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Retinoic acid-induced protein 3 (G-protein coupled receptor family C group 5 member A) (Phorbol ester induced gene 1) (PEIG-1) (Retinoic acid-induced gene 1 protein) (RAIG-1)

 RAI3_HUMAN              Reviewed;         357 AA.
Q8NFJ5; B3KV45; O95357;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 2.
30-AUG-2017, entry version 137.
RecName: Full=Retinoic acid-induced protein 3;
AltName: Full=G-protein coupled receptor family C group 5 member A;
AltName: Full=Phorbol ester induced gene 1 {ECO:0000303|PubMed:8832110};
Short=PEIG-1;
AltName: Full=Retinoic acid-induced gene 1 protein;
Short=RAIG-1;
Name=GPRC5A; Synonyms=GPCR5A, RAI3, RAIG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Colon carcinoma;
PubMed=8832110;
Cafferata E.G., Gonzalez-Guerrico A.M., Pivetta O.H.,
Santa-Coloma T.A.;
"Identification by differential display of a mRNA specifically induced
by 12-O-tetradecanoylphorbol-13-acetate (TPA) in T84 human colon
carcinoma cells.";
Cell. Mol. Biol. 42:797-804(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, AND
TISSUE SPECIFICITY.
TISSUE=Lung;
PubMed=9857033; DOI=10.1074/jbc.273.52.35008;
Cheng Y., Lotan R.;
"Molecular cloning and characterization of a novel retinoic acid-
inducible gene that encodes a putative G protein-coupled receptor.";
J. Biol. Chem. 273:35008-35015(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY.
PubMed=10783259; DOI=10.1006/geno.2000.6164;
Braeuner-Osborne H., Krogsgaard-Larsen P.;
"Sequence and expression pattern of a novel human orphan G-protein-
coupled receptor, GPRC5B, a family C receptor with a short amino-
terminal domain.";
Genomics 65:121-128(2000).
[7]
TISSUE SPECIFICITY.
PubMed=10945465; DOI=10.1006/geno.2000.6226;
Robbins M.J., Michalovich D., Hill J., Calver A.R., Medhurst A.D.,
Gloger I., Sims M.A., Middlemiss D.N., Pangalos M.N.;
"Molecular cloning and characterization of two novel retinoic acid-
inducible orphan G-protein-coupled receptors (GPRC5B and GPRC5C).";
Genomics 67:8-18(2000).
[8]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=18000218; DOI=10.1093/jnci/djm208;
Tao Q., Fujimoto J., Men T., Ye X., Deng J., Lacroix L.,
Clifford J.L., Mao L., Van Pelt C.S., Lee J.J., Lotan D., Lotan R.;
"Identification of the retinoic acid-inducible Gprc5a as a new lung
tumor suppressor gene.";
J. Natl. Cancer Inst. 99:1668-1682(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-345, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345 AND TYR-347, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
INTERACTION WITH EGFR, AND PHOSPHORYLATION AT TYR-317; TYR-320;
TYR-347 AND TYR-350 BY EGFR.
PubMed=25311788; DOI=10.1186/1476-4598-13-233;
Lin X., Zhong S., Ye X., Liao Y., Yao F., Yang X., Sun B., Zhang J.,
Li Q., Gao Y., Wang Y., Liu J., Han B., Chin Y.E., Zhou B.P., Deng J.;
"EGFR phosphorylates and inhibits lung tumor suppressor GPRC5A in lung
cancer.";
Mol. Cancer 13:233-233(2014).
-!- FUNCTION: Orphan receptor. Could be involved in modulating
differentiation and maintaining homeostasis of epithelial cells.
This retinoic acid-inducible GPCR provide evidence for a possible
interaction between retinoid and G-protein signaling pathways.
Functions as a negative modulator of EGFR signaling (By
similarity). May act as a lung tumor suppressor (PubMed:18000218).
{ECO:0000250|UniProtKB:Q8BHL4, ECO:0000269|PubMed:18000218}.
-!- SUBUNIT: Interacts (via its transmembrane domain) with EGFR.
{ECO:0000269|PubMed:25311788}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9857033};
Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle
membrane {ECO:0000269|PubMed:9857033}; Multi-pass membrane protein
{ECO:0000255}. Note=Localized in perinuclear vesicles, probably
Golgi-associated vesicles. {ECO:0000269|PubMed:18000218}.
-!- TISSUE SPECIFICITY: Expressed at high level in fetal and adult
lung tissues but repressed in most human lung cancers
(PubMed:9857033, PubMed:18000218). Constitutively expressed in
fetal kidney and adult placenta, kidney, prostate, testis, ovary,
small intestine, colon, stomach, and spinal chord at low to
moderate levels. Not detectable in fetal heart, brain, and liver
and adult heart, brain, liver, skeletal muscle, pancreas, spleen,
thymus, and peripheral leukocytes. According to PubMed:10783259,
expressed at low but detectable level in pancreas and heart.
{ECO:0000269|PubMed:10783259, ECO:0000269|PubMed:10945465,
ECO:0000269|PubMed:18000218, ECO:0000269|PubMed:9857033}.
-!- INDUCTION: By all-trans retinoic acid (ATRA).
{ECO:0000269|PubMed:9857033}.
-!- PTM: Phosphorylated in two conserved double-tyrosine motifs, TYR-
317/TYR-320 and TYR-347/TYR-350, by EGFR; leading to inactivation
of the tumor suppressive function of GPRC5A in lung cancer cells.
TYR-317 and TYR-320 are the preferred residues responsible for
EGFR-mediated GPRC5A phosphorylation.
