GPHR_BOVIN
ID GPHR_BOVIN Reviewed; 455 AA.
AC Q5BIM9; Q0VCS7;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Golgi pH regulator;
DE AltName: Full=Protein GPR89;
GN Name=GPR89; Synonyms=GPHR, GPR89A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Voltage dependent anion channel required for acidification
CC and functions of the Golgi apparatus that may function in counter-ion
CC conductance (By similarity). Plays a role in lymphocyte development,
CC probably by acting as a RABL3 effector in hematopoietic cells (By
CC similarity). {ECO:0000250|UniProtKB:B2ZXD5,
CC ECO:0000250|UniProtKB:Q8BS95}.
CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with RABL3; the
CC interaction stabilizes GPR89 (By similarity).
CC {ECO:0000250|UniProtKB:B7ZAQ6, ECO:0000250|UniProtKB:Q8BS95}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:B2ZXD5}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5BIM9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BIM9-2; Sequence=VSP_039345;
CC -!- SIMILARITY: Belongs to the Golgi pH regulator (TC 1.A.38) family.
CC {ECO:0000305}.
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DR EMBL; BT021195; AAX31377.1; -; mRNA.
DR EMBL; BT021606; AAX46453.1; -; mRNA.
DR EMBL; BC120025; AAI20026.1; -; mRNA.
DR RefSeq; NP_001070438.1; NM_001076970.1. [Q5BIM9-2]
DR AlphaFoldDB; Q5BIM9; -.
DR SMR; Q5BIM9; -.
DR STRING; 9913.ENSBTAP00000043069; -.
DR PaxDb; Q5BIM9; -.
DR PRIDE; Q5BIM9; -.
DR Ensembl; ENSBTAT00000007637; ENSBTAP00000007637; ENSBTAG00000005809. [Q5BIM9-2]
DR GeneID; 767859; -.
DR KEGG; bta:767859; -.
DR CTD; 653519; -.
DR VEuPathDB; HostDB:ENSBTAG00000005809; -.
DR eggNOG; KOG2417; Eukaryota.
DR GeneTree; ENSGT00390000000684; -.
DR InParanoid; Q5BIM9; -.
DR OrthoDB; 1065554at2759; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000005809; Expressed in caput epididymis and 106 other tissues.
DR ExpressionAtlas; Q5BIM9; baseline and differential.
DR GO; GO:0032580; C:Golgi cisterna membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008308; F:voltage-gated anion channel activity; ISS:UniProtKB.
DR GO; GO:0051452; P:intracellular pH reduction; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Golgi apparatus; Ion channel;
KW Ion transport; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..455
FT /note="Golgi pH regulator"
FT /id="PRO_0000223259"
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 VAR_SEQ 304..335
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752, ECO:0000303|Ref.2"
FT /id="VSP_039345"
SQ SEQUENCE 455 AA; 52952 MW; 604C01CDC82B549E CRC64;
MSFLIDSSIM ITSQILFFGF GWLFFMRQLF KDYEVRQYVV QVIFSVTFAF SCTMFELIIF
EILGVLNSSS RYFHWKMNLC VILLILVFMV PFYIGYFIVS NIRLLHKQRL LFSCLLWLTF
MYFFWKLGDP FPILSPKHGI LSIEQLISRV GVIGVTLMAL LSGFGAVNCP YTYMSYFLRN
VTDTDILALE RRLLQTMDMI ISKKKRMAMT RRTMFQKGEV HNKPSGFWGM IKSVTTSAPG
SENLTLIQQE VDALEELSRQ LFLETADLYA TKERIEYSKT FKGKYFNFLG YFFSIYCVWK
IFMATINIVF DRVGKTDPVT RGIEITVNYL GIQFDVKFWS QHISFILVGI IIVTSIRGLL
ITLTKFFYAI SSSKSSNVIV LLLAQIMGMY FVSSVLLIRM SMPLEYRTII TEVLGELQFN
FYHRWFDVIF LVSALSSILF LYLAHKQAPE KHMAP
