GPR34_GORGO
ID GPR34_GORGO Reviewed; 381 AA.
AC Q6XCF2;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Probable G-protein coupled receptor 34;
GN Name=GPR34;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12835326; DOI=10.1074/jbc.m303346200;
RA Schulz A., Schoneberg T.;
RT "The structural evolution of a P2Y-like G-protein-coupled receptor.";
RL J. Biol. Chem. 278:35531-35541(2003).
CC -!- FUNCTION: Orphan receptor.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY241078; AAP04287.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6XCF2; -.
DR SMR; Q6XCF2; -.
DR InParanoid; Q6XCF2; -.
DR Proteomes; UP000001519; 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:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..381
FT /note="Probable G-protein coupled receptor 34"
FT /id="PRO_0000069558"
FT TOPO_DOM 1..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 127..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 381 AA; 43860 MW; 491FC016E5624379 CRC64;
MRSHTITMTT TSVSSWPYSS HRMRFITNHS DQPPQNFSAT PNVTTCPMDE KLLSTVLTTS
YSVIFIVGLV GNIIALYVFL GIHRKRNSIQ IYLLNVAIAD LLLIFCLPFR IMYHINQNKW
TLGVILCKVV GTLFYMNMYI SIILLGFISL DRYIKINRSI QQRKAITTKQ SIYVCCIVWM
LALGGFLTMI ILTLKKGGHN STMCFHYRDK HNAKGEAIFN FILVVMFWLI FLLIILSYIK
IGKNLLRISK RRSKFPNSGK YATTARNSFI VLIIFTICFV PYHAFRFIYI SSQLNVSSCY
WKEIVHKTNE IMLVLSSFNS CLDPVMYFLM SSNIRKIMCQ LLFRRFQGEP SRSESTSEFK
PGYSLHDTSV AVKIQSSSKS T