CML1_BOVIN
ID CML1_BOVIN Reviewed; 362 AA.
AC B9VR26;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Chemerin-like receptor 1;
DE AltName: Full=Chemokine-like receptor 1;
DE Short=CMKLR-1;
GN Name=CMLKR1;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=White adipose tissue;
RX PubMed=20399065; DOI=10.1016/j.domaniend.2010.02.007;
RA Song S.H., Fukui K., Nakajima K., Kozakai T., Sasaki S., Roh S.G.,
RA Katoh K.;
RT "Cloning, expression analysis, and regulatory mechanisms of bovine chemerin
RT and chemerin receptor.";
RL Domest. Anim. Endocrinol. 39:97-105(2010).
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: Widely expressed in several tissues including
CC adipose, muscle, liver and brain. {ECO:0000269|PubMed:20399065}.
CC -!- SIMILARITY: Belongs to the chemokine-like receptor (CMKLR) family.
CC {ECO:0000305}.
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DR EMBL; FJ594407; ACM47222.1; -; mRNA.
DR RefSeq; NP_001138707.1; NM_001145235.1.
DR RefSeq; XP_005218152.1; XM_005218095.2.
DR RefSeq; XP_005218153.1; XM_005218096.3.
DR RefSeq; XP_005218155.1; XM_005218098.3.
DR RefSeq; XP_010812411.1; XM_010814109.2.
DR RefSeq; XP_010812412.1; XM_010814110.2.
DR RefSeq; XP_010812415.1; XM_010814113.2.
DR AlphaFoldDB; B9VR26; -.
DR SMR; B9VR26; -.
DR STRING; 9913.ENSBTAP00000029488; -.
DR PaxDb; B9VR26; -.
DR Ensembl; ENSBTAT00000029488; ENSBTAP00000029488; ENSBTAG00000022039.
DR GeneID; 615411; -.
DR KEGG; bta:615411; -.
DR CTD; 1240; -.
DR VEuPathDB; HostDB:ENSBTAG00000022039; -.
DR VGNC; VGNC:52753; CMKLR1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230438; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; B9VR26; -.
DR OMA; TACVVIW; -.
DR OrthoDB; 910274at2759; -.
DR TreeFam; TF330976; -.
DR Reactome; R-BTA-373076; Class A/1 (Rhodopsin-like receptors).
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000022039; Expressed in lung and 99 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: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; IEA:Ensembl.
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; IBA:GO_Central.
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 2: Evidence at transcript 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..362
FT /note="Chemerin-like receptor 1"
FT /id="PRO_0000411102"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 336..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35786"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 362 AA; 40711 MW; 46C5511BEE8B0F78 CRC64;
MEAEDYNASY EDYPDDVDPI VVLEELSPLE GRVVRILLVA VYSVICLLGI LGNGLVIVMI
TCKMKRTVNT VWFLNