GP182_RAT
ID GP182_RAT Reviewed; 395 AA.
AC P31392; Q64166;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=G-protein coupled receptor 182;
DE AltName: Full=G10D;
DE AltName: Full=NOW;
GN Name=Gpr182; Synonyms=Admr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=8382168; DOI=10.1016/0014-5793(93)81318-t;
RA Harrison J.K., Barber C.M., Lynch K.R.;
RT "Molecular cloning of a novel rat G-protein-coupled receptor gene expressed
RT prominently in lung, adrenal, and liver.";
RL FEBS Lett. 318:17-22(1993).
RN [2]
RP SEQUENCE REVISION.
RA Harrison J.K.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=8390839; DOI=10.1089/dna.1993.12.393;
RA Eva C., Sprengel R.;
RT "A novel putative G protein-coupled receptor highly expressed in lung and
RT testis.";
RL DNA Cell Biol. 12:393-399(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=7592696; DOI=10.1074/jbc.270.43.25344;
RA Kapas S., Catt K.J., Clark A.J.;
RT "Cloning and expression of cDNA encoding a rat adrenomedullin receptor.";
RL J. Biol. Chem. 270:25344-25347(1995).
RN [5]
RP DOUBTS ON THE ORIGINAL FUNCTION.
RX PubMed=9535752; DOI=10.1006/bbrc.1998.8349;
RA Kennedy S.P., Sun D., Oleynek J.J., Hoth C.F., Kong J., Hill R.J.;
RT "Expression of the rat adrenomedullin receptor or a putative human
RT adrenomedullin receptor does not correlate with adrenomedullin binding or
RT functional response.";
RL Biochem. Biophys. Res. Commun. 244:832-837(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Orphan receptor.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of peripheral tissues
CC in the adult rat with prominent expression in lung, testis, adrenal and
CC liver. {ECO:0000269|PubMed:8382168, ECO:0000269|PubMed:8390839}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Was originally thought to be a receptor for adrenomedullin.
CC {ECO:0000305|PubMed:7592696}.
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DR EMBL; L09249; AAB05356.1; -; Genomic_DNA.
DR EMBL; L04672; AAA41271.1; -; mRNA.
DR EMBL; S79811; AAB35457.1; -; mRNA.
DR PIR; S40685; S40685.
DR AlphaFoldDB; P31392; -.
DR SMR; P31392; -.
DR STRING; 10116.ENSRNOP00000054500; -.
DR GuidetoPHARMACOLOGY; 146; -.
DR GlyGen; P31392; 2 sites.
DR iPTMnet; P31392; -.
DR PhosphoSitePlus; P31392; -.
DR PaxDb; P31392; -.
DR UCSC; RGD:61903; rat.
DR RGD; 61903; Gpr182.
DR eggNOG; ENOG502QSNU; Eukaryota.
DR InParanoid; P31392; -.
DR PRO; PR:P31392; -.
DR Proteomes; UP000002494; 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:0001605; F:adrenomedullin receptor activity; IDA:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR InterPro; IPR001350; G10D_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00643; G10DORPHANR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..395
FT /note="G-protein coupled receptor 182"
FT /id="PRO_0000069114"
FT TOPO_DOM 1..53
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..295
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 122..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 8..9
FT /note="RP -> EA (in Ref. 3; AAA41271)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="H -> R (in Ref. 1; AAB05356)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="V -> A (in Ref. 3; AAA41271)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="V -> A (in Ref. 1; AAB05356)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="I -> T (in Ref. 1; AAB05356)"
FT /evidence="ECO:0000305"
FT CONFLICT 366..395
FT /note="PLQRICTPTPSETCRPPLCLRTPHLHSAIP -> LAAADLHTHAIRNVQASS
FT LPPNTSPTLCNSIAS (in Ref. 1; AAB05356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 45196 MW; DA0499C99E48128D CRC64;
MSVIPSSRPV STLAPDNDFR EIHNWTELLH LFNQTFSDCH MELNENTKQV VLFVFYLAIF
VVGLVENVLV ICVNCRRSGR VGMLNLYILN MAVADLGIIL SLPVWMLEVM LEYTWLWGSF
SCRFIHYFYL ANMYSSIFFL TCLSIDRYVT LTNTSPSWQR HQHRIRRAVC AGVWVLSAII
PLPEVVHIQL LDGSEPMCLF LAPFETYSAW ALAVALSATI LGFLLPFPLI AVFNILSACR
LRRQGQTESR RHCLLMWAYI VVFVICWLPY HVTMLLLTLH TTHIFLHCNL VNFLYFFYEI
IDCFSMLHCV ANPILYNFLS PSFRGRLLSL VVRYLPKEQA RAAGGRASSS SSTQHSIIIT
KEGSLPLQRI CTPTPSETCR PPLCLRTPHL HSAIP
