ID   SSRB_CANLF              Reviewed;         183 AA.
AC   P23438;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Translocon-associated protein subunit beta;
DE            Short=TRAP-beta;
DE   AltName: Full=Glycoprotein 25H;
DE            Short=gp25H;
DE   AltName: Full=Signal sequence receptor subunit beta;
DE            Short=SSR-beta;
DE   Flags: Precursor;
GN   Name=SSR2;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-50 AND 83-120.
RX   PubMed=2177473; DOI=10.1083/jcb.111.6.2283;
RA   Goerlich D., Prehn S., Hartmann E., Herz J., Otto A., Kraft R.,
RA   Wiedmann M., Knespel S., Dobberstein B., Rapoport T.A.;
RT   "The signal sequence receptor has a second subunit and is part of a
RT   translocation complex in the endoplasmic reticulum as probed by
RT   bifunctional reagents.";
RL   J. Cell Biol. 111:2283-2294(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-42; 59-106 AND
RP   140-162.
RC   TISSUE=Pancreas;
RX   PubMed=1918067; DOI=10.1016/s0021-9258(18)55036-5;
RA   Wada I., Rindress D., Cameron P.H., Ou W.-J., Doherty J.J. II, Louvard D.,
RA   Bell A.W., Dignard D., Thomas D.Y., Bergeron J.J.M.;
RT   "SSR alpha and associated calnexin are major calcium binding proteins of
RT   the endoplasmic reticulum membrane.";
RL   J. Biol. Chem. 266:19599-19610(1991).
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.
CC   -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC       gamma. Interacts with STING1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC       I membrane protein.
CC   -!- SIMILARITY: Belongs to the TRAP-beta family. {ECO:0000305}.
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; X53529; CAA37609.1; -; mRNA.
DR   EMBL; X53591; CAA37661.1; -; mRNA.
DR   PIR; A36679; A36679.
DR   RefSeq; NP_001003269.1; NM_001003269.2.
DR   AlphaFoldDB; P23438; -.
DR   CORUM; P23438; -.
DR   STRING; 9615.ENSCAFP00000024839; -.
DR   PaxDb; P23438; -.
DR   Ensembl; ENSCAFT00030000502; ENSCAFP00030000440; ENSCAFG00030000294.
DR   Ensembl; ENSCAFT00040039674; ENSCAFP00040034620; ENSCAFG00040021358.
DR   Ensembl; ENSCAFT00845018570; ENSCAFP00845014487; ENSCAFG00845010530.
DR   GeneID; 403950; -.
DR   KEGG; cfa:403950; -.
DR   CTD; 6746; -.
DR   VEuPathDB; HostDB:ENSCAFG00845010530; -.
DR   eggNOG; KOG3317; Eukaryota.
DR   GeneTree; ENSGT00390000005125; -.
DR   InParanoid; P23438; -.
DR   OrthoDB; 1286165at2759; -.
DR   Proteomes; UP000002254; Chromosome 7.
DR   Bgee; ENSCAFG00000016882; Expressed in saliva-secreting gland and 48 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   InterPro; IPR008856; TRAP_beta.
DR   PIRSF; PIRSF016400; TRAP_beta; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:1918067,
FT                   ECO:0000269|PubMed:2177473"
FT   CHAIN           18..183
FT                   /note="Translocon-associated protein subunit beta"
FT                   /id="PRO_0000033289"
FT   TOPO_DOM        18..149
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..183
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   183 AA;  20100 MW;  0D05C4AC2E72C72D CRC64;
     MRLLASVLLA LFAVSHAEEG ARLLASKSLL NRYAVEGRDL TLQYNIYNVG SSAALDVELS
     DDSFPPEDFG IVSGMLNVKW DRIAPASNVS HTVVLRPLKA GYFNFTSATV TYLAQEDGPV
     VIGFTSAPGQ GGILAQREFD RRFSPHFLDW AAFGVMTLPS IGIPLLLWYS SKRKYDTPKS
     KKN