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GPC5B_HUMAN
ID   GPC5B_HUMAN             Reviewed;         403 AA.
AC   Q9NZH0; D2DFB0; O75205; Q8NBZ8;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=G-protein coupled receptor family C group 5 member B;
DE   AltName: Full=A-69G12.1;
DE   AltName: Full=Retinoic acid-induced gene 2 protein;
DE            Short=RAIG-2;
DE   Flags: Precursor;
GN   Name=GPRC5B; Synonyms=RAIG2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=10783259; DOI=10.1006/geno.2000.6164;
RA   Braeuner-Osborne H., Krogsgaard-Larsen P.;
RT   "Sequence and expression pattern of a novel human orphan G-protein-coupled
RT   receptor, GPRC5B, a family C receptor with a short amino-terminal domain.";
RL   Genomics 65:121-128(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, AND INDUCTION.
RX   PubMed=10945465; DOI=10.1006/geno.2000.6226;
RA   Robbins M.J., Michalovich D., Hill J., Calver A.R., Medhurst A.D.,
RA   Gloger I., Sims M.A., Middlemiss D.N., Pangalos M.N.;
RT   "Molecular cloning and characterization of two novel retinoic acid-
RT   inducible orphan G-protein-coupled receptors (GPRC5B and GPRC5C).";
RL   Genomics 67:8-18(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Wei H., Osborne B., Spruyt M., Murphy D.;
RT   "Cloning of a novel G protein-coupled receptor localized on human
RT   chromosome 16p12.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Cool B.H., Chan G.C.K., Lee L., Oshima J., Martin G.M., Hu Q.;
RT   "C-terminal splice variants of Gprc5b, an orphan G protein-coupled receptor
RT   that binds Frizzled Wnt receptors, are expressed in maturing neurons and
RT   influence neurite outgrowth.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA   Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA   Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA   Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA   Adams M.D.;
RT   "Genome duplications and other features in 12 Mb of DNA sequence from human
RT   chromosome 16p and 16q.";
RL   Genomics 60:295-308(1999).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
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).
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.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10945465};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:10945465}. Cytoplasmic
CC       vesicle membrane {ECO:0000269|PubMed:10945465}; Multi-pass membrane
CC       protein {ECO:0000269|PubMed:10945465}. Note=Localized in the plasma
CC       membrane and perinuclear vesicles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NZH0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NZH0-2; Sequence=VSP_047585;
CC   -!- TISSUE SPECIFICITY: Expression is high in kidney, pancreas, and testis,
CC       medium in brain, heart, prostate, small intestine, and spleen, low in
CC       liver, placenta, skeletal muscle, colon, ovary, and thymus, and not
CC       detectable in lung and peripheral leukocyte. According to
CC       PubMed:10945465, highly expressed in most brain areas examined, with
CC       the highest levels observed in corpus callosum, caudate nucleus,
CC       putamen, substantia nigra, thalamus, hippocampus, and spinal cord as
CC       well as in dorsal root ganglia (DRG). In the periphery, expression
CC       levels are relatively low, compared to the CNS, with the strongest
CC       expression detected in pancreas, testis, uterus, and stomach.
CC       {ECO:0000269|PubMed:10783259, ECO:0000269|PubMed:10945465}.
CC   -!- INDUCTION: By all-trans retinoic acid (ATRA).
CC       {ECO:0000269|PubMed:10945465}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AF202640; AAF67321.1; -; mRNA.
DR   EMBL; AJ276101; CAC00632.1; -; mRNA.
DR   EMBL; AF181862; AAF05331.1; -; mRNA.
DR   EMBL; FJ529380; ACU30030.1; -; mRNA.
DR   EMBL; AK075119; BAC11414.1; -; mRNA.
DR   EMBL; AC004131; AAC27544.1; -; Genomic_DNA.
DR   EMBL; AC134300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC034467; AAH34467.1; -; mRNA.
DR   CCDS; CCDS10581.1; -. [Q9NZH0-1]
DR   RefSeq; NP_057319.1; NM_016235.2. [Q9NZH0-1]
DR   RefSeq; XP_006721114.1; XM_006721051.2. [Q9NZH0-1]
DR   RefSeq; XP_006721115.1; XM_006721052.2. [Q9NZH0-1]
DR   AlphaFoldDB; Q9NZH0; -.
DR   SMR; Q9NZH0; -.
DR   BioGRID; 119688; 117.
DR   IntAct; Q9NZH0; 24.
DR   MINT; Q9NZH0; -.
DR   STRING; 9606.ENSP00000300571; -.
DR   ChEMBL; CHEMBL4523926; -.
DR   GlyGen; Q9NZH0; 1 site.
DR   iPTMnet; Q9NZH0; -.
DR   PhosphoSitePlus; Q9NZH0; -.
DR   BioMuta; GPRC5B; -.
DR   DMDM; 46396016; -.
DR   EPD; Q9NZH0; -.
DR   jPOST; Q9NZH0; -.
