GPHRB_HUMAN
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 03-AUG-2022, entry version 82.
DE RecName: Full=Golgi pH regulator B;
DE AltName: Full=Protein GPR89B;
GN Name=GPR89B; Synonyms=GPHRB, GPR89C; 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, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE 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 dependent anion channel required for acidification
CC and functions of the Golgi apparatus that may function in counter-ion
CC conductance (PubMed:18794847). Plays a role in lymphocyte development,
CC probably by acting as a RABL3 effector in hematopoietic cells (By
CC similarity). {ECO:0000250|UniProtKB:Q8BS95,
CC 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:0000250|UniProtKB:B2ZXD5}; 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 -!- 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; 33.
DR BioGRID; 575849; 126.
DR IntAct; P0CG08; 16.
DR MINT; P0CG08; -.
DR GlyGen; P0CG08; 2 sites.
DR iPTMnet; P0CG08; -.
DR PhosphoSitePlus; P0CG08; -.
DR SwissPalm; P0CG08; -.
DR BioMuta; GPR89B; -.
DR DMDM; 298351693; -.
DR EPD; P0CG08; -.
DR jPOST; P0CG08; -.
DR MassIVE; P0CG08; -.
DR PeptideAtlas; P0CG08; -.
DR PRIDE; P0CG08; -.
DR Antibodypedia; 65496; 54 antibodies from 13 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; ENST00000313835.14; ENSP00000319673.9; NM_001097612.2; NP_001091081.1.
DR MANE-Select; ENST00000314163.12; ENSP00000358233.4; NM_016334.5; NP_057418.1.
DR CTD; 51463; -.
DR CTD; 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; 1065554at2759; -.
DR PhylomeDB; P0CG08; -.
DR TreeFam; TF313484; -.
DR PathwayCommons; P0CG08; -.
DR SignaLink; P0CG08; -.
DR BioGRID-ORCS; 51463; 94 hits in 629 CRISPR screens.
DR BioGRID-ORCS; 653519; 244 hits in 988 CRISPR screens.
DR Pharos; P0CG08; Tbio.
DR PRO; PR:P0CG08; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P0CG08; protein.
DR Bgee; ENSG00000188092; Expressed in duodenum and 99 other tissues.
DR ExpressionAtlas; P0CG08; baseline and differential.
DR Genevisible; P0CG08; HS.
DR GO; GO:0032580; C:Golgi cisterna membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008308; F:voltage-gated 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:0034765; P:regulation of ion transmembrane 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; PTHR15948; 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
