ID   SSRA_BOVIN              Reviewed;         286 AA.
AC   A6QLP7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Translocon-associated protein subunit alpha;
DE            Short=TRAP-alpha;
DE   AltName: Full=Signal sequence receptor subunit alpha;
DE            Short=SSR-alpha;
DE   Flags: Precursor;
GN   Name=SSR1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- DOMAIN: Shows a remarkable charge distribution with the N-terminus
CC       being highly negatively charged, and the cytoplasmic C-terminus
CC       positively charged.
CC   -!- PTM: Phosphorylated in its cytoplasmic tail. {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; BC148041; AAI48042.1; -; mRNA.
DR   RefSeq; NP_001095592.1; NM_001102122.2.
DR   AlphaFoldDB; A6QLP7; -.
DR   STRING; 9913.ENSBTAP00000008253; -.
DR   PaxDb; A6QLP7; -.
DR   PeptideAtlas; A6QLP7; -.
DR   PRIDE; A6QLP7; -.
DR   Ensembl; ENSBTAT00000008253; ENSBTAP00000008253; ENSBTAG00000022731.
DR   GeneID; 529312; -.
DR   KEGG; bta:529312; -.
DR   CTD; 6745; -.
DR   VEuPathDB; HostDB:ENSBTAG00000022731; -.
DR   VGNC; VGNC:35319; SSR1.
DR   eggNOG; KOG1631; Eukaryota.
DR   GeneTree; ENSGT00400000022103; -.
DR   HOGENOM; CLU_073618_0_0_1; -.
DR   InParanoid; A6QLP7; -.
DR   OrthoDB; 1349929at2759; -.
DR   TreeFam; TF321074; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000022731; Expressed in spermatocyte and 106 other tissues.
DR   ExpressionAtlas; A6QLP7; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Calcium; Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..286
FT                   /note="Translocon-associated protein subunit alpha"
FT                   /id="PRO_0000330739"
FT   TOPO_DOM        21..207
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..286
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          37..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..77
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43307"
FT   MOD_RES         260
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P43307"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43307"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   286 AA;  32054 MW;  2FBB1D7095BF5631 CRC64;
     MSSLRRLLLL LLLVFPATLL LRVGPGGSLA VAQDLTEDEE TVEDSIIEDE DDEAEVEEDE
     PTDLAEDKEE DDVSGEPEAS PSADTTILFV KGEDFPANNI VKFLVGFTNK GTEDFIVESL
     DASFRYPQDY QFYIQNFTAL PLNTVVPPQR QATFEYSFIP AEPMGGRPFG LVINLNYKDL
     NGNVFQDAVF NQTVTIIERE DGLDGETIFM YMFLAGLGLL VVVGLHQLLE SRKRKRPIQK
     VEMGTSSQND VDMSWIPQET LNQINKASPR RLPRKRAQKR SVGSDE