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Database: UniProt
Entry: A8WWG0_CAEBR
LinkDB: A8WWG0_CAEBR
Original site: A8WWG0_CAEBR 
ID   A8WWG0_CAEBR            Unreviewed;       257 AA.
AC   A8WWG0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 83.
DE   RecName: Full=Translocon-associated protein subunit alpha {ECO:0000256|ARBA:ARBA00020280};
DE   AltName: Full=Signal sequence receptor subunit alpha {ECO:0000256|ARBA:ARBA00031071};
GN   Name=trap-1 {ECO:0000313|WormBase:CBG04219};
GN   Synonyms=Cbr-trap-1 {ECO:0000313|EMBL:CAP24969.1};
GN   ORFNames=CBG04219 {ECO:0000313|WormBase:CBG04219}, CBG_04219
GN   {ECO:0000313|EMBL:CAP24969.1};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP24969.1, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP24969.1, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP24969.1,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: TRAP proteins are part of a complex whose function is to bind
CC       calcium to the ER membrane and thereby regulate the retention of ER
CC       resident proteins. May be involved in the recycling of the
CC       translocation apparatus after completion of the translocation process
CC       or may function as a membrane-bound chaperone facilitating folding of
CC       translocated proteins. {ECO:0000256|ARBA:ARBA00025620}.
CC   -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC       gamma. Interacts with palmitoylated calnexin (CALX), the interaction is
CC       required for efficient folding of glycosylated proteins.
CC       {ECO:0000256|ARBA:ARBA00025854}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004115}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the TRAP-alpha family.
CC       {ECO:0000256|ARBA:ARBA00006776}.
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DR   EMBL; HE600926; CAP24969.1; -; Genomic_DNA.
DR   RefSeq; XP_002639582.1; XM_002639536.1.
DR   AlphaFoldDB; A8WWG0; -.
DR   STRING; 6238.A8WWG0; -.
DR   EnsemblMetazoa; CBG04219.1; CBG04219.1; WBGene00026938.
DR   GeneID; 8581575; -.
DR   KEGG; cbr:CBG_04219; -.
DR   CTD; 8581575; -.
DR   WormBase; CBG04219; CBP00993; WBGene00026938; Cbr-trap-1.
DR   eggNOG; KOG1631; Eukaryota.
DR   HOGENOM; CLU_073618_2_0_1; -.
DR   InParanoid; A8WWG0; -.
DR   OMA; EWIPRDA; -.
DR   OrthoDB; 5403315at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR005595; TRAP_alpha.
DR   PANTHER; PTHR12924:SF0; TRANSLOCON-ASSOCIATED PROTEIN SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR12924; TRANSLOCON-ASSOCIATED PROTEIN, ALPHA SUBUNIT; 1.
DR   Pfam; PF03896; TRAP_alpha; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..257
FT                   /note="Translocon-associated protein subunit alpha"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005661227"
FT   TRANSMEM        180..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          235..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   257 AA;  28650 MW;  C9AA18262FD4A385 CRC64;
     MKLTSILLLT VLGFCAVYAA DVVDGEVTDD APKANLEEDD LTIGASPDAE LAFHFVQPAD
     ANVLHEFYTG KPVKFLIGFQ NKGEKDFVVK YSETSFRFPT DYNYHLQNFT RGEYNRRVSP
     KEEVTLDYGF YAHETFAGRP VGLVVNIHYQ DADGNVFVNN VFNQTVNILE DDSGFSGETG
     FLFIFFVALS IGGLYLANQF LSKLSRKSGL SKRRVVEQGT SSEVDFEWIP RDAVKNKEKK
     SPVAGSPKAR KSAKKAE
//
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