8.A.142.1.1 PAT heterodimeric complex consisting of two proteins, coiled-coil domain-containing (CCDC) protein, (CDCC47) of 483 aas and 1 N-terminal TMS, and possibly another TMS towards the C-terminus, and Asterix of 106 aas and 2 TMSs. Together they form the PAT chaparone complex in the endoplasmic reticulum (ER) that helps to properly insert multispanning membrane proteins into the ER membranes of eukaryotes (Chitwood and Hegde 2020). It is involved in the regulation of calcium ion homeostasis in the ER (Morimoto et al. 2018) and is required for proper protein degradation via the ERAD pathway (Yamamoto et al. 2014). It plays an essential role in the maintenance of ER organization during embryogenesis. The PAT complex engages early TMSs of multipass proteins to promote their
biogenesis. The nascent chain is not engaged with Sec61, which is occluded and
latched closed by CCDC47. Instead, Asterix binds to and redirects the
substrate to a location behind Sec61, where the PAT complex contributes
to a multipass translocon surrounding a semi-enclosed, lipid-filled
cavity (SmalinskaitÄ— et al. 2022).
|
Accession Number: | Q96A33 |
Protein Name: | Coiled-coil domain-containing protein 47 |
Length: | 483 |
Molecular Weight: | 55874.00 |
Species: | Homo sapiens (Human) [9606] |
Number of TMSs: | 1 |
Location1 / Topology2 / Orientation3: |
Endoplasmic reticulum membrane1 |
Substrate |
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1: MKAFHTFCVV LLVFGSVSEA KFDDFEDEED IVEYDDNDFA EFEDVMEDSV TESPQRVIIT
61: EDDEDETTVE LEGQDENQEG DFEDADTQEG DTESEPYDDE EFEGYEDKPD TSSSKNKDPI
121: TIVDVPAHLQ NSWESYYLEI LMVTGLLAYI MNYIIGKNKN SRLAQAWFNT HRELLESNFT
181: LVGDDGTNKE ATSTGKLNQE NEHIYNLWCS GRVCCEGMLI QLRFLKRQDL LNVLARMMRP
241: VSDQVQIKVT MNDEDMDTYV FAVGTRKALV RLQKEMQDLS EFCSDKPKSG AKYGLPDSLA
301: ILSEMGEVTD GMMDTKMVHF LTHYADKIES VHFSDQFSGP KIMQEEGQPL KLPDTKRTLL
361: FTFNVPGSGN TYPKDMEALL PLMNMVIYSI DKAKKFRLNR EGKQKADKNR ARVEENFLKL
421: THVQRQEAAQ SRREEKKRAE KERIMNEEDP EKQRRLEEAA LRREQKKLEK KQMKMKQIKV
481: KAM