ID   CCD47_PONAB             Reviewed;         483 AA.
AC   Q5RCI4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Coiled-coil domain-containing protein 47;
DE   Flags: Precursor;
GN   Name=CCDC47;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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   -!- SEQUENCE CAUTION:
CC       Sequence=CAH90523.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CR858286; CAH90523.1; ALT_FRAME; mRNA.
DR   AlphaFoldDB; Q5RCI4; -.
DR   SMR; Q5RCI4; -.
DR   STRING; 9601.ENSPPYP00000009581; -.
DR   eggNOG; KOG2357; Eukaryota.
DR   InParanoid; Q5RCI4; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0036503; P:ERAD pathway; 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="Coiled-coil domain-containing protein 47"
FT                   /id="PRO_0000235800"
FT   TRANSMEM        136..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          46..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          451..481
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;  55874 MW;  AF3AFFCC6382164C CRC64;
     MKAFHTFCVV LLVFGSVSEA KFDDFEDEED IVEYDDNDFA EFEDVMEDSV TESPQRVIIT
     EDDEDETTVE LEGQDENQEG DFEDADTQEG DTESEPYDDE EFEGYEDKPD TSSSKNKDPI
     TIVDVPAHLQ NSWESYYLEI LMVTGLLAYI MNYIIGKNKN SRLAQAWFNT HRELLESNFT
     LVGDDGTNKE ATSTGKLNQE NEHIYNLWCS GRVCCEGMLI QLRFLKRQDL LNVLARMMRP
     VSDQVQIKVT MNDEDMETYV FAVGTRKALV RLQKEMQDLS EFCSDKPKSG AKYGLPDSLA
     ILSEMGEVTD GMMDTKMVHF LTHYADKIES VHFSDQFSGP KIMQEEGQPL KLPDTKRTLL
     FTFNVPGSGN TYPKDMEALL PLMNMVIYSI DKAKKFRLNR EGKQKADKNR ARVEENFLKL
     THVQRQEAAQ SRREEKKRAE KERIMNEEDP EKQRRLEEAA LRRDQKKLEK KQMKMKQIKV
     KAM