Summary: Trafficking protein particle complex subunit 10, TRAPPC10
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Trafficking protein particle complex subunit 10, TRAPPC10 Provide feedback
This domain forms part of the TRAPP complex for mediating vesicle docking and fusion in the Golgi apparatus. The fungal version is referred to as Trs130, and an alternative vertebrate alias is TMEM1 [1,2].
Sacher M, Jiang Y, Barrowman J, Scarpa A, Burston J, Zhang L, Schieltz D, Yates JR 3rd, Abeliovich H, Ferro-Novick S; , EMBO J 1998;17:2494-2503.: TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion. PUBMED:9564032 EPMC:9564032
Sacher M, Barrowman J, Wang W, Horecka J, Zhang Y, Pypaert M, Ferro-Novick S;, Mol Cell. 2001;7:433-442.: TRAPP I implicated in the specificity of tethering in ER-to-Golgi transport. PUBMED:11239471 EPMC:11239471
Internal database links
|Similarity to PfamA using HHSearch:||Gryzun Gryzun-like|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR022233
The trafficking protein particle complex TRAPP is a multi-protein complex needed in the early stages of the secretory pathway. To date, two kinds of TRAPP complexes have been studied, TRAPPI and TRAPP II. These complexes differ in subunit composition [PUBMED:11239471]. TRAPP I binds vesicles derived from the endoplasmic reticulum bringing them closer to the acceptor membrane.
This entry represents a domain which forms part of the TRAPP complex for mediating vesicle docking and fusion in the Golgi apparatus. The fungal version is referred to as Trs130, and an alternative vertebrate alias is TMEM1 [PUBMED:9564032, PUBMED:11239471].
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Curation and family details
|Number in seed:||32|
|Number in full:||265|
|Average length of the domain:||163.40 aa|
|Average identity of full alignment:||21 %|
|Average coverage of the sequence by the domain:||14.07 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||3|
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