []. It has been proposed that the N-terminal domain interacts with another uniform component of the coated vesicles. Short Name:  Clathrin/coatomer_adapt-like_N
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0 Child Features

0 Contains

1 Cross References

Identifier
PF01602

7 Found Ins

DB identifier Type Name
IPR017104 Family Adaptor protein complex AP-2, alpha subunit
IPR017106 Family Coatomer gamma subunit
IPR016460 Family Coatomer beta subunit (COPB1)
IPR016342 Family AP-1, 2,4 complex subunit beta
IPR017109 Family Adaptor protein complex AP-4, epsilon subunit
IPR017105 Family Adaptor protein complex AP-3, delta subunit
IPR017107 Family Adaptor protein complex AP-1, gamma subunit

3 GO Annotations

GO Term Gene Name
GO:0006886 IPR002553
GO:0016192 IPR002553
GO:0030117 IPR002553

3 Ontology Annotations

GO Term Gene Name
GO:0006886 IPR002553
GO:0016192 IPR002553
GO:0030117 IPR002553

1 Parent Features

DB identifier Type Name
IPR011989 Domain Armadillo-like helical

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
233268 D8S746 PAC:15421058 Selaginella moellendorffii 861  
230624 D8R188 PAC:15415405 Selaginella moellendorffii 997  
118138 D8SIN4 PAC:15406190 Selaginella moellendorffii 906  
422500 D8SIM6 PAC:15419381 Selaginella moellendorffii 433  
740 D8SIN0 PAC:15422224 Selaginella moellendorffii 602  
268757 D8SJW9 PAC:15416460 Selaginella moellendorffii 886  
168054 D8R5I2 PAC:15419184 Selaginella moellendorffii 846  
269184 D8SU50 PAC:15414966 Selaginella moellendorffii 871  
160340 D8T279 PAC:15420382 Selaginella moellendorffii 960  
867 D8QMJ2 PAC:15423027 Selaginella moellendorffii 612  
170737 D8REG2 PAC:15408209 Selaginella moellendorffii 922  
evm.TU.contig_32953.1 PAC:16430181 Carica papaya 881  
evm.model.supercontig_180.11 PAC:16411493 Carica papaya 413  
evm.model.supercontig_23.22 PAC:16414230 Carica papaya 526  
evm.model.supercontig_24.17 PAC:16414467 Carica papaya 598  
evm.model.supercontig_3.486 PAC:16416797 Carica papaya 969  
evm.model.supercontig_47.59 PAC:16420664 Carica papaya 958  
evm.model.supercontig_62.141 PAC:16423941 Carica papaya 544  
evm.model.supercontig_62.140 PAC:16423940 Carica papaya 279  
evm.model.supercontig_69.3 PAC:16424898 Carica papaya 388  
evm.model.supercontig_69.4 PAC:16424909 Carica papaya 410  
29747.m001105 B9SFZ1 PAC:16807771 Ricinus communis 848  
29785.m000969 B9SB76 PAC:16808515 Ricinus communis 903  
29827.m002653 B9S1S1 PAC:16810084 Ricinus communis 981  
29848.m004454 B9RNM4 PAC:16811111 Ricinus communis 819  
29883.m002039 B9S4M0 PAC:16812126 Ricinus communis 875  
29991.m000630 B9SN68 PAC:16815248 Ricinus communis 1018  
30190.m010889 B9RBE3 PAC:16823253 Ricinus communis 887  
27383.m000162 B9T4I4 PAC:16798183 Ricinus communis 1121  
Cucsa.385480.1 PAC:16982576 Cucumis sativus 1019  

7 Publications

First Author Title Year Journal Volume Pages PubMed ID
            12858162
            14690497
            15261670
            17041781
            17449236
            2495531
            12086608