SSRG_MOUSE
ID SSRG_MOUSE Reviewed; 185 AA.
AC Q9DCF9; Q8C0Z8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Kidney, Liver, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-11, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC gamma.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DCF9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DCF9-2; Sequence=VSP_013474, VSP_013475;
CC -!- SIMILARITY: Belongs to the TRAP-gamma family. {ECO:0000305}.
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DR EMBL; AK002818; BAB22381.1; -; mRNA.
DR EMBL; AK029353; BAC26413.1; -; mRNA.
DR EMBL; AK076235; BAC36268.1; -; mRNA.
DR EMBL; AK088555; BAC40420.1; -; mRNA.
DR EMBL; BC011111; AAH11111.1; -; mRNA.
DR CCDS; CCDS17386.1; -. [Q9DCF9-1]
DR RefSeq; NP_080431.1; NM_026155.3. [Q9DCF9-1]
DR AlphaFoldDB; Q9DCF9; -.
DR BioGRID; 212185; 4.
DR IntAct; Q9DCF9; 1.
DR STRING; 10090.ENSMUSP00000029414; -.
DR iPTMnet; Q9DCF9; -.
DR PhosphoSitePlus; Q9DCF9; -.
DR EPD; Q9DCF9; -.
DR jPOST; Q9DCF9; -.
DR MaxQB; Q9DCF9; -.
DR PaxDb; Q9DCF9; -.
DR PRIDE; Q9DCF9; -.
DR ProteomicsDB; 258744; -. [Q9DCF9-1]
DR ProteomicsDB; 258745; -. [Q9DCF9-2]
DR Antibodypedia; 18400; 64 antibodies from 19 providers.
DR DNASU; 67437; -.
DR Ensembl; ENSMUST00000029414; ENSMUSP00000029414; ENSMUSG00000027828. [Q9DCF9-1]
DR Ensembl; ENSMUST00000119896; ENSMUSP00000113831; ENSMUSG00000027828. [Q9DCF9-2]
DR GeneID; 67437; -.
DR KEGG; mmu:67437; -.
DR UCSC; uc008pkn.1; mouse. [Q9DCF9-1]
DR UCSC; uc008pko.1; mouse. [Q9DCF9-2]
DR CTD; 6747; -.
DR MGI; MGI:1914687; Ssr3.
DR VEuPathDB; HostDB:ENSMUSG00000027828; -.
DR eggNOG; KOG4490; Eukaryota.
DR GeneTree; ENSGT00390000000970; -.
DR HOGENOM; CLU_092935_0_0_1; -.
DR InParanoid; Q9DCF9; -.
DR OMA; TKFTLKH; -.
DR PhylomeDB; Q9DCF9; -.
DR TreeFam; TF314998; -.
DR BioGRID-ORCS; 67437; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Ssr3; mouse.
DR PRO; PR:Q9DCF9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9DCF9; protein.
DR Bgee; ENSMUSG00000027828; Expressed in endothelial cell of lymphatic vessel and 262 other tissues.
DR ExpressionAtlas; Q9DCF9; baseline and differential.
DR Genevisible; Q9DCF9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Alternative splicing; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..185
FT /note="Translocon-associated protein subunit gamma"
FT /id="PRO_0000191691"
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:0007744|PubMed:21183079"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT VAR_SEQ 165..179
FT /note="NYILSISASSGLIAL -> YPLESFPINSSLLCF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013474"
FT VAR_SEQ 180..185
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013475"
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
