ID   SSRB_CAEEL              Reviewed;         188 AA.
AC   Q22169;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Translocon-associated protein subunit beta;
DE   Flags: Precursor;
GN   Name=trap-2 {ECO:0000312|WormBase:T04G9.5}; ORFNames=T04G9.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA   Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT   "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT   elegans.";
RL   Glycobiology 15:952-964(2005).
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. {ECO:0000250|UniProtKB:P43308}.
CC   -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC       gamma. {ECO:0000250|UniProtKB:P43308}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P43308}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P43308}.
CC   -!- SIMILARITY: Belongs to the TRAP-beta family. {ECO:0000255}.
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; FO080299; CCD62717.1; -; Genomic_DNA.
DR   PIR; G89450; G89450.
DR   RefSeq; NP_508150.1; NM_075749.5.
DR   AlphaFoldDB; Q22169; -.
DR   BioGRID; 45375; 7.
DR   STRING; 6239.T04G9.5; -.
DR   iPTMnet; Q22169; -.
DR   EPD; Q22169; -.
DR   PaxDb; Q22169; -.
DR   PeptideAtlas; Q22169; -.
DR   EnsemblMetazoa; T04G9.5.1; T04G9.5.1; WBGene00020216.
DR   GeneID; 180422; -.
DR   KEGG; cel:CELE_T04G9.5; -.
DR   UCSC; T04G9.5.1; c. elegans.
DR   CTD; 180422; -.
DR   WormBase; T04G9.5; CE04886; WBGene00020216; trap-2.
DR   eggNOG; KOG3317; Eukaryota.
DR   GeneTree; ENSGT00390000005125; -.
DR   HOGENOM; CLU_102025_1_0_1; -.
DR   InParanoid; Q22169; -.
DR   OMA; ILWHSSK; -.
DR   OrthoDB; 1286165at2759; -.
DR   PhylomeDB; Q22169; -.
DR   PRO; PR:Q22169; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00020216; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008856; TRAP_beta.
DR   PIRSF; PIRSF016400; TRAP_beta; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..188
FT                   /note="Translocon-associated protein subunit beta"
FT                   /id="PRO_0000391386"
FT   TOPO_DOM        16..151
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   188 AA;  21563 MW;  45BAA2ADE7A22CE8 CRC64;
     MKFSLFALLF VVVSCVDVGT QTRDAFILAH KQPLSTYAVE NMDFVLEYGL YNVGDKPAQK
     VTIDDRHSFP TNSFDIVKGL LFVHFEQIPA GSNVTHSVVI RPRAFGFFNY TAAQVTYYTD
     NENHHVTLTN TPGEGYIYRQ REYDRRFAPK YTYFLVFFLI VAPTTLGSFL LFQQSKARFP
     NVIKKKST