CML2_RAT
ID CML2_RAT Reviewed; 353 AA.
AC P46090; M0RCK7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 115.
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 {ECO:0000312|RGD:2728};
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].
RX PubMed=7811287; DOI=10.1006/bbrc.1994.2899;
RA Marchese A., Cheng R., Lee M.C., Porter C.A., Heiber M., Goodman M.,
RA George S.R., O'Dowd B.F.;
RT "Mapping studies of two G protein-coupled receptor genes: an amino acid
RT difference may confer a functional variation between a human and rodent
RT receptor.";
RL Biochem. Biophys. Res. Commun. 205:1952-1958(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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; S74702; AAB32978.1; -; Genomic_DNA.
DR EMBL; AC141169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473965; EDL98895.1; -; Genomic_DNA.
DR PIR; JC2492; JC2492.
DR RefSeq; NP_037093.1; NM_012961.1.
DR RefSeq; XP_008765299.1; XM_008767077.2.
DR RefSeq; XP_017451774.1; XM_017596285.1.
DR AlphaFoldDB; P46090; -.
DR SMR; P46090; -.
DR STRING; 10116.ENSRNOP00000067327; -.
DR GlyGen; P46090; 1 site.
DR PhosphoSitePlus; P46090; -.
DR PaxDb; P46090; -.
DR Ensembl; ENSRNOT00000072737; ENSRNOP00000067327; ENSRNOG00000045532.
DR GeneID; 25457; -.
DR KEGG; rno:25457; -.
DR UCSC; RGD:2728; rat.
DR CTD; 2825; -.
DR RGD; 2728; Gpr1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160642; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; P46090; -.
DR OMA; ISSKHFW; -.
DR OrthoDB; 910274at2759; -.
DR PhylomeDB; P46090; -.
DR PRO; PR:P46090; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Proteomes; UP000234681; Chromosome 9.
DR Bgee; ENSRNOG00000045532; Expressed in skeletal muscle tissue and 2 other tissues.
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: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; 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..353
FT /note="Chemerin-like receptor 2"
FT /id="PRO_0000069509"
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..353
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"
FT CONFLICT 85
FT /note="V -> I (in Ref. 1; AAB32978)"
FT CONFLICT 304
FT /note="L -> I (in Ref. 1; AAB32978)"
SQ SEQUENCE 353 AA; 40887 MW; 84C98E03E796E77A CRC64;
MEVSREMLFE ELDNYSYALE YYSQEPDAEE NVYPGIVHWI SLLLYALAFV LGIPGNAIVI
WFMGFKWKKT VTTLWFLNLA IADFVFVLFL PLYISYVALS FHWPFGRWLC KLNSFIAQLN
MFSSVFFLTV ISLDRYIHLI HPGLSHPHRT LKNSLLVVLF VWLLASLLGG PTLYFRDTVE
VNNRIICYNN FQEYELTLMR HHVLTWVKFL FGYLLPLLTM SSCYLCLIFK TKKQNILISS
KHLWMILSVV IAFMVCWTPF HLFSIWELSI HHNSSFQNVL QGGIPLSTGL AFLNSCLNPI
LYVLISKKFQ ARFRASVAEV LKRSLWEASC SGTVSEQLRS AETKSLSLLE TAQ
