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CCD47_XENLA
ID   CCD47_XENLA             Reviewed;         489 AA.
AC   Q6AZI2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Necessary for the biogenesis, correct folding and transport
CC       of multi-pass membrane proteins into the endoplasmic reticulum (ER)
CC       membrane. Involved in the regulation of calcium ion homeostasis in the
CC       ER. Required for proper protein degradation via the ERAD (ER-associated
CC       degradation) pathway. {ECO:0000250|UniProtKB:Q96A33}.
CC   -!- SUBUNIT: Heteromeric complex composed of WDR83OS/Asterix and CCDC47.
CC       Component of the ribosome-associated ER translocon complex.
CC       {ECO:0000250|UniProtKB:Q96A33}.
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; BC077957; AAH77957.1; -; mRNA.
DR   RefSeq; NP_001087058.1; NM_001093589.1.
DR   AlphaFoldDB; Q6AZI2; -.
DR   SMR; Q6AZI2; -.
DR   MaxQB; Q6AZI2; -.
DR   DNASU; 446893; -.
DR   GeneID; 446893; -.
DR   KEGG; xla:446893; -.
DR   CTD; 446893; -.
DR   Xenbase; XB-GENE-6255087; ccdc47.S.
DR   OrthoDB; 1337297at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 446893; Expressed in egg cell and 19 other tissues.
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; IEA:InterPro.
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; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..489
FT                   /note="PAT complex subunit CCDC47"
FT                   /id="PRO_0000235803"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          33..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          428..489
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        62..103
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  56421 MW;  3D1E7BF2E0F58B72 CRC64;
     MILFTRLLAV SLLLVSGAFA KFQEFDDSDD VAEYDDNDFA EFEDAADEAP TLRPPSQQVP
     EKEDEIEDDD EEEEEATVEL EGQEEFEEDT EGQEGDADAE PYDDEEFENY DDRLDTGTPN
     KNNDPITIVD VPAHLQNSWE SYYMEILMVT GLLAYIMNYI IGKNKNSRLA QAWFNSHREL
     LESNFSLVGD DGMNKDAVST GMLNQENDHI YNMWCSGRLC CEGMLIQLKF IKRQDLLNVL
     SRMMRPVCDQ VQIKVTMNDE DMDTYVFSVG TRKTLIRLQK EMQDLSEFCG DKPKSAAKMG
     LPESMAVLAE MGEVTDGIMD TKMVHYLTNY SDKIESIHFS DQFSGPKIMQ EEGQPLKLPE
     TKKTLLFTFN VPGSGNASVK DMEALLPLMN MVIYSIDKVK KFRLNREGKQ KADKNRARVE
     ENFLKITHVQ RQEAAQTRRE EKKRAEKERI MNEEDPEKQR RLEEAAQRRE QKKIEKKQMK
     MKQIKVKAM
 
 
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