GPR39_BOVIN
ID GPR39_BOVIN Reviewed; 454 AA.
AC B4XF06;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=G-protein coupled receptor 39;
GN Name=GPR39;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Duodenum;
RX PubMed=19498292; DOI=10.1292/jvms.71.641;
RA Yamamoto I., Kimura N., Arai T., Tanaka M.;
RT "cDNA cloning and mRNA expression of bovine GPR39.";
RL J. Vet. Med. Sci. 71:641-644(2009).
CC -!- FUNCTION: Zn(2+) acts as an agonist. This receptor mediates its action
CC by association with G proteins that activate a phosphatidylinositol-
CC calcium second messenger system. Its effect is mediated mainly through
CC G(q)-alpha and G(12)/G(13) proteins. Involved in regulation of body
CC weight, gastrointestinal mobility, hormone secretion and cell death (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in liver, kidney, abomasum, uterus, small
CC intestine and colon. {ECO:0000269|PubMed:19498292}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; EU031892; ABV83042.1; -; mRNA.
DR RefSeq; NP_001137216.1; NM_001143744.1.
DR AlphaFoldDB; B4XF06; -.
DR SMR; B4XF06; -.
DR STRING; 9913.ENSBTAP00000053900; -.
DR PaxDb; B4XF06; -.
DR GeneID; 100139476; -.
DR KEGG; bta:100139476; -.
DR CTD; 2863; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; B4XF06; -.
DR OrthoDB; 890529at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..454
FT /note="G-protein coupled receptor 39"
FT /id="PRO_0000379076"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 56..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 70..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 90..109
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 110..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 132..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 173..217
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 218..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 243..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 284..305
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 306..323
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 324..344
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 345..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT REGION 415..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O43194"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O43194"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43194"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 11..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 108..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 454 AA; 51445 MW; 47E112B6F5EB646A CRC64;
MASPSHPSRD CSQVIDHSHV PEFEVATWIK ITLILVYLVI FVVGILGNSV TIRVTQVLQK
KGYLQKEVTD HMVSLACSDI LVFLIGMPME FYSIIWNPLT TPSYTVSCKV HTFLFEACSY
ATLLHVLTLS FERYIAICHP FRYKAMSGPC QVKLLIGFVW VTSALVALPL LFAMGVEYPL
VNVPSHRGLI CNRSRTRHQE QPESSNMSIC TNLSSRWTVF QSSIFSAFVV YLVVLVSVAF
MCWSMMQVLR RSKQGTLAAQ GQQLQLRKLE SQESRSARRQ TIIFLELIVV TLAVCWMPNQ
VRRIMAAAKP KHDWTKSYFR AYMILLPFSD TFFYLSSVVN PLLYNVSSQQ FRSVFGQVLR
CQLTLPHANQ EKHLRAHVAS TMDSTRSACR PLIFPASQRS SSSARANMVF LSTFHSEAKP
ESKPQELSCE SPEPNSERKP ANPATRNGFQ EHEV
