ID   GPR34_HUMAN             Reviewed;         381 AA.
AC   Q9UPC5; O95853;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 2.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Probable G-protein coupled receptor 34;
GN   Name=GPR34;
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].
RC   TISSUE=Fetal brain;
RX   PubMed=10395919; DOI=10.1016/s0167-4781(99)00081-0;
RA   Schoneberg T., Schulz A., Grosse R., Schade R., Henklein P., Schultz G.,
RA   Gudermann T.;
RT   "A novel subgroup of class I G-protein-coupled receptors.";
RL   Biochim. Biophys. Acta 1446:57-70(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10036181; DOI=10.1006/geno.1998.5655;
RA   Marchese A., Sawzdargo M., Nguyen T., Cheng R., Heng H.H.Q., Nowak T.,
RA   Im D.-S., Lynch K.R., George S.R., O'Dowd B.F.;
RT   "Discovery of three novel orphan G-protein-coupled receptors.";
RL   Genomics 56:12-21(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10982042; DOI=10.1007/s004390000337;
RA   Jacobi F.K., Broghammer M., Pesch K., Zrenner E., Berger W., Meindl A.,
RA   Pusch C.M.;
RT   "Physical mapping and exclusion of GPR34 as the causative gene for
RT   congenital stationary night blindness type 1.";
RL   Hum. Genet. 107:89-91(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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=16460680; DOI=10.1016/j.bbrc.2006.01.069;
RA   Sugo T., Tachimoto H., Chikatsu T., Murakami Y., Kikukawa Y., Sato S.,
RA   Kikuchi K., Nagi T., Harada M., Ogi K., Ebisawa M., Mori M.;
RT   "Identification of a lysophosphatidylserine receptor on mast cells.";
RL   Biochem. Biophys. Res. Commun. 341:1078-1087(2006).
RN   [7]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=27086875; DOI=10.1016/j.bbamcr.2016.04.010;
RA   Hasegawa H., Patel N., Ettehadieh E., Li P., Lim A.C.;
RT   "Topogenesis and cell surface trafficking of GPR34 are facilitated by
RT   positive-inside rule that effects through a tri-basic motif in the first
RT   intracellular loop.";
RL   Biochim. Biophys. Acta 1863:1534-1551(2016).
CC   -!- FUNCTION: G-protein-coupled receptor of lysophosphatidylserine (LysoPS)
CC       that plays different roles in immune response (PubMed:16460680). Acts a
CC       damage-sensing receptor that triggers tissue repair upon recognition of
CC       dying neutrophils (By similarity). Mechanistically, apoptotic
CC       neutrophils release lysophosphatydilserine that are recognized by type
CC       3 innate lymphoid cells (ILC3s) via GPR34, which activates downstream
CC       PI3K-AKT and RAS-ERK signaling pathways leading to STAT3 activation and
CC       IL-22 production (By similarity). Plays an important role in microglial
CC       function, controlling morphology and phagocytosis (By similarity).
CC       {ECO:0000250|UniProtKB:Q9R1K6, ECO:0000269|PubMed:16460680}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27086875};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:27086875}.
CC   -!- TISSUE SPECIFICITY: Broadly expressed. Highly expressed on mast cells
CC       (PubMed:16460680). {ECO:0000269|PubMed:16460680}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF039686; AAD50531.1; -; mRNA.
DR   EMBL; AF118670; AAD17248.1; -; Genomic_DNA.
DR   EMBL; AK027780; BAB55362.1; -; mRNA.
DR   EMBL; BC020678; AAH20678.1; -; mRNA.
DR   CCDS; CCDS14258.1; -.
DR   RefSeq; NP_001091048.1; NM_001097579.1.
DR   RefSeq; NP_005291.1; NM_005300.3.
DR   RefSeq; XP_005272654.1; XM_005272597.3.
DR   PDB; 8K4N; EM; 2.83 A; D=49-327.
DR   PDB; 8SAI; EM; 3.27 A; A=38-373.
DR   PDB; 8WRB; EM; 2.91 A; R=1-344.
DR   PDBsum; 8K4N; -.
DR   PDBsum; 8SAI; -.
DR   PDBsum; 8WRB; -.
DR   AlphaFoldDB; Q9UPC5; -.
DR   EMDB; EMD-36887; -.
DR   EMDB; EMD-37771; -.
DR   EMDB; EMD-40270; -.
DR   SMR; Q9UPC5; -.
DR   BioGRID; 109115; 16.
DR   IntAct; Q9UPC5; 1.
DR   STRING; 9606.ENSP00000367384; -.
DR   BindingDB; Q9UPC5; -.
DR   ChEMBL; CHEMBL3562165; -.
DR   GuidetoPHARMACOLOGY; 101; -.
DR   GlyCosmos; Q9UPC5; 5 sites, No reported glycans.
DR   GlyGen; Q9UPC5; 5 sites.
