ID   SSRA_RAT                Reviewed;         319 AA.
AC   Q7TPJ0;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Translocon-associated protein subunit alpha;
DE            Short=TRAP-alpha;
DE   AltName: Full=Liver regeneration-related protein LRRG137;
DE   AltName: Full=Signal sequence receptor subunit alpha;
DE            Short=SSR-alpha;
DE   Flags: Precursor;
GN   Name=Ssr1; ORFNames=Ac2-238;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RA   Xu C.S., Li W.Q., Li Y.C., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J.,
RA   Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., Han H.P.,
RA   Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT   "Liver regeneration after PH.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: Seems to bind calcium. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAP-alpha family. {ECO:0000305}.
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DR   EMBL; AY321345; AAP86277.1; -; mRNA.
DR   AlphaFoldDB; Q7TPJ0; -.
DR   IntAct; Q7TPJ0; 1.
DR   STRING; 10116.ENSRNOP00000019040; -.
DR   GlyGen; Q7TPJ0; 2 sites.
DR   jPOST; Q7TPJ0; -.
DR   PRIDE; Q7TPJ0; -.
DR   Ensembl; ENSRNOT00000089736; ENSRNOP00000070167; ENSRNOG00000014165.
DR   UCSC; RGD:1310961; rat.
DR   RGD; 1310961; Ssr1.
DR   eggNOG; KOG1631; Eukaryota.
DR   GeneTree; ENSGT00400000022103; -.
DR   InParanoid; Q7TPJ0; -.
DR   PhylomeDB; Q7TPJ0; -.
DR   TreeFam; TF321074; -.
DR   PRO; PR:Q7TPJ0; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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; IPR005595; TRAP_alpha.
DR   Pfam; PF03896; TRAP_alpha; 1.
PE   1: Evidence at protein level;
KW   Calcium; Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..319
FT                   /note="Translocon-associated protein subunit alpha"
FT                   /id="PRO_0000033285"
FT   TOPO_DOM        22..208
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..319
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          35..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..78
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43307"
FT   MOD_RES         261
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P43307"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   319 AA;  35629 MW;  F9194C23FAB14740 CRC64;
     MRLLPRLLLL FLLAFPAAVL LRGGPGGSLA VAQDLTEDEE TVEDPIIEDE DDEAEVEEDE
     PTDLAEEKEE EEDVSSEPEA SPSADTTILF VKGEDFPANN IVKFLVGFTN KGTEDFIVES
     LDASFRYPQD YQFYIQNFTA LPLNTIVPPQ RQATFEYSFI PAEPMGGRPF GLVINLNYKD
     LNGNVFQDAV FNQTVTVIER EDGLDGETIF MYMFLAGLGL LVVVGLHQLL ESRKRKRPIQ
     KVEMGTSSQN DVDMSWIPQE TLNQISAGRE RHTEVTLQLH RPVVSDASYA CFSCFRKLPR
     PATLAAWTSS LRQLAVCGI