ID   RCAS1_RAT               Reviewed;         213 AA.
AC   Q5PQP2;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Receptor-binding cancer antigen expressed on SiSo cells;
DE   AltName: Full=Estrogen receptor-binding fragment-associated gene 9 protein;
GN   Name=Ebag9;
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 [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16396499; DOI=10.1021/pr0503073;
RA   Moser K., White F.M.;
RT   "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT   MS/MS.";
RL   J. Proteome Res. 5:98-104(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, 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: 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   -!- DOMAIN: The coiled coil domain is necessary for the homodimerization.
CC       {ECO:0000250}.
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DR   EMBL; BC087093; AAH87093.1; -; mRNA.
DR   RefSeq; NP_001009665.1; NM_001009665.1.
DR   RefSeq; XP_006241675.1; XM_006241613.3.
DR   AlphaFoldDB; Q5PQP2; -.
DR   SMR; Q5PQP2; -.
DR   IntAct; Q5PQP2; 1.
DR   STRING; 10116.ENSRNOP00000005705; -.
DR   iPTMnet; Q5PQP2; -.
DR   PhosphoSitePlus; Q5PQP2; -.
DR   SwissPalm; Q5PQP2; -.
DR   PaxDb; Q5PQP2; -.
DR   PRIDE; Q5PQP2; -.
DR   Ensembl; ENSRNOT00000105146; ENSRNOP00000079314; ENSRNOG00000004220.
DR   GeneID; 299864; -.
DR   KEGG; rno:299864; -.
DR   UCSC; RGD:1307293; rat.
DR   CTD; 9166; -.
DR   RGD; 1307293; Ebag9.
DR   eggNOG; ENOG502QSN4; Eukaryota.
DR   GeneTree; ENSGT00390000004040; -.
DR   HOGENOM; CLU_094995_0_0_1; -.
DR   InParanoid; Q5PQP2; -.
DR   OMA; LGEMENW; -.
DR   OrthoDB; 1552653at2759; -.
DR   PhylomeDB; Q5PQP2; -.
DR   TreeFam; TF326584; -.
DR   PRO; PR:Q5PQP2; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000004220; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q5PQP2; RN.
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; IDA:RGD.
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_0000097197"
FT   TOPO_DOM        1..6
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..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          168..209
FT                   /evidence="ECO:0000255"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16396499,
FT                   ECO:0007744|PubMed:22673903"
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"
SQ   SEQUENCE   213 AA;  24187 MW;  B151945039179878 CRC64;
     MAITQFRLFK VCTCLATVLS FLKRLICRSG RGRKLSGDQI TLPTTVDYSS VPKQTDVEEW
     TSWDEDAPTS VKIEGGTGNA AAQQNSLEQL EPDYFKDMTP TIRKTQKIVI KKREPLSFGV
     PDGSTGFSSR LAATQDMPFI HQSSELGDLD TWQENSNAWE EEEDAAWQAE EVLRQQKIAD
     REKRAAEQQR KKMEKEAQRL LKKEQNKMGV KLS