ID GPHRB_HUMAN Reviewed; 455 AA. AC P0CG08; A6NKF9; A6NN37; B2RUV3; B3KMN3; Q53FQ9; Q5T2V8; Q5T5P5; Q659E2; AC Q6NVY5; Q9P0S4; Q9Y302; DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot. DT 15-JUN-2010, sequence version 1. DT 02-OCT-2024, entry version 94. DE RecName: Full=Golgi pH regulator B {ECO:0000305}; DE AltName: Full=Protein GPR89B; GN Name=GPR89B {ECO:0000312|HGNC:HGNC:13840}; GN Synonyms=GPHR {ECO:0000303|PubMed:18794847}, GPR89 GN {ECO:0000303|PubMed:19135895}, GPR89C, SH120 {ECO:0000303|Ref.1}; GN ORFNames=HSPC201; 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=Ovary; RA Lee P.L., Gelbart T., West C., Adams M., Blackstone R., Meyer A.; RT "Identification of 15 genes mapping to chromosome 6p21.3 spanning the RT microsatellite markers D6S306 and D6S1260. Characterization of three genes RT encoding zinc finger proteins."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-247. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 249-455. RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [5] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE RP SPECIFICITY. RX PubMed=18794847; DOI=10.1038/ncb1773; RA Maeda Y., Ide T., Koike M., Uchiyama Y., Kinoshita T.; RT "GPHR is a novel anion channel critical for acidification and functions of RT the Golgi apparatus."; RL Nat. Cell Biol. 10:1135-1145(2008). RN [6] RP LACK OF GTP-BINDING. RX PubMed=19135895; DOI=10.1016/j.cell.2008.12.026; RA Pandey S., Nelson D.C., Assmann S.M.; RT "Two novel GPCR-type G proteins are abscisic acid receptors in RT Arabidopsis."; RL Cell 136:136-148(2009). CC -!- FUNCTION: Voltage-gated channel that enables the transfer of anions CC such as iodide, chloride, bromide and fluoride which may function in CC counter-ion conductance and participates in Golgi acidification CC (PubMed:18794847). Plays a role in lymphocyte development, probably by CC acting as a RABL3 effector in hematopoietic cells (By similarity). CC {ECO:0000250|UniProtKB:Q8BS95, ECO:0000269|PubMed:18794847}. CC -!- CATALYTIC ACTIVITY: CC Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324, CC ChEBI:CHEBI:16382; Evidence={ECO:0000269|PubMed:18794847}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:18794847}; CC -!- CATALYTIC ACTIVITY: CC Reaction=bromide(in) = bromide(out); Xref=Rhea:RHEA:75383, CC ChEBI:CHEBI:15858; Evidence={ECO:0000269|PubMed:18794847}; CC -!- CATALYTIC ACTIVITY: CC Reaction=fluoride(in) = fluoride(out); Xref=Rhea:RHEA:76159, CC ChEBI:CHEBI:17051; Evidence={ECO:0000269|PubMed:18794847}; CC -!- SUBUNIT: Homotrimer (PubMed:18794847). Interacts with RABL3; the CC interaction stabilizes GPR89B (By similarity). CC {ECO:0000250|UniProtKB:Q8BS95, ECO:0000269|PubMed:18794847}. CC -!- INTERACTION: CC P0CG08; O76024: WFS1; NbExp=3; IntAct=EBI-11905631, EBI-720609; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:18794847}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18794847}. CC -!- MISCELLANEOUS: Does not seem to be able to bind GTP. CC {ECO:0000269|PubMed:19135895}. CC -!- SIMILARITY: Belongs to the Golgi pH regulator (TC 1.A.38) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF36121.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U78723; AAF21463.1; -; mRNA. DR EMBL; AL356004; CAI17085.1; -; Genomic_DNA. DR EMBL; AL445591; CAH72386.1; -; Genomic_DNA. DR EMBL; BX537254; CAH72386.1; JOINED; Genomic_DNA. DR EMBL; BX537254; CAI18821.1; -; Genomic_DNA. DR EMBL; AL445591; CAI18821.1; JOINED; Genomic_DNA. DR EMBL; AL133020; CAH56393.1; -; mRNA. DR EMBL; AF151035; AAF36121.1; ALT_SEQ; mRNA. DR CCDS; CCDS930.1; -. DR RefSeq; NP_001091081.1; NM_001097612.1. DR RefSeq; NP_057418.1; NM_016334.3. DR RefSeq; XP_005277458.1; XM_005277401.3. DR RefSeq; XP_006711555.1; XM_006711492.3. DR RefSeq; XP_011507915.1; XM_011509613.2. DR RefSeq; XP_011508212.1; XM_011509910.2. DR AlphaFoldDB; P0CG08; -. DR SMR; P0CG08; -. DR BioGRID; 119554; 50. DR BioGRID; 575849; 132. DR IntAct; P0CG08; 31. DR MINT; P0CG08; -. DR GlyCosmos; P0CG08; 2 sites, No reported glycans. DR GlyGen; P0CG08; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; P0CG08; -. DR PhosphoSitePlus; P0CG08; -. DR SwissPalm; P0CG08; -. DR BioMuta; GPR89B; -. DR DMDM; 298351693; -. DR jPOST; P0CG08; -. DR MassIVE; P0CG08; -. DR PeptideAtlas; P0CG08; -. DR Pumba; P0CG08; -. DR Antibodypedia; 65496; 58 antibodies from 15 providers. DR DNASU; 51463; -. DR Ensembl; ENST00000314163.12; ENSP00000358233.4; ENSG00000188092.15. DR GeneID; 51463; -. DR GeneID; 653519; -. DR KEGG; hsa:51463; -. DR KEGG; hsa:653519; -. DR MANE-Select; ENST00000314163.12; ENSP00000358233.4; NM_016334.5; NP_057418.1. DR AGR; HGNC:13840; -. DR AGR; HGNC:31984; -. DR CTD; 51463; -. DR CTD; 653519; -. DR DisGeNET; 653519; -. DR GeneCards; GPR89B; -. DR HGNC; HGNC:13840; GPR89B. DR HPA; ENSG00000188092; Low tissue specificity. DR MIM; 612806; gene. DR neXtProt; NX_P0CG08; -. DR PharmGKB; PA134986137; -. DR VEuPathDB; HostDB:ENSG00000188092; -. DR GeneTree; ENSGT00390000000684; -. DR HOGENOM; CLU_030540_1_0_1; -. DR InParanoid; P0CG08; -. DR OMA; IEIGVHW; -. DR OrthoDB; 90523at2759; -. DR PhylomeDB; P0CG08; -. DR TreeFam; TF313484; -. DR PathwayCommons; P0CG08; -. DR SignaLink; P0CG08; -. DR BioGRID-ORCS; 51463; 102 hits in 680 CRISPR screens. DR BioGRID-ORCS; 653519; 250 hits in 1041 CRISPR screens. DR Pharos; P0CG08; Tbio. DR PRO; PR:P0CG08; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P0CG08; protein. DR Bgee; ENSG00000188092; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 100 other cell types or tissues. DR ExpressionAtlas; P0CG08; baseline and differential. DR GO; GO:0032580; C:Golgi cisterna membrane; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW. DR GO; GO:0008308; F:voltage-gated monoatomic anion channel activity; IBA:GO_Central. DR GO; GO:0051452; P:intracellular pH reduction; IBA:GO_Central. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB. DR InterPro; IPR025969; ABA_GPCR_dom. DR InterPro; IPR022535; Golgi_pH-regulator_cons_dom. DR InterPro; IPR015672; GPHR/GTG. DR PANTHER; PTHR15948; G-PROTEIN COUPLED RECEPTOR 89-RELATED; 1. DR PANTHER; PTHR15948:SF0; GOLGI PH REGULATOR A-RELATED; 1. DR Pfam; PF12430; ABA_GPCR; 1. DR Pfam; PF12537; GPHR_N; 1. PE 1: Evidence at protein level; KW Glycoprotein; Golgi apparatus; Ion channel; Ion transport; Membrane; KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix; KW Transport; Voltage-gated channel. FT CHAIN 1..455 FT /note="Golgi pH regulator B" FT /id="PRO_0000395006" FT TRANSMEM 5..25 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 46..66 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 79..99 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 114..134 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 150..170 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 290..310 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 343..363 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 378..398 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 425..445 FT /note="Helical" FT /evidence="ECO:0000255" FT CARBOHYD 180 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 243 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 244..247 FT /note="LTLI -> NTMA (in Ref. 3; CAH56393)" FT /evidence="ECO:0000305" FT CONFLICT 251 FT /note="V -> E (in Ref. 4; AAF36121)" FT /evidence="ECO:0000305" FT CONFLICT 418 FT /note="Q -> R (in Ref. 4; AAF36121)" FT /evidence="ECO:0000305" SQ SEQUENCE 455 AA; 52917 MW; D831F66E682643F9 CRC64; MSFLIDSSIM ITSQILFFGF GWLFFMRQLF KDYEIRQYVV QVIFSVTFAF SCTMFELIIF EILGVLNSSS RYFHWKMNLC VILLILVFMV PFYIGYFIVS NIRLLHKQRL LFSCLLWLTF MYFFWKLGDP FPILSPKHGI LSIEQLISRV GVIGVTLMAL LSGFGAVNCP YTYMSYFLRN VTDTDILALE RRLLQTMDMI ISKKKRMAMA RRTMFQKGEV HNKPSGFWGM IKSVTTSASG SENLTLIQQE VDALEELSRQ LFLETADLYA TKERIEYSKT FKGKYFNFLG YFFSIYCVWK IFMATINIVF DRVGKTDPVT RGIEITVNYL GIQFDVKFWS QHISFILVGI IIVTSIRGLL ITLTKFFYAI SSSKSSNVIV LLLAQIMGMY FVSSVLLIRM SMPLEYRTII TEVLGELQFN FYHRWFDVIF LVSALSSILF LYLAHKQAPE KQMAP //