GPC5B_MOUSE
ID GPC5B_MOUSE Reviewed; 410 AA.
AC Q923Z0; Q8CCV3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=G-protein coupled receptor family C group 5 member B;
DE AltName: Full=Retinoic acid-induced gene 2 protein;
DE Short=RAIG-2;
DE Flags: Precursor;
GN Name=Gprc5b; Synonyms=Raig2;
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].
RA Tao Q., Lotan R.;
RT "Molecular cloning and characterization of mouse retinoic acid-inducible
RT orphan G protein-coupled receptors.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Kidney;
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: Unknown. This retinoic acid-inducible G-protein coupled
CC receptor provide evidence for a possible interaction between retinoid
CC and G-protein signaling pathways (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; AF378831; AAK58076.1; -; mRNA.
DR EMBL; AK032047; BAC27669.1; -; mRNA.
DR EMBL; BC020004; AAH20004.1; -; mRNA.
DR CCDS; CCDS21777.1; -.
DR RefSeq; NP_071865.1; NM_022420.2.
DR AlphaFoldDB; Q923Z0; -.
DR SMR; Q923Z0; -.
DR STRING; 10090.ENSMUSP00000008878; -.
DR GlyGen; Q923Z0; 1 site.
DR iPTMnet; Q923Z0; -.
DR PhosphoSitePlus; Q923Z0; -.
DR MaxQB; Q923Z0; -.
DR PaxDb; Q923Z0; -.
DR PeptideAtlas; Q923Z0; -.
DR PRIDE; Q923Z0; -.
DR ProteomicsDB; 271430; -.
DR Antibodypedia; 12141; 310 antibodies from 31 providers.
DR DNASU; 64297; -.
DR Ensembl; ENSMUST00000008878; ENSMUSP00000008878; ENSMUSG00000008734.
DR GeneID; 64297; -.
DR KEGG; mmu:64297; -.
DR UCSC; uc009jkx.2; mouse.
DR CTD; 51704; -.
DR MGI; MGI:1927596; Gprc5b.
DR VEuPathDB; HostDB:ENSMUSG00000008734; -.
DR eggNOG; ENOG502QWT9; Eukaryota.
DR GeneTree; ENSGT00950000182961; -.
DR HOGENOM; CLU_044162_1_1_1; -.
DR InParanoid; Q923Z0; -.
DR OMA; RDNKLAC; -.
DR PhylomeDB; Q923Z0; -.
DR TreeFam; TF321410; -.
DR BioGRID-ORCS; 64297; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Gprc5b; mouse.
DR PRO; PR:Q923Z0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q923Z0; protein.
DR Bgee; ENSMUSG00000008734; Expressed in epithelium of lens and 223 other tissues.
DR ExpressionAtlas; Q923Z0; baseline and differential.
DR Genevisible; Q923Z0; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR InterPro; IPR017978; GPCR_3_C.
DR Pfam; PF00003; 7tm_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..410
FT /note="G-protein coupled receptor family C group 5 member
FT B"
FT /id="PRO_0000012966"
FT TOPO_DOM 29..56
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..271
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 356..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 118
FT /note="D -> G (in Ref. 2; BAC27669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 45899 MW; E1DA5283270FFF34 CRC64;
MFLVLERKMR THQVFPLPLL LVIASVASEN ASTSRGCGLD LLPQYVSLCD LDAIWGIVVE
AVAGAGALIT LLLMLILLVR LPFIKDKERK RPVCLHFLFL LGTLGLFGLT FAFIIQMDET
ICSIRRFLWG VLFALCFSCL LSQAWRVRRL VRQGTSPASW QLVSLALCLM LVQVIIATEW
LVLTVLRDTK PACAYEPMDF VMALIYDMVL LAITLAQSLF TLCGKFKRWK VNGAFILVTT
FLSALIWVVW MTMYLFGNSL IKQGDAWSDP TLAITLAASG WVFVIFHAIP EIHYTLLPPL
QENPPNYFDT SQPRMRETAF DEEMHLPRAY MENKAFSMDE HNAALRSAVG FSNGSLEQRS
SSLGKKPSSL GNRPSAPFRS NVYQPTEMAV VLNGGTIPTA PPSHTGRHHW
