CCD47_BOVIN
ID CCD47_BOVIN Reviewed; 483 AA.
AC Q3ZC50; A5D9E2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Rumen;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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}.
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DR EMBL; BT030561; ABQ13001.1; -; mRNA.
DR EMBL; BC102915; AAI02916.1; -; mRNA.
DR RefSeq; NP_001030505.1; NM_001035428.1.
DR AlphaFoldDB; Q3ZC50; -.
DR SMR; Q3ZC50; -.
DR PRIDE; Q3ZC50; -.
DR Ensembl; ENSBTAT00000075749; ENSBTAP00000058460; ENSBTAG00000011834.
DR Ensembl; ENSBTAT00000082660; ENSBTAP00000060375; ENSBTAG00000011834.
DR GeneID; 540167; -.
DR KEGG; bta:540167; -.
DR CTD; 57003; -.
DR VEuPathDB; HostDB:ENSBTAG00000011834; -.
DR VGNC; VGNC:97247; CCDC47.
DR GeneTree; ENSGT00390000013997; -.
DR InParanoid; Q3ZC50; -.
DR OMA; PPIDQKV; -.
DR OrthoDB; 1337297at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000011834; Expressed in saliva-secreting gland and 108 other tissues.
DR ExpressionAtlas; Q3ZC50; baseline.
DR GO; GO:0101031; C:chaperone complex; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
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:0006983; P:ER overload response; IEA:Ensembl.
DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0045048; P:protein insertion into ER membrane; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
DR InterPro; IPR012879; CCDC47.
DR PANTHER; PTHR12883; PTHR12883; 1.
DR Pfam; PF07946; DUF1682; 1.
PE 2: Evidence at transcript level;
KW Chaperone; 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_0000235796"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 44..118
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; 55742 MW; E7AC14D738117483 CRC64;
MKGFHAFCVI LLIFGSVSEA KFDDFEDEED IVEYDDNDFA EFEDVAEDSV TESPQRVIIT
EDDEDETTVE LEGQDESQEG DFEDADTQEG DTESEPYDDE EFEGYEDKPD TSSSKSKDPI
TIVDVPAHLQ NSWESYYLEI LMVTGLLAYI MNYIIGKNKN SRLAQAWFNT HRELLESNFT
LVGDDGTNKE ATSTGKLNQE NEHIYNLWCS GRVCCEGMLI QLRFLKRQDL LNVLARMMRP
VSDQVQIKVT MNDEDMDTYV FAVGARKALV RLQKEMQDLS EFCSDKPKSG AKYGLPDSLA
ILSEMGEVTD GMMDTKMLHF LTHYADKIES IHFSDQFSGP KIMQEEGQPL KLPDTKRTLL
FTFNVPGSGN TYPKDMEALL PLMNMVIYSI DKAKKFRLNR EGKQKADKNR ARVEENFLKL
THVQRQEAAQ SRREEKKRAE KERIMNEEDP EKQRRLEEAA LRREQKKLEK KQMKMKQIKV
KAM
