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GPR75_MOUSE
ID   GPR75_MOUSE             Reviewed;         540 AA.
AC   Q6X632; Q3URC1; Q8BXP3;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Probable G-protein coupled receptor 75;
GN   Name=Gpr75;
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], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Brain;
RX   PubMed=17001303; DOI=10.1038/sj.bjp.0706909;
RA   Ignatov A., Robert J., Gregory-Evans C., Schaller H.C.;
RT   "RANTES stimulates Ca2+ mobilization and inositol trisphosphate (IP3)
RT   formation in cells transfected with G protein-coupled receptor 75.";
RL   Br. J. Pharmacol. 149:490-497(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Retina;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=23979485; DOI=10.1007/s00125-013-3022-x;
RA   Liu B., Hassan Z., Amisten S., King A.J., Bowe J.E., Huang G.C.,
RA   Jones P.M., Persaud S.J.;
RT   "The novel chemokine receptor, G-protein-coupled receptor 75, is expressed
RT   by islets and is coupled to stimulation of insulin secretion and improved
RT   glucose homeostasis.";
RL   Diabetologia 56:2467-2476(2013).
CC   -!- FUNCTION: G protein-coupled receptor that is activated by the chemokine
CC       CCL5/RANTES. Probably coupled to heterotrimeric Gq proteins, it
CC       stimulates inositol trisphosphate production and calcium mobilization
CC       upon activation. Together with CCL5/RANTES, may play a role in neuron
CC       survival through activation of a downstream signaling pathway involving
CC       the PI3, Akt and MAP kinases. CCL5/RANTES may also regulate insulin
CC       secretion by pancreatic islet cells through activation of this
CC       receptor. {ECO:0000269|PubMed:17001303, ECO:0000303|PubMed:23979485}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:17001303}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and heart. Also detected
CC       in skeletal muscle, liver and kidney. Also expressed by islet cells (at
CC       protein level). {ECO:0000269|PubMed:17001303,
CC       ECO:0000269|PubMed:23979485}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 7 dpc and 11 dpc. Also detected at 17
CC       dpc. {ECO:0000269|PubMed:17001303}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31978.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY253852; AAP83130.1; -; mRNA.
DR   EMBL; AK044553; BAC31978.1; ALT_INIT; mRNA.
DR   EMBL; AK141614; BAE24767.1; -; mRNA.
DR   EMBL; AL662891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS24508.1; -.
DR   RefSeq; NP_780699.2; NM_175490.4.
DR   RefSeq; XP_006514759.1; XM_006514696.3.
DR   AlphaFoldDB; Q6X632; -.
DR   SMR; Q6X632; -.
DR   STRING; 10090.ENSMUSP00000105057; -.
DR   GlyGen; Q6X632; 3 sites.
DR   iPTMnet; Q6X632; -.
DR   PhosphoSitePlus; Q6X632; -.
DR   PaxDb; Q6X632; -.
DR   PRIDE; Q6X632; -.
DR   Antibodypedia; 15401; 412 antibodies from 32 providers.
DR   DNASU; 237716; -.
DR   Ensembl; ENSMUST00000109430; ENSMUSP00000105057; ENSMUSG00000043999.
DR   GeneID; 237716; -.
DR   KEGG; mmu:237716; -.
DR   UCSC; uc007iib.2; mouse.
DR   CTD; 10936; -.
DR   MGI; MGI:2441843; Gpr75.
DR   VEuPathDB; HostDB:ENSMUSG00000043999; -.
DR   eggNOG; ENOG502QVED; Eukaryota.
DR   GeneTree; ENSGT00390000007723; -.
DR   HOGENOM; CLU_041999_0_0_1; -.
DR   InParanoid; Q6X632; -.
DR   OMA; GHQHYGQ; -.
DR   OrthoDB; 1363902at2759; -.
DR   PhylomeDB; Q6X632; -.
DR   TreeFam; TF331523; -.
DR   BioGRID-ORCS; 237716; 2 hits in 71 CRISPR screens.
DR   PRO; PR:Q6X632; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q6X632; protein.
DR   Bgee; ENSMUSG00000043999; Expressed in lumbar dorsal root ganglion and 77 other tissues.
DR   ExpressionAtlas; Q6X632; baseline and differential.
DR   Genevisible; Q6X632; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IC:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016493; F:C-C chemokine receptor activity; IDA:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:1901214; P:regulation of neuron death; IDA:UniProtKB.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..540
FT                   /note="Probable G-protein coupled receptor 75"
FT                   /id="PRO_0000069584"
FT   TOPO_DOM        1..46
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..120
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..160
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..318
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        340..350
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..371
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        372..540
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          443..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        476
FT                   /note="N -> D (in Ref. 2; BAC31978)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   540 AA;  59531 MW;  E8704067FCC70E69 CRC64;
     MNTSAPLQNV PNATLLNMPP LHGGNSTSLQ EGLRDFIHTA TLVTCTFLLA IIFCLGSYGN
     FIVFLSFFDP SFRKFRTNFD FMILNLSFCD LFICGVTAPM FTFVLFFSSA SSIPDSFCFT
     FHLTSSGFVI MSLKMVAVIA LHRLRMVMGK QPNCTASFSC ILLLTLLLWA TSFTLATLAT
     LRTNKSHLCL PMSSLMDGEG KAILSLYVVD FTFCVAVVSV SYIMIAQTLR KNAQVKKCPP
     VITVDASRPQ PFMGASVKGN GDPIQCTMPA LYRNQNYNKL QHSQTHGYTK NINQMPIPSA
     SRLQLVSAIN FSTAKDSKAV VTCVVIVLSV LVCCLPLGIS LVQMVLSDNG SFILYQFELF
     GFTLIFFKSG LNPFIYSRNS AGLRRKVLWC LRYTGLGFLC CKQKTRLRAM GKGNLEINRN
     KSSHHETNSA YMLSPKPQRK FVDQACGPSH SKESAASPKV SAGHQPCGQS SSTPINTRIE
     PYYSIYNSSP SQQESGPANL PPVNSFGFAS SYIAMHYYTT NDLMQEYDST SAKQIPIPSV
 
 
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