ID   SSRA_ONCMY              Reviewed;         288 AA.
AC   P45433;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8050590; DOI=10.1016/0014-5793(94)00693-8;
RA   Hartmann E., Prehn S.;
RT   "The N-terminal region of the alpha-subunit of the TRAP complex has a
RT   conserved cluster of negative charges.";
RL   FEBS Lett. 349:324-326(1994).
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.
CC   -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC       gamma.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC       I membrane protein.
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.
CC   -!- SIMILARITY: Belongs to the TRAP-alpha 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; Z12831; CAA78291.1; -; mRNA.
DR   PIR; I51332; I51332.
DR   RefSeq; NP_001118198.1; NM_001124726.1.
DR   AlphaFoldDB; P45433; -.
DR   Ensembl; ENSOMYT00000004747; ENSOMYP00000004235; ENSOMYG00000002217.
DR   GeneID; 100136780; -.
DR   KEGG; omy:100136780; -.
DR   GeneTree; ENSGT00400000022103; -.
DR   OrthoDB; 1349929at2759; -.
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   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..288
FT                   /note="Translocon-associated protein subunit alpha"
FT                   /id="PRO_0000033286"
FT   TOPO_DOM        29..208
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..288
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          34..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..69
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   288 AA;  31856 MW;  84723DBF17FD7C8E CRC64;
     MFNFGSKILV LFLVAFPCGL ISFGRVSADS ESAEDIFPDS TVDEEEEEEE DEVLVEEDQV
     PGSETEDDID EDAAVGDVTS HPDADTTIVF VTGEEFPANE IVKFLVGFTN KGSQDFTVHS
     LEASFRYPQD FQFYIQNFTA LPLSTVVQPQ KQASFEYSFI PAQPMAGRPF GLVILLNYQD
     SEGNGFQTAI YNQTVTIVEL EEGLDGETIF MYIFLTGLVV LAVFGMYQVL ESRTRKRFPV
     KVETGTGGMN GVDISWIPQE TLNIMSKASA SPKASPRKRT KRAVGVDQ