GPR75_HUMAN
ID GPR75_HUMAN Reviewed; 540 AA.
AC O95800; B2RC02; Q6NWR2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable G-protein coupled receptor 75;
GN Name=GPR75;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=10381362; DOI=10.1006/bbrc.1999.0753;
RA Tarttelin E.E., Kirschner L.S., Bellingham J., Baffi J., Taymans S.E.,
RA Gregory-Evans K., Csaky K., Stratakis C.A., Gregory-Evans C.Y.;
RT "Cloning and characterization of a novel orphan G-protein-coupled receptor
RT localized to human chromosome 2p16.";
RL Biochem. Biophys. Res. Commun. 260:174-180(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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).
RN [7]
RP VARIANTS LYS-78; LEU-99; THR-108; THR-116 AND PRO-135, AND TISSUE
RP SPECIFICITY.
RX PubMed=11466257; DOI=10.1136/bjo.85.8.969;
RA Sauer C.G., White K., Stohr H., Grimm T., Hutchinson A., Bernstein P.S.,
RA Lewis R.A., Simonelli F., Pauleikhoff D., Allikmets R., Weber B.H.;
RT "Evaluation of the G protein coupled receptor-75 (GPR75) in age related
RT macular degeneration.";
RL Br. J. Ophthalmol. 85:969-975(2001).
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:0000250|UniProtKB:Q6X632, ECO:0000303|PubMed:23979485}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain and spinal cord
CC and at detectable levels in retinal pigment epithelium. In situ
CC hybridization of adult eye sections localized transcripts only to the
CC perivascular cells, surrounding retinal arterioles, in the ganglion
CC cell/nerve fiber layer. Also expressed by islet cells (at protein
CC level). {ECO:0000269|PubMed:10381362, ECO:0000269|PubMed:11466257,
CC ECO:0000269|PubMed:23979485}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF072693; AAD19849.1; -; mRNA.
DR EMBL; AF101472; AAD22770.1; -; Genomic_DNA.
DR EMBL; AK314885; BAG37399.1; -; mRNA.
DR EMBL; AC008068; AAY15018.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00162.1; -; Genomic_DNA.
DR EMBL; BC067475; AAH67475.1; -; mRNA.
DR EMBL; BC067476; AAH67476.1; -; mRNA.
DR CCDS; CCDS1849.1; -.
DR RefSeq; NP_006785.1; NM_006794.3.
DR AlphaFoldDB; O95800; -.
DR SMR; O95800; -.
DR STRING; 9606.ENSP00000378195; -.
DR ChEMBL; CHEMBL4523861; -.
DR GuidetoPHARMACOLOGY; 115; -.
DR GlyGen; O95800; 3 sites.
DR iPTMnet; O95800; -.
DR PhosphoSitePlus; O95800; -.
DR BioMuta; GPR75; -.
DR PaxDb; O95800; -.
DR PeptideAtlas; O95800; -.
DR PRIDE; O95800; -.
DR Antibodypedia; 15401; 412 antibodies from 32 providers.
DR DNASU; 10936; -.
DR Ensembl; ENST00000394705.3; ENSP00000378195.2; ENSG00000119737.6.
DR GeneID; 10936; -.
DR KEGG; hsa:10936; -.
DR MANE-Select; ENST00000394705.3; ENSP00000378195.2; NM_006794.4; NP_006785.1.
DR UCSC; uc002rxo.4; human.
DR CTD; 10936; -.
DR DisGeNET; 10936; -.
DR GeneCards; GPR75; -.
DR HGNC; HGNC:4526; GPR75.
DR HPA; ENSG00000119737; Group enriched (brain, retina).
DR MIM; 606704; gene.
DR neXtProt; NX_O95800; -.
DR OpenTargets; ENSG00000119737; -.
DR PharmGKB; PA28919; -.
DR VEuPathDB; HostDB:ENSG00000119737; -.
DR eggNOG; ENOG502QVED; Eukaryota.
DR GeneTree; ENSGT00390000007723; -.
DR HOGENOM; CLU_041999_0_0_1; -.
DR InParanoid; O95800; -.
DR OMA; GHQHYGQ; -.
DR OrthoDB; 1363902at2759; -.
DR PhylomeDB; O95800; -.
DR TreeFam; TF331523; -.
DR PathwayCommons; O95800; -.
DR BioGRID-ORCS; 10936; 11 hits in 1068 CRISPR screens.
DR GeneWiki; GPR75; -.
DR GenomeRNAi; 10936; -.
DR Pharos; O95800; Tbio.
DR PRO; PR:O95800; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O95800; protein.
DR Bgee; ENSG00000119737; Expressed in ventricular zone and 98 other tissues.
DR Genevisible; O95800; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016493; F:C-C chemokine receptor activity; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1901214; P:regulation of neuron death; ISS: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_0000069583"
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 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 78
FT /note="N -> K (found in a patient with age-related macular
FT degeneration; unknown pathological significance;
FT dbSNP:rs72799238)"
FT /evidence="ECO:0000269|PubMed:11466257"
FT /id="VAR_071258"
FT VARIANT 99
FT /note="P -> L (found in a patient with age-related macular
FT degeneration; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:11466257"
FT /id="VAR_071259"
FT VARIANT 108
FT /note="S -> T (found in a patient with age-related macular
FT degeneration; unknown pathological significance;
FT dbSNP:rs763005023)"
FT /evidence="ECO:0000269|PubMed:11466257"
FT /id="VAR_071260"
FT VARIANT 116
FT /note="A -> T (in dbSNP:rs34000641)"
FT /evidence="ECO:0000269|PubMed:11466257"
FT /id="VAR_033471"
FT VARIANT 135
FT /note="T -> P (found in a patient with age-related macular
FT degeneration; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:11466257"
FT /id="VAR_071261"
FT VARIANT 160
FT /note="C -> G (in dbSNP:rs35349235)"
FT /id="VAR_033472"
FT VARIANT 433
FT /note="L -> V (in dbSNP:rs3731969)"
FT /id="VAR_033473"
FT CONFLICT 175
FT /note="L -> P (in Ref. 5; AAH67475)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="N -> D (in Ref. 5; AAH67475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 59359 MW; B5BE87BB384190EE CRC64;
MNSTGHLQDA PNATSLHVPH SQEGNSTSLQ EGLQDLIHTA TLVTCTFLLA VIFCLGSYGN
FIVFLSFFDP AFRKFRTNFD FMILNLSFCD LFICGVTAPM FTFVLFFSSA SSIPDAFCFT
FHLTSSGFII MSLKTVAVIA LHRLRMVLGK QPNRTASFPC TVLLTLLLWA TSFTLATLAT
LKTSKSHLCL PMSSLIAGKG KAILSLYVVD FTFCVAVVSV SYIMIAQTLR KNAQVRKCPP
VITVDASRPQ PFMGVPVQGG GDPIQCAMPA LYRNQNYNKL QHVQTRGYTK SPNQLVTPAA
SRLQLVSAIN LSTAKDSKAV VTCVIIVLSV LVCCLPLGIS LVQVVLSSNG SFILYQFELF
GFTLIFFKSG LNPFIYSRNS AGLRRKVLWC LQYIGLGFFC CKQKTRLRAM GKGNLEVNRN
KSSHHETNSA YMLSPKPQKK FVDQACGPSH SKESMVSPKI SAGHQHCGQS SSTPINTRIE
PYYSIYNSSP SQEESSPCNL QPVNSFGFAN SYIAMHYHTT NDLVQEYDST SAKQIPVPSV
