RCAS1_MOUSE
ID RCAS1_MOUSE Reviewed; 213 AA.
AC Q9D0V7; Q0VET4; Q3TVG2; Q3TWY4; Q9QYD0;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Receptor-binding cancer antigen expressed on SiSo cells;
DE AltName: Full=Cancer-associated surface antigen RCAS1;
DE AltName: Full=Estrogen receptor-binding fragment-associated gene 9 protein;
GN Name=Ebag9; Synonyms=Rcas1;
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 [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC TISSUE=Brain;
RX PubMed=11374862; DOI=10.1006/bbrc.2001.4892;
RA Tsuchiya F., Ikeda K., Tsutsumi O., Hiroi H., Momoeda M., Taketani Y.,
RA Muramatsu M., Inoue S.;
RT "Molecular cloning and characterization of mouse EBAG9, homolog of a human
RT cancer associated surface antigen: expression and regulation by estrogen.";
RL Biochem. Biophys. Res. Commun. 284:2-10(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Nakashima M., Sonoda K., Watanabe T.;
RT "Human type II receptor like cancer associated surface antigen (RCAS1).";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP 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: May participate in suppression of cell proliferation and
CC induces apoptotic cell death through activation of interleukin-1-beta
CC converting enzyme (ICE)-like proteases. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type III membrane protein {ECO:0000250}. Note=Predominantly
CC located in the Golgi. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain,
CC spleen, liver, kidney and testis. {ECO:0000269|PubMed:11374862}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing embryo.
CC {ECO:0000269|PubMed:11374862}.
CC -!- INDUCTION: By 17-beta-estradiol (E2). {ECO:0000269|PubMed:11374862}.
CC -!- DOMAIN: The coiled coil domain is necessary for the homodimerization.
CC {ECO:0000250}.
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; AY009091; AAG41054.1; -; mRNA.
DR EMBL; AF076524; AAF23857.1; -; mRNA.
DR EMBL; AK004366; BAB23277.1; -; mRNA.
DR EMBL; AK159499; BAE35132.1; -; mRNA.
DR EMBL; AK160149; BAE35657.1; -; mRNA.
DR EMBL; BC108397; AAI08398.1; -; mRNA.
DR EMBL; BC119118; AAI19119.1; -; mRNA.
DR EMBL; BC119120; AAI19121.1; -; mRNA.
DR EMBL; BC144740; AAI44741.1; -; mRNA.
DR CCDS; CCDS27457.1; -.
DR PIR; JC7696; JC7696.
DR RefSeq; NP_062353.3; NM_019480.4.
DR RefSeq; XP_006521256.1; XM_006521193.2.
DR RefSeq; XP_006521257.1; XM_006521194.3.
DR RefSeq; XP_006521258.1; XM_006521195.3.
DR AlphaFoldDB; Q9D0V7; -.
DR SMR; Q9D0V7; -.
DR STRING; 10090.ENSMUSP00000022964; -.
DR iPTMnet; Q9D0V7; -.
DR PhosphoSitePlus; Q9D0V7; -.
DR SwissPalm; Q9D0V7; -.
DR EPD; Q9D0V7; -.
DR jPOST; Q9D0V7; -.
DR MaxQB; Q9D0V7; -.
DR PaxDb; Q9D0V7; -.
DR PeptideAtlas; Q9D0V7; -.
DR PRIDE; Q9D0V7; -.
DR ProteomicsDB; 254903; -.
DR Antibodypedia; 13458; 424 antibodies from 39 providers.
DR DNASU; 55960; -.
DR Ensembl; ENSMUST00000022964; ENSMUSP00000022964; ENSMUSG00000022339.
DR Ensembl; ENSMUST00000226165; ENSMUSP00000153791; ENSMUSG00000022339.
DR Ensembl; ENSMUST00000227691; ENSMUSP00000154361; ENSMUSG00000022339.
DR GeneID; 55960; -.
DR KEGG; mmu:55960; -.
DR UCSC; uc007vpz.1; mouse.
DR CTD; 9166; -.
DR MGI; MGI:1859920; Ebag9.
DR VEuPathDB; HostDB:ENSMUSG00000022339; -.
DR eggNOG; ENOG502QSN4; Eukaryota.
DR GeneTree; ENSGT00390000004040; -.
DR HOGENOM; CLU_094995_0_0_1; -.
DR InParanoid; Q9D0V7; -.
DR OMA; LGEMENW; -.
DR OrthoDB; 1552653at2759; -.
DR PhylomeDB; Q9D0V7; -.
DR TreeFam; TF326584; -.
DR BioGRID-ORCS; 55960; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Ebag9; mouse.
DR PRO; PR:Q9D0V7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D0V7; protein.
DR Bgee; ENSMUSG00000022339; Expressed in seminal vesicle and 243 other tissues.
DR ExpressionAtlas; Q9D0V7; baseline and differential.
DR Genevisible; Q9D0V7; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR InterPro; IPR017025; Cancer-assoc_antigen_RCAS1.
DR PANTHER; PTHR15208; PTHR15208; 1.
DR PIRSF; PIRSF034247; RCAS1; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Coiled coil; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..213
FT /note="Receptor-binding cancer antigen expressed on SiSo
FT cells"
FT /id="PRO_0000097196"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..27
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 179..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 163..211
FT /evidence="ECO:0000255"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00559"
FT MOD_RES 94
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O00559"
FT CONFLICT 11
FT /note="V -> G (in Ref. 3; AAF23857)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="P -> A (in Ref. 3; AAF23857)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="D -> G (in Ref. 3; BAE35132)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="N -> S (in Ref. 3; AAF23857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 213 AA; 24319 MW; 349FAD1E2AEFF529 CRC64;
MAITQFRLFK VCTCLATVFS FLKRLICRSG RGRKLSGDQI TLPTTVDYSS VPKQTDVEEW
TSWDEDAPTS VKIEGGNGNV ATQQNSLEQL EPDYFKDMTP TIRKTQKIVI KKREPLNFGV
PDGSTGFSSR LAATQDMPFI HQSSELGDLD TWQENSNAWE EEEDAAWQAE EVLRQQKIAD
REKRAAEQQR KKMEKEAQRL MKKEQNKIGV KLS
