CCD47_MACFA
ID CCD47_MACFA Reviewed; 483 AA.
AC P0C204;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=PAT complex subunit CCDC47 {ECO:0000250|UniProtKB:Q96A33};
DE AltName: Full=Coiled-coil domain-containing protein 47;
DE Flags: Precursor;
GN Name=CCDC47; ORFNames=QtrA-15751;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the PAT complex, an endoplasmic reticulum (ER)-
CC resident membrane multiprotein complex that facilitates multi-pass
CC membrane proteins insertion into membranes. The PAT complex acts as an
CC intramembrane chaperone by directly interacting with nascent
CC transmembrane domains (TMDs), releasing its substrates upon correct
CC folding, and is needed for optimal biogenesis of multi-pass membrane
CC proteins. WDR83OS/Asterix is the substrate-interacting subunit of the
CC PAT complex, whereas CCDC47 is required to maintain the stability of
CC WDR83OS/Asterix. The PAT complex favors the binding to TMDs with
CC exposed hydrophilic amino acids within the lipid bilayer and provides a
CC membrane-embedded partially hydrophilic environment in which the first
CC transmembrane domain binds. Component of a ribosome-associated ER
CC translocon complex involved in multi-pass membrane protein transport
CC into the ER membrane and biogenesis. Involved in the regulation of
CC calcium ion homeostasis in the ER. Required for proper protein
CC degradation via the ERAD (ER-associated degradation) pathway (By
CC similarity). Has an essential role in the maintenance of ER
CC organization during embryogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q96A33, ECO:0000250|UniProtKB:Q9D024}.
CC -!- SUBUNIT: The PAT complex includes WDR83OS/Asterix and CCDC47. The
CC ribosome-associated ER translocon complex includes SEC61A1, SEC61B,
CC SEC61G, TMCO1, CCDC47, NCLN/Nicalin, NOMO and TMEM147; in the absence
CC of ribosomes, only the complex forms with NCLN/Nicalin, NOMO and
CC TMEM147 remains intact (By similarity). Interacts with VCP, HSPA5,
CC DERL1, DERL2 and SELENOS (By similarity).
CC {ECO:0000250|UniProtKB:Q96A33, ECO:0000250|UniProtKB:Q9D024}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96A33}; Single-pass membrane protein
CC {ECO:0000305}. Rough endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9D024}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB174266; BAE91328.1; -; mRNA.
DR AlphaFoldDB; P0C204; -.
DR SMR; P0C204; -.
DR STRING; 9541.XP_005584723.1; -.
DR PRIDE; P0C204; -.
DR eggNOG; KOG2357; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0044183; F:protein folding chaperone; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR GO; GO:0045048; P:protein insertion into ER membrane; ISS:UniProtKB.
DR InterPro; IPR012879; CCDC47.
DR PANTHER; PTHR12883; PTHR12883; 1.
DR Pfam; PF07946; DUF1682; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..483
FT /note="PAT complex subunit CCDC47"
FT /id="PRO_0000235798"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 46..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..483
FT /evidence="ECO:0000255"
FT COMPBIAS 63..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 483 AA; 55802 MW; 8A2A71138E100968 CRC64;
MKAFHTFCVV LLVFGSVSEA KFDDFEDEED IVEYDDNDFA EFEDVMEDSV TESPQRVITT
EDDEDETTVE LEGQDENQEG DFEDADTQEG DTESEPYDDE EFEGYEDKPD TSSSKNKDPI
TIVDVPAHLQ NSWESYYLEI LMVTGLLAYI MNYIIGKNKN SRLAQAWFNT HRELLESNFT
LVGDDGTNKE ATSTGKLNQE NEHIYNLWCS GRVCCEGMLI QLRFLKRQDL LNVLARMMRP
VSDQVQIKVT MNDEDMDTYV FAVGTRKALV RLQKEMQDLS EFCSDKPKSG AKYGLPDSLA
ILSEMGEVTD GMMDTKMVHF LTHYADKIES VHFSDQSSGP KIMQEEGQPL KLPDTKRTLL
FTFNVPGSGN TYPKDMEALL PLMNMVIYSI DKAKKFRLNR EGKQKADKNR ARVEENFLKL
THVQRQEAAQ SRREEKKRAE KERIMNEEDP EKQRRLEEAA LRREQKKLEK KQMKMKQIKV
KAM