DR   MassIVE; Q9NZH0; -.
DR   MaxQB; Q9NZH0; -.
DR   PaxDb; Q9NZH0; -.
DR   PeptideAtlas; Q9NZH0; -.
DR   PRIDE; Q9NZH0; -.
DR   ProteomicsDB; 12732; -.
DR   ProteomicsDB; 83386; -. [Q9NZH0-1]
DR   Antibodypedia; 12141; 310 antibodies from 31 providers.
DR   DNASU; 51704; -.
DR   Ensembl; ENST00000300571.7; ENSP00000300571.2; ENSG00000167191.12. [Q9NZH0-1]
DR   Ensembl; ENST00000535671.5; ENSP00000442858.1; ENSG00000167191.12. [Q9NZH0-2]
DR   Ensembl; ENST00000569479.5; ENSP00000454727.1; ENSG00000167191.12. [Q9NZH0-1]
DR   Ensembl; ENST00000569847.1; ENSP00000457283.1; ENSG00000167191.12. [Q9NZH0-1]
DR   GeneID; 51704; -.
DR   KEGG; hsa:51704; -.
DR   MANE-Select; ENST00000300571.7; ENSP00000300571.2; NM_016235.3; NP_057319.1.
DR   UCSC; uc002dgt.4; human. [Q9NZH0-1]
DR   CTD; 51704; -.
DR   DisGeNET; 51704; -.
DR   GeneCards; GPRC5B; -.
DR   HGNC; HGNC:13308; GPRC5B.
DR   HPA; ENSG00000167191; Tissue enriched (brain).
DR   MIM; 605948; gene.
DR   neXtProt; NX_Q9NZH0; -.
DR   OpenTargets; ENSG00000167191; -.
DR   PharmGKB; PA28938; -.
DR   VEuPathDB; HostDB:ENSG00000167191; -.
DR   eggNOG; ENOG502QWT9; Eukaryota.
DR   GeneTree; ENSGT00950000182961; -.
DR   HOGENOM; CLU_044162_1_1_1; -.
DR   InParanoid; Q9NZH0; -.
DR   OMA; RDNKLAC; -.
DR   TreeFam; TF321410; -.
DR   PathwayCommons; Q9NZH0; -.
DR   SignaLink; Q9NZH0; -.
DR   BioGRID-ORCS; 51704; 15 hits in 1086 CRISPR screens.
DR   ChiTaRS; GPRC5B; human.
DR   GeneWiki; GPRC5B; -.
DR   GenomeRNAi; 51704; -.
DR   Pharos; Q9NZH0; Tbio.
DR   PRO; PR:Q9NZH0; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q9NZH0; protein.
DR   Bgee; ENSG00000167191; Expressed in medial globus pallidus and 192 other tissues.
DR   ExpressionAtlas; Q9NZH0; baseline and differential.
DR   Genevisible; Q9NZH0; HS.
DR   GO; GO:0009986; C:cell surface; ISS:CAFA.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0001664; F:G protein-coupled receptor binding; ISS:CAFA.
DR   GO; GO:0030295; F:protein kinase activator activity; IDA:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISS:CAFA.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:CAFA.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:CAFA.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISS:CAFA.
DR   GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISS:CAFA.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:CAFA.
DR   GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:CAFA.
DR   InterPro; IPR017978; GPCR_3_C.
DR   Pfam; PF00003; 7tm_3; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Cytoplasmic vesicle;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..403
FT                   /note="G-protein coupled receptor family C group 5 member
FT                   B"
FT                   /id="PRO_0000012965"
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..162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..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..403
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          349..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q923Z0"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         390..403
FT                   /note="IPTAPPSHTGRHLW -> EMVTHPRSLESFGAF (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_047585"
FT   CONFLICT        46
FT                   /note="V -> A (in Ref. 5; BAC11414)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   403 AA;  44795 MW;  3902A16C4F69C26E CRC64;
     MFVASERKMR AHQVLTFLLL FVITSVASEN ASTSRGCGLD LLPQYVSLCD LDAIWGIVVE
     AVAGAGALIT LLLMLILLVR LPFIKEKEKK SPVGLHFLFL LGTLGLFGLT FAFIIQEDET
     ICSVRRFLWG VLFALCFSCL LSQAWRVRRL VRHGTGPAGW QLVGLALCLM LVQVIIAVEW
     LVLTVLRDTR PACAYEPMDF VMALIYDMVL LVVTLGLALF TLCGKFKRWK LNGAFLLITA
     FLSVLIWVAW MTMYLFGNVK LQQGDAWNDP TLAITLAASG WVFVIFHAIP EIHCTLLPAL
     QENTPNYFDT SQPRMRETAF EEDVQLPRAY MENKAFSMDE HNAALRTAGF PNGSLGKRPS
     GSLGKRPSAP FRSNVYQPTE MAVVLNGGTI PTAPPSHTGR HLW
 
 
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