CML1_RAT
ID CML1_RAT Reviewed; 372 AA.
AC O35786; G3V625;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Chemerin-like receptor 1;
DE AltName: Full=Chemokine-like receptor 1;
DE AltName: Full=G-protein coupled chemoattractant-like receptor;
DE AltName: Full=G-protein coupled receptor DEZ;
GN Name=Cmklr1; Synonyms=Dez;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Albino; TISSUE=Pituitary anterior lobe;
RX PubMed=9425281; DOI=10.1006/bbrc.1997.7822;
RA Owman C.S.O., LoLait S.J., Santen S., Olde B.;
RT "Molecular cloning and tissue distribution of cDNA encoding a novel
RT chemoattractant-like receptor.";
RL Biochem. Biophys. Res. Commun. 241:390-394(1997).
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; THR-341; SER-348 AND
RP SER-357, AND IDENTIFICATION BY 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: Receptor for the chemoattractant adipokine chemerin/RARRES2
CC and for the omega-3 fatty acid derived molecule resolvin E1.
CC Interaction with RARRES2 initiates activation of G proteins G(i)/G(o)
CC and beta-arrestin pathways inducing cellular responses via second
CC messenger pathways such as intracellular calcium mobilization,
CC phosphorylation of MAP kinases MAPK1/MAPK3 (ERK1/2), TYRO3,
CC MAPK14/P38MAPK and PI3K leading to multifunctional effects, like,
CC reduction of immune responses, enhancing of adipogenesis and
CC angionesis. Resolvin E1 down-regulates cytokine production in
CC macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-
CC kappa-B. Positively regulates adipogenesis and adipocyte metabolism (By
CC similarity). {ECO:0000250|UniProtKB:Q99788}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99788};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: High expression in heart and lung, low in small
CC intestines, colon, kidney, liver, uterus and brain.
CC {ECO:0000269|PubMed:9425281}.
CC -!- SIMILARITY: Belongs to the chemokine-like receptor (CMKLR) family.
CC {ECO:0000305}.
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DR EMBL; AJ002745; CAA05715.1; -; mRNA.
DR EMBL; AC128917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473973; EDM13970.1; -; Genomic_DNA.
DR EMBL; CH473973; EDM13971.1; -; Genomic_DNA.
DR PIR; JC5796; JC5796.
DR RefSeq; NP_071554.2; NM_022218.2.
DR RefSeq; XP_006249567.1; XM_006249505.3.
DR RefSeq; XP_006249568.1; XM_006249506.3.
DR RefSeq; XP_006249569.1; XM_006249507.3.
DR RefSeq; XP_006249570.1; XM_006249508.3.
DR RefSeq; XP_006249571.1; XM_006249509.3.
DR AlphaFoldDB; O35786; -.
DR SMR; O35786; -.
DR STRING; 10116.ENSRNOP00000000893; -.
DR GlyGen; O35786; 2 sites.
DR iPTMnet; O35786; -.
DR PhosphoSitePlus; O35786; -.
DR PaxDb; O35786; -.
DR Ensembl; ENSRNOT00000000893; ENSRNOP00000000893; ENSRNOG00000000704.
DR Ensembl; ENSRNOT00000097365; ENSRNOP00000089521; ENSRNOG00000000704.
DR Ensembl; ENSRNOT00000101222; ENSRNOP00000085339; ENSRNOG00000000704.
DR Ensembl; ENSRNOT00000105285; ENSRNOP00000091942; ENSRNOG00000000704.
DR GeneID; 60669; -.
DR KEGG; rno:60669; -.
DR UCSC; RGD:69359; rat.
DR CTD; 1240; -.
DR RGD; 69359; Cmklr1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230438; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; O35786; -.
DR OMA; TACVVIW; -.
DR OrthoDB; 910274at2759; -.
DR PhylomeDB; O35786; -.
DR TreeFam; TF330976; -.
DR Reactome; R-RNO-373076; Class A/1 (Rhodopsin-like receptors).
DR PRO; PR:O35786; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Proteomes; UP000234681; Chromosome 12.
DR Bgee; ENSRNOG00000000704; Expressed in lung and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0001637; F:G protein-coupled chemoattractant receptor activity; TAS:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; ISS:UniProtKB.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; ISS:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISO:RGD.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISS:UniProtKB.
DR InterPro; IPR002258; CML1.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; PTHR24225; 1.
DR PANTHER; PTHR24225:SF49; PTHR24225:SF49; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01126; DEZORPHANR.
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..372
FT /note="Chemerin-like receptor 1"
FT /id="PRO_0000069309"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..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..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..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..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..319
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 371
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 164..170
FT /note="LAFFLSS -> WLSSESP (in Ref. 1; CAA05715)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..178
FT /note="RDT -> GH (in Ref. 1; CAA05715)"
FT CONFLICT 251
FT /note="L -> Q (in Ref. 1; CAA05715)"
SQ SEQUENCE 372 AA; 41865 MW; 478D475020E6BEDC CRC64;
MEYEGYNDSS IYGEEYSDGS DYIVDLEEAG PLEAKVAEVF LVVIYSLVCF LGILGNGLVI
VIATFKMKKT VNTVWFVNLA VADFLFNIFL PIHITYAAMD YHWVFGKAMC KISSFLLSHN
MYTSVFLLTV ISFDRCISVL LPVWSQNHRS VRLAYMTCVV VWVLAFFLSS PSLVFRDTVS
TSHGKITCFN NFSLAAPEPF SHSTHPRTDP VGYSRHVAVT VTRFLCGFLI PVFIITACYL
TIVFKLQRNR LAKTKKPFKI IITIIITFFL CWCPYHTLYL LELHHTAVPA SVFSLGLPLA
TAVAIANSCM NPILYVFMGH DFKKFKVALF SRLVNALSED TGPSSYPSHR SFTKMSSLIE
KASVNEKETS TL