DR   iPTMnet; Q9UPC5; -.
DR   PhosphoSitePlus; Q9UPC5; -.
DR   BioMuta; GPR34; -.
DR   DMDM; 12643337; -.
DR   jPOST; Q9UPC5; -.
DR   MassIVE; Q9UPC5; -.
DR   PaxDb; 9606-ENSP00000367384; -.
DR   PeptideAtlas; Q9UPC5; -.
DR   ProteomicsDB; 85365; -.
DR   Antibodypedia; 547; 331 antibodies from 30 providers.
DR   DNASU; 2857; -.
DR   Ensembl; ENST00000378138.5; ENSP00000367378.5; ENSG00000171659.16.
DR   Ensembl; ENST00000378142.9; ENSP00000367384.4; ENSG00000171659.16.
DR   Ensembl; ENST00000649219.1; ENSP00000498130.1; ENSG00000171659.16.
DR   GeneID; 2857; -.
DR   KEGG; hsa:2857; -.
DR   MANE-Select; ENST00000378142.9; ENSP00000367384.4; NM_001097579.2; NP_001091048.1.
DR   UCSC; uc004dfp.4; human.
DR   AGR; HGNC:4490; -.
DR   CTD; 2857; -.
DR   DisGeNET; 2857; -.
DR   GeneCards; GPR34; -.
DR   HGNC; HGNC:4490; GPR34.
DR   HPA; ENSG00000171659; Tissue enhanced (placenta).
DR   MIM; 300241; gene.
DR   neXtProt; NX_Q9UPC5; -.
DR   OpenTargets; ENSG00000171659; -.
DR   PharmGKB; PA28878; -.
DR   VEuPathDB; HostDB:ENSG00000171659; -.
DR   eggNOG; ENOG502QT81; Eukaryota.
DR   GeneTree; ENSGT01060000248589; -.
DR   InParanoid; Q9UPC5; -.
DR   OMA; IIHKCNE; -.
DR   OrthoDB; 3875139at2759; -.
DR   PhylomeDB; Q9UPC5; -.
DR   TreeFam; TF330969; -.
DR   PathwayCommons; Q9UPC5; -.
DR   SignaLink; Q9UPC5; -.
DR   SIGNOR; Q9UPC5; -.
DR   BioGRID-ORCS; 2857; 20 hits in 766 CRISPR screens.
DR   ChiTaRS; GPR34; human.
DR   GenomeRNAi; 2857; -.
DR   Pharos; Q9UPC5; Tchem.
DR   PRO; PR:Q9UPC5; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9UPC5; Protein.
DR   Bgee; ENSG00000171659; Expressed in calcaneal tendon and 149 other cell types or tissues.
DR   ExpressionAtlas; Q9UPC5; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR   GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   CDD; cd15148; 7tmA_GPR34-like; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR048057; GPR34_7tmA.
DR   PANTHER; PTHR24233:SF1; G-PROTEIN COUPLED RECEPTOR 34-RELATED; 1.
DR   PANTHER; PTHR24233; P2Y PURINOCEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01157; P2YPURNOCPTR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q9UPC5; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..381
FT                   /note="Probable G-protein coupled receptor 34"
FT                   /id="PRO_0000069559"
FT   TOPO_DOM        1..61
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TRANSMEM        62..82
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TOPO_DOM        83..88
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TRANSMEM        89..109
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TOPO_DOM        110..128
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TRANSMEM        129..149
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TOPO_DOM        150..171
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TRANSMEM        172..192
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TOPO_DOM        193..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TRANSMEM        217..237
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TOPO_DOM        238..269
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TRANSMEM        270..290
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TOPO_DOM        291..310
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TRANSMEM        311..331
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   TOPO_DOM        332..381
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:27086875"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        127..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        181
FT                   /note="L -> V (in Ref. 1; AAD50531)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  43860 MW;  491FC016E5624379 CRC64;
     MRSHTITMTT TSVSSWPYSS HRMRFITNHS DQPPQNFSAT PNVTTCPMDE KLLSTVLTTS
     YSVIFIVGLV GNIIALYVFL GIHRKRNSIQ IYLLNVAIAD LLLIFCLPFR IMYHINQNKW
     TLGVILCKVV GTLFYMNMYI SIILLGFISL DRYIKINRSI QQRKAITTKQ SIYVCCIVWM
     LALGGFLTMI ILTLKKGGHN STMCFHYRDK HNAKGEAIFN FILVVMFWLI FLLIILSYIK
     IGKNLLRISK RRSKFPNSGK YATTARNSFI VLIIFTICFV PYHAFRFIYI SSQLNVSSCY
     WKEIVHKTNE IMLVLSSFNS CLDPVMYFLM SSNIRKIMCQ LLFRRFQGEP SRSESTSEFK
     PGYSLHDTSV AVKIQSSSKS T
//