ID   SSRA_PONAB              Reviewed;         291 AA.
AC   Q5R4X4;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR861115; CAH93192.1; -; mRNA.
DR   RefSeq; NP_001126878.1; NM_001133406.2.
DR   AlphaFoldDB; Q5R4X4; -.
DR   STRING; 9601.ENSPPYP00000018126; -.
DR   Ensembl; ENSPPYT00000050058; ENSPPYP00000033492; ENSPPYG00000016205.
DR   GeneID; 100173891; -.
DR   KEGG; pon:100173891; -.
DR   CTD; 6745; -.
DR   eggNOG; KOG1631; Eukaryota.
DR   GeneTree; ENSGT00400000022103; -.
DR   InParanoid; Q5R4X4; -.
DR   OrthoDB; 1349929at2759; -.
DR   Proteomes; UP000001595; Chromosome 6.
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..291
FT                   /note="Translocon-associated protein subunit alpha"
FT                   /id="PRO_0000033283"
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..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          34..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..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         273
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   291 AA;  32855 MW;  4A168E3047C7022C CRC64;
     MRLLPRLLLL LLLVFPATVL FRGGPRGSLA VAQDLTEDEE TVEDSIIEDE DDEAEVEEDE
     PTDLVEDKEE EDVSGEPEAS PSADTTILFV KGEDFPANNI VKFLVGFTNK GTEDFIVESL
     DASFRYPQDY QFYIQNFTAL PLNTVVPPQR QATFEYSFIP AEPMGGRPFG LVINLNYKDL
     NGNVFQDAVF NQTVTVIERE DGLDGETIFM YMFLAGLGLL VIVGLHQLLE SRKRKRPVQK
     VEMGTSSQND VDMSWIPQET LNQIMQSRRD KASPRRLPRK RAQKRSVGSD E