SSRG_RAT
ID SSRG_RAT Reviewed; 185 AA.
AC Q08013; Q6P6U5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Translocon-associated protein subunit gamma;
DE Short=TRAP-gamma;
DE AltName: Full=Signal sequence receptor subunit gamma;
DE Short=SSR-gamma;
GN Name=Ssr3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7916687; DOI=10.1111/j.1432-1033.1993.tb17933.x;
RA Hartmann E., Goerlich D., Kostka S., Otto A., Kraft R., Knespel S.,
RA Buerger E., Rapoport T.A., Prehn S.;
RT "A tetrameric complex of membrane proteins in the endoplasmic reticulum.";
RL Eur. J. Biochem. 214:375-381(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
CC -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC gamma.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the TRAP-gamma family. {ECO:0000305}.
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DR EMBL; Z14030; CAA78405.1; -; mRNA.
DR EMBL; BC062015; AAH62015.1; -; mRNA.
DR PIR; S33294; S33294.
DR RefSeq; NP_112382.2; NM_031120.2.
DR AlphaFoldDB; Q08013; -.
DR STRING; 10116.ENSRNOP00000014912; -.
DR iPTMnet; Q08013; -.
DR PhosphoSitePlus; Q08013; -.
DR jPOST; Q08013; -.
DR PRIDE; Q08013; -.
DR GeneID; 81784; -.
DR KEGG; rno:81784; -.
DR UCSC; RGD:621630; rat.
DR CTD; 6747; -.
DR RGD; 621630; Ssr3.
DR InParanoid; Q08013; -.
DR OrthoDB; 1450535at2759; -.
DR PhylomeDB; Q08013; -.
DR PRO; PR:Q08013; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005784; C:Sec61 translocon complex; NAS:RGD.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR InterPro; IPR009779; SSR3.
DR PANTHER; PTHR13399; PTHR13399; 1.
DR Pfam; PF07074; TRAP-gamma; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..185
FT /note="Translocon-associated protein subunit gamma"
FT /id="PRO_0000191693"
FT TOPO_DOM 1..27
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..135
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNL2"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCF9"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNL2"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 163
FT /note="T -> R (in Ref. 1; CAA78405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 21064 MW; 18E0A54483E45D6E CRC64;
MAPKGGSKQQ SEEDLLLQDF SRNLSAKSSA LFFGNAFIVS AIPIWLYWRI WHMDLIQSAV
LYSVMTLVST YLVAFAYKNV KFVLKHKVAQ KREDAVSKEV TRKLSEADNR KMSRKEKDER
ILWKKNEVAD YEATTFSIFY NNTLFLVLVI VASFFILKNF NPTVNYILSI SASSGLIALL
STGSK
