CML2_MACMU
ID CML2_MACMU Reviewed; 355 AA.
AC O97664;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Chemerin-like receptor 2;
DE AltName: Full=Chemerin chemokine-like receptor 2;
DE AltName: Full=Chemokine-like receptor 2;
DE AltName: Full=G-protein coupled receptor 1;
GN Name=CMKLR2; Synonyms=GPR1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Spleen;
RX PubMed=11461684; DOI=10.1089/088922201750290104;
RA Margulies B.J., Hauer D.A., Clements J.E.;
RT "Identification and comparison of eleven rhesus macaque chemokine
RT receptors.";
RL AIDS Res. Hum. Retroviruses 17:981-986(2001).
CC -!- FUNCTION: Receptor for chemoattractant adipokine chemerin/RARRES2
CC suggesting a role for this receptor in the regulation of inflammation
CC and energy homesotasis (By similarity). Signals mainly via beta-
CC arrestin pathway. Binding of RARRES2 activates weakly G proteins,
CC calcium mobilization and MAPK1/MAPK3 (ERK1/2) phosphorylation too. Acts
CC also as a receptor for TAFA1, mediates its effects on neuronal stem-
CC cell proliferation and differentiation via the activation of ROCK/ERK
CC and ROCK/STAT3 signaling pathway (By similarity).
CC {ECO:0000250|UniProtKB:P46091, ECO:0000250|UniProtKB:Q8K087}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8K087};
CC Multi-pass membrane protein {ECO:0000255}. Note=Internalizes in
CC presence of its ligand, TAFA1 (By similarity). Internalizes efficiently
CC in response to RARRES2 (By similarity). {ECO:0000250|UniProtKB:P46091,
CC ECO:0000250|UniProtKB:Q8K087}.
CC -!- SIMILARITY: Belongs to the chemokine-like receptor (CMKLR) family.
CC {ECO:0000305}.
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DR EMBL; AF100204; AAC72402.1; -; Genomic_DNA.
DR RefSeq; NP_001040594.1; NM_001047129.1.
DR RefSeq; XP_014966212.1; XM_015110726.1.
DR RefSeq; XP_014966213.1; XM_015110727.1.
DR RefSeq; XP_014966214.1; XM_015110728.1.
DR RefSeq; XP_014966215.1; XM_015110729.1.
DR AlphaFoldDB; O97664; -.
DR SMR; O97664; -.
DR STRING; 9544.ENSMMUP00000010928; -.
DR Ensembl; ENSMMUT00000011655; ENSMMUP00000010928; ENSMMUG00000008334.
DR GeneID; 707120; -.
DR KEGG; mcc:707120; -.
DR CTD; 2825; -.
DR VEuPathDB; HostDB:ENSMMUG00000008334; -.
DR VGNC; VGNC:73124; CMKLR2.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160642; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; O97664; -.
DR OMA; ISSKHFW; -.
DR OrthoDB; 910274at2759; -.
DR TreeFam; TF330976; -.
DR Proteomes; UP000006718; Chromosome 12.
DR Bgee; ENSMMUG00000008334; Expressed in fibroblast and 17 other tissues.
DR ExpressionAtlas; O97664; baseline.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0097004; F:adipokinetic hormone binding; ISS:UniProtKB.
DR GO; GO:0097003; F:adipokinetic hormone receptor activity; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR InterPro; IPR002275; CML2.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01146; GPR1ORPHANR.
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..355
FT /note="Chemerin-like receptor 2"
FT /id="PRO_0000069507"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 355 AA; 41361 MW; 48BB9EBF1091486E CRC64;
MEDLEETLFE EFENYSYALD YYSLESDLEE KVQLGVVHWV SLVLYCLSFV LGIPGNAIVI
WFTGFKWKKT VSTLWFLNLA IADFIFLLFL PLYISYVVMN FHWPFGIWLC KANSFTAQLN
MFASVFFLTV ISLDHYIHLI HPVLSHRHRT LKNSLIVIIF IWLLASLIGG PALYFRDTVE
FNNHTLCYNN FQKHDPDLTV IRHHVLTWVK FIVGYLFPLL TMSICYLCLI FKVKKRSILI
SSRHFWTILA VVVAFVVCWT PYHLFSIWEL TIHHNSYSHH VMQAGIPLST GLAFLNSCLN
PILYVLISKK FQARFRSSVA EILKYTLWEV SCSGTVSEQL RNSETKNLCL LETAQ
