GPHR_CRIGR
ID GPHR_CRIGR Reviewed; 455 AA.
AC B2ZXD5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Golgi pH regulator;
DE AltName: Full=Protein GPR89;
GN Name=GPR89; Synonyms=GPHR;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
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).
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 (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:0000269|PubMed:18794847}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Delayed transport of newly synthesized protein
CC from the Golgi to the plasma membrane, impaired glycosylation of
CC proteins along the exocytic pathway, and structural disorganization of
CC the Golgi apparatus. Defects are associated with decreased
CC acidification of the cisternae of the Golgi and trans-Golgi network by
CC 0.4-0.5 pH units with no effect on lysosomal pH and no effect on
CC endocytosis or recycling. {ECO:0000269|PubMed:18794847}.
CC -!- MISCELLANEOUS: Experiments do not strictly demonstrate that altered
CC chloride permeability of the Golgi or that the lack of acidification is
CC due to absence of counterion conductance in the absence of GPR89/GPHR.
CC It is therefore possible that GPR89/GPHR regulates Golgi pH by some
CC other mechanism (PubMed:18794847). {ECO:0000305|PubMed:18794847}.
CC -!- SIMILARITY: Belongs to the Golgi pH regulator (TC 1.A.38) family.
CC {ECO:0000305}.
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DR EMBL; AB362891; BAG41890.1; -; mRNA.
DR RefSeq; NP_001233742.1; NM_001246813.1.
DR AlphaFoldDB; B2ZXD5; -.
DR SMR; B2ZXD5; -.
DR STRING; 10029.NP_001233742.1; -.
DR TCDB; 1.A.38.1.1; the golgi ph regulator (gphr) family.
DR GeneID; 100689387; -.
DR KEGG; cge:100689387; -.
DR CTD; 36682; -.
DR eggNOG; KOG2417; Eukaryota.
DR OrthoDB; 1065554at2759; -.
DR GO; GO:0032580; C:Golgi cisterna membrane; IDA:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0051452; P:intracellular pH reduction; IDA: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 Glycoprotein; Golgi apparatus; Ion channel; Ion transport; Membrane;
KW Protein transport; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..455
FT /note="Golgi pH regulator"
FT /id="PRO_0000395005"
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"
SQ SEQUENCE 455 AA; 52738 MW; 8F14ED2211444388 CRC64;
MSFLIDSSIM VTSQILFFGF GWLFFMRQLF KDYEVRQYVV QVIFSVTFAF SCTMFELIIF
EILGVLNSSS RYFHWKMNLC VILLILVFMV PFYIGYFIVS NIQLLHKQRL LFSCLLWLTF
MYFFWKLGDP FPILSPKHGI LSIEQLISRV GVIGVTLMAL LSGFGAVNCP YTYMSYFLRN
VTDTDILALE RRLLQTMDMI ISKKKRMAVA RRTMFQRGEV QNKPSGLWGM LKSVTASAPG
SENLTLIQQE VDALEELSRQ LFLETADLYA TKERIEYSKT FKGKYFNFLG YFFSIYCVWK
IFMATINIVL DRVGKTDPVT RGIEITVNYL GIQFDVKFWS QHISFILVGI IIVSSIRGLL
ITLTKFFYAI SSSKSSNVIV LLLAQIMGMY FVSSVLLIRM SMPPEYRTII TQVLGELQFN
FYHRWFDVIF LVSALSSILF LYLAHKQAPE KHMAP
