SSRA_CANLF
ID SSRA_CANLF Reviewed; 286 AA.
AC P16967;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Translocon-associated protein subunit alpha;
DE Short=TRAP-alpha;
DE AltName: Full=PGP35;
DE AltName: Full=Signal sequence receptor subunit alpha;
DE Short=SSR-alpha;
DE Flags: Precursor;
GN Name=SSR1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=2156703; DOI=10.1111/j.1432-1033.1990.tb15421.x;
RA Prehn S., Herz J., Hartmann E., Kurzchalia T.V., Frank R., Roemisch K.,
RA Dobberstein B., Rapoport T.A.;
RT "Structure and biosynthesis of the signal-sequence receptor.";
RL Eur. J. Biochem. 188:439-445(1990).
RN [2]
RP PROTEIN SEQUENCE OF 165-186 AND 254-264.
RX PubMed=1918067; DOI=10.1016/s0021-9258(18)55036-5;
RA Wada I., Rindress D., Cameron P.H., Ou W.-J., Doherty J.J. II, Louvard D.,
RA Bell A.W., Dignard D., Thomas D.Y., Bergeron J.J.M.;
RT "SSR alpha and associated calnexin are major calcium binding proteins of
RT the endoplasmic reticulum membrane.";
RL J. Biol. Chem. 266:19599-19610(1991).
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.
CC -!- MISCELLANEOUS: Seems to bind calcium.
CC -!- SIMILARITY: Belongs to the TRAP-alpha family. {ECO:0000305}.
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DR EMBL; X51367; CAA35752.1; -; mRNA.
DR PIR; S08993; S08993.
DR RefSeq; NP_001003270.1; NM_001003270.1.
DR AlphaFoldDB; P16967; -.
DR CORUM; P16967; -.
DR STRING; 9615.ENSCAFP00000053130; -.
DR PaxDb; P16967; -.
DR PRIDE; P16967; -.
DR GeneID; 403951; -.
DR KEGG; cfa:403951; -.
DR CTD; 6745; -.
DR eggNOG; KOG1631; Eukaryota.
DR InParanoid; P16967; -.
DR OrthoDB; 1349929at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..286
FT /note="Translocon-associated protein subunit alpha"
FT /id="PRO_0000033280"
FT TOPO_DOM 24..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; 31976 MW; E0E0F1CF5D97E72E CRC64;
MRVLPRLLLL LLLAFPAAVL LRGGPGGSLV AAQDLTEDEE TVEDSIIEDE DDEAEVEEDE
PTDLAEDKEE EDVSGEPEAS PSADTTILFV KGEDFPANNI VKFLVGFTNK GTEDFIVESL
DASFRYPQDY QFYIQNFTAL PLNTVVPPQR QATFEYSFIP AEPMGGRPFG LVINLNYKDL
NGNVFQDAVF NQTVTIIERE DGLDGETIFM YMFLAGLGLL VVVGLHQLLE SRKRKRPIQK
VEMGTSSQND VDMSWIPQET LNQINKASPR RLPRKRAQKR SVGSDE
