GPR39_PIG
ID GPR39_PIG Reviewed; 456 AA.
AC B2ZHY2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=G-protein coupled receptor 39;
GN Name=GPR39;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tang S.Q., Jiang Q.Y., Dong X.Y., Shu G., Zhang Y.L., Zhu X.T., Gao P.;
RT "cDNA cloning and mRNA expression of G-protein coupled receptor 39 (GPR39)
RT in Sus scrofa liver.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; EU669821; ACD39430.1; -; mRNA.
DR RefSeq; NP_001121959.1; NM_001128487.1.
DR AlphaFoldDB; B2ZHY2; -.
DR SMR; B2ZHY2; -.
DR STRING; 9823.ENSSSCP00000016648; -.
DR PaxDb; B2ZHY2; -.
DR PRIDE; B2ZHY2; -.
DR GeneID; 100158236; -.
DR KEGG; ssc:100158236; -.
DR CTD; 2863; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; B2ZHY2; -.
DR OrthoDB; 890529at2759; -.
DR ChiTaRS; GPR39; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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..456
FT /note="G-protein coupled receptor 39"
FT /id="PRO_0000379077"
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..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT REGION 406..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..434
FT /note="Polar residues"
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 456 AA; 51508 MW; 5D74E484D7274D93 CRC64;
MASPSRPGND CSHVIDHSHV PEFEVATWIK ITLILLFLVI FVVGILGNSV TIRVTQVLQK
KGYLQKEVTD HMVSLACSDI LVFLIGMPVE FYSIIWNPLT TPSYTVSCKL HSFLFETCSY
ATLLHVLTLS FERYIAICHP FRYKAMSGPC QVKLLIGFVW VTSTLVALPL LFAMGVEYPL
VDVPSHRGLS CNRSRNHHSE HPETSNMSVC TNLSSRWTVF QSSIFGAFII YLVVLVSVAF
MCWSMMQALQ RSKQGTLAAK GQQLQLRKSE SEESRSARRQ TIIFLRLIVV TLAICWMPNQ
IRRMMAAAKP KQDWTKAYFK AYMILLPFSD TFFYLSSVVN PLLYNVSSQQ FRSVFAQVLR
CRLTLPHANQ DKRLRAQAAS TMDSARSVHR PLIFLASRSN SSARRTDKVF LSTSQSESEA
KPQSKPQLLN HESPESDSVM KPANPATENG IQEHEV