{ECO:0000269|PubMed:25311788}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
{ECO:0000305}.
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EMBL; AF506289; AAM77594.1; -; mRNA.
EMBL; AF095448; AAC98506.1; -; mRNA.
EMBL; AK001761; BAA91890.1; -; mRNA.
EMBL; AK122672; BAG53657.1; -; mRNA.
EMBL; CH471094; EAW96289.1; -; Genomic_DNA.
EMBL; BC003665; AAH03665.1; -; mRNA.
CCDS; CCDS8657.1; -.
RefSeq; NP_003970.1; NM_003979.3.
UniGene; Hs.631733; -.
ProteinModelPortal; Q8NFJ5; -.
BioGrid; 114514; 36.
IntAct; Q8NFJ5; 29.
MINT; MINT-5005465; -.
STRING; 9606.ENSP00000014914; -.
DrugBank; DB00755; Tretinoin.
iPTMnet; Q8NFJ5; -.
PhosphoSitePlus; Q8NFJ5; -.
SwissPalm; Q8NFJ5; -.
BioMuta; GPRC5A; -.
DMDM; 46396943; -.
EPD; Q8NFJ5; -.
MaxQB; Q8NFJ5; -.
PaxDb; Q8NFJ5; -.
PeptideAtlas; Q8NFJ5; -.
PRIDE; Q8NFJ5; -.
DNASU; 9052; -.
Ensembl; ENST00000014914; ENSP00000014914; ENSG00000013588.
GeneID; 9052; -.
KEGG; hsa:9052; -.
UCSC; uc001rba.4; human.
CTD; 9052; -.
DisGeNET; 9052; -.
GeneCards; GPRC5A; -.
GeneCards; MIR614; -.
HGNC; HGNC:9836; GPRC5A.
HPA; HPA007928; -.
HPA; HPA046526; -.
MIM; 604138; gene.
neXtProt; NX_Q8NFJ5; -.
OpenTargets; ENSG00000013588; -.
PharmGKB; PA34194; -.
eggNOG; ENOG410IIGU; Eukaryota.
eggNOG; ENOG410YD51; LUCA.
GeneTree; ENSGT00520000055551; -.
HOGENOM; HOG000116197; -.
HOVERGEN; HBG049967; -.
InParanoid; Q8NFJ5; -.
KO; K08468; -.
OMA; WDDTILS; -.
OrthoDB; EOG091G0DAG; -.
PhylomeDB; Q8NFJ5; -.
TreeFam; TF321410; -.
ChiTaRS; GPRC5A; human.
GeneWiki; GPRC5A; -.
GenomeRNAi; 9052; -.
PRO; PR:Q8NFJ5; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000013588; -.
CleanEx; HS_GPRC5A; -.
ExpressionAtlas; Q8NFJ5; baseline and differential.
Genevisible; Q8NFJ5; HS.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR017978; GPCR_3_C.
Pfam; PF00003; 7tm_3; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasmic vesicle;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix; Tumor suppressor.
CHAIN 1 357 Retinoic acid-induced protein 3.
/FTId=PRO_0000206895.
TOPO_DOM 1 33 Extracellular. {ECO:0000305}.
TRANSMEM 34 54 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 55 68 Cytoplasmic. {ECO:0000305}.
TRANSMEM 69 89 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 90 97 Extracellular. {ECO:0000305}.
TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 119 129 Cytoplasmic. {ECO:0000305}.
TRANSMEM 130 150 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 151 176 Extracellular. {ECO:0000305}.
TRANSMEM 177 197 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 198 212 Cytoplasmic. {ECO:0000305}.
TRANSMEM 213 233 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 234 247 Extracellular. {ECO:0000305}.
TRANSMEM 248 268 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 269 357 Cytoplasmic. {ECO:0000305}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 317 317 Phosphotyrosine.
{ECO:0000269|PubMed:25311788}.
MOD_RES 320 320 Phosphotyrosine.
{ECO:0000269|PubMed:25311788}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 347 347 Phosphotyrosine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:25311788}.
MOD_RES 350 350 Phosphotyrosine.
{ECO:0000269|PubMed:25311788}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 9 9 C -> F (in dbSNP:rs11550683).
/FTId=VAR_049281.
VARIANT 118 118 S -> G (in dbSNP:rs850932).
/FTId=VAR_018296.
VARIANT 182 182 T -> A (in dbSNP:rs12368599).
/FTId=VAR_049282.
CONFLICT 292 292 S -> G (in Ref. 1; AAM77594).
{ECO:0000305}.
SEQUENCE 357 AA; 40251 MW; 7BEB524BF6F307E5 CRC64;
MATTVPDGCR NGLKSKYYRL CDKAEAWGIV LETVATAGVV TSVAFMLTLP ILVCKVQDSN
RRKMLPTQFL FLLGVLGIFG LTFAFIIGLD GSTGPTRFFL FGILFSICFS CLLAHAVSLT
KLVRGRKPLS LLVILGLAVG FSLVQDVIAI EYIVLTMNRT NVNVFSELSA PRRNEDFVLL
LTYVLFLMAL TFLMSSFTFC GSFTGWKRHG AHIYLTMLLS IAIWVAWITL LMLPDFDRRW
DDTILSSALA ANGWVFLLAY VSPEFWLLTK QRNPMDYPVE DAFCKPQLVK KSYGVENRAY
SQEEITQGFE ETGDTLYAPY STHFQLQNQP PQKEFSIPRA HAWPSPYKDY EVKKEGS


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Genprice Inc, Invoices and accounting
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