ID   SSRA_RABIT              Reviewed;         286 AA.
AC   P53815;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 90.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RA   Applequist S.E., Raman C., Beck-Engeser G.B., Jaeck H.-M.;
RL   Submitted (APR-1996) 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.
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; 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; U34847; AAA96272.1; -; mRNA.
DR   RefSeq; NP_001076222.1; NM_001082753.1.
DR   AlphaFoldDB; P53815; -.
DR   STRING; 9986.ENSOCUP00000007844; -.
DR   PRIDE; P53815; -.
DR   GeneID; 100009532; -.
DR   KEGG; ocu:100009532; -.
DR   CTD; 6745; -.
DR   eggNOG; KOG1631; Eukaryota.
DR   InParanoid; P53815; -.
DR   OrthoDB; 1349929at2759; -.
DR   Proteomes; UP000001811; Unplaced.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..286
FT                   /note="Translocon-associated protein subunit alpha"
FT                   /id="PRO_0000033284"
FT   TOPO_DOM        22..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          28..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..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;  32091 MW;  3269B24C53E1CD87 CRC64;
     MRLLPRLLLL LLLVFPATVL LRGGPGGSLA EAQDLSEDEE TVEDSVIEDE DDEAEVEEDE
     PTDLAEDREE EDVSGEPEAS PSADTTILFV KGEDFPANNI VRFLVGFTNK GTEDFIVESL
     DASFRYPQDY QFYIQNFTAL PLNTIVPPQR QATFEYSFIP AEPMGGRPFG LVINLNYKDF
     NGNVFQDAVF NQTVTVIERE DGLDGQTIFM YMSLAGLGLL VVVGLHQLLE SRNRKRPIQK
     VEMGTSSQND VDMSWIPQET LNQINKASPR RLPRKRPQKR SVGSDE