GPR84_BOVIN
ID GPR84_BOVIN Reviewed; 396 AA.
AC Q2KI97; A5D964;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=G-protein coupled receptor 84;
GN Name=GPR84;
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].
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].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for medium-chain free fatty acid (FFA) with carbon
CC chain lengths of C9 to C14. Capric acid (C10:0), undecanoic acid
CC (C11:0) and lauric acid (C12:0) are the most potent agonists. Not
CC activated by short-chain and long-chain saturated and unsaturated FFAs.
CC Activation by medium-chain free fatty acid is coupled to a pertussis
CC toxin sensitive G(i/o) protein pathway. May have important roles in
CC processes from fatty acid metabolism to regulation of the immune system
CC (By similarity). {ECO:0000250}.
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; BT030483; ABQ12923.1; -; mRNA.
DR EMBL; BC112718; AAI12719.1; -; mRNA.
DR AlphaFoldDB; Q2KI97; -.
DR SMR; Q2KI97; -.
DR STRING; 9913.ENSBTAP00000020710; -.
DR PaxDb; Q2KI97; -.
DR Ensembl; ENSBTAT00000020710; ENSBTAP00000020710; ENSBTAG00000015592.
DR VEuPathDB; HostDB:ENSBTAG00000015592; -.
DR VGNC; VGNC:29601; GPR84.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00390000009609; -.
DR HOGENOM; CLU_009579_3_10_1; -.
DR InParanoid; Q2KI97; -.
DR OMA; QVLHMFC; -.
DR OrthoDB; 732872at2759; -.
DR TreeFam; TF333474; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Proteomes; UP000009136; Chromosome 5.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0001604; F:urotensin II receptor activity; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide 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 SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..396
FT /note="G-protein coupled receptor 84"
FT /id="PRO_0000247893"
FT TOPO_DOM 1..26
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..94
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..352
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 243..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CIM5"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CIM5"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 396 AA; 43517 MW; 5961126CA3E9F5C9 CRC64;
MWNASDVNFS CYHESVLGYR YVAVSWGIVV AVTGTVGNVL TLLALAIQPK LRTRFNLLIA
NLTVADLLYC TLLQPFSVDT YLHLHWRTGA TFCQIFGFLL FVSNSVSILT LCLIALGRYL
LIAHPKLFPQ VFSAKGIVLA LVSTWVVAVA SFAPLWPIYI LVPVVCTCSF DRIRGQPYTT
ILMGIYFVVG LSSVGVFYCL IHQQVKRAAQ AMNQYKLRQA SIRSNHVAGA HEAVPGRFQE
LDSGLASGGP SEGISSEPVS AATTQTLEGD SSEVRDQSNS KAAKQMAEKN PPGVAAKART
TKGAQRAQDS PSEFGKVTRM CFAVFLCFTL SYIPFLLLNI LDAKVQAPRV VHMLAANLTW
LNGCINPVLY AAMNRQFRQA YGSLLRRGPQ SFHRFH
