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Protein Domain : IPR013041

Name  Coatomer/clathrin adaptor appendage, Ig-like subdomain Short Name  Coatomer/clathrin_app_Ig-like
Type  Domain 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 a beta-sandwich structural motif found in the appendage (ear) domain of alpha-, beta- and gamma-adaptin from AP clathrin adaptor complexes, the GAE (gamma-adaptin ear) domain of GGA adaptor proteins, and the appendage domain of the gamma subunit of coatomer complexes. These domains have an immunoglobulin-like beta-sandwich fold containing 7 or 8 strands in 2 beta-sheets in a Greek key topology [, , ]. Although the appendage domains from AP / GGA adaptins and coatomers share a similar fold, there is little sequence identity between them. However, they also share similar motif-based cargo recognition and accessory factor recruitment mechanisms. More information about these proteins can be found at Protein of the Month: Clathrin [].

Publication Counts Displayer

4 Child Features

DB identifier Name Short Name Type
IPR008153 Clathrin adaptor, gamma-adaptin, appendage Clathrin_g-adaptin_app Domain
IPR013038 Clathrin adaptor, alpha-adaptin, appendage, Ig-like subdomain Clathrin_a-adaptin_app_Ig-like Domain
IPR013040 Coatomer, gamma subunit, appendage, Ig-like subdomain Coatomer_gsu_app_Ig-like-sub Domain
IPR013037 Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain Clathrin_b-adaptin_app_Ig-like Domain

0 Contains

1 Cross References

Identifier
Source . Name

Subject . Primary Identifier
SSF49348 SSF IPR013041

2 Data Sets

Name URL
TrEMBL data set http://www.ebi.ac.uk/trembl/
InterPro data set  

0 Found In

0 GO Annotation

0 Ontology Annotations

0 Parent Features

62 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0085155 Q8I0G5 Drosophila melanogaster
FBpp0074558 Q24253 Drosophila melanogaster
FBpp0088945 E8NH12 Drosophila melanogaster
FBpp0088490 P91926 Drosophila melanogaster
FBpp0071298 Q9W329 Drosophila melanogaster
FBpp0301194 Q86B59 Drosophila melanogaster
FBpp0071231 Q9W388 Drosophila melanogaster
FBpp0071230 Q7KVR7 Drosophila melanogaster
FBpp0071232 Q7KVR8 Drosophila melanogaster
FBpp0272566 Q29H04 Drosophila pseudoobscura
FBpp0280380 Q29N38 Drosophila pseudoobscura
FBpp0280960 B5DN54 Drosophila pseudoobscura
FBpp0297038 I5ANE0 Drosophila pseudoobscura
FBpp0282417 Q29AE5 Drosophila pseudoobscura
FBpp0282999 Q29HG8 Drosophila pseudoobscura
FBpp0164020 B4L4S8 Drosophila mojavensis
FBpp0164750 B4L3F0 Drosophila mojavensis
FBpp0165315 B4L6V2 Drosophila mojavensis
FBpp0167254 B4KFJ2 Drosophila mojavensis
FBpp0172613 B4K7Z2 Drosophila mojavensis
FBpp0229295 B4MET3 Drosophila virilis
FBpp0230163 B4MA28 Drosophila virilis
FBpp0233885 B4M2D2 Drosophila virilis
FBpp0234164 B4LTK9 Drosophila virilis
FBpp0237503 B4M106 Drosophila virilis
FBpp0255956 B4PNE7 Drosophila yakuba
FBpp0260830 B4PZX8 Drosophila yakuba
FBpp0260880 B4PZ07 Drosophila yakuba
FBpp0261149 B4P2D9 Drosophila yakuba
FBpp0262810 B4PWX6 Drosophila yakuba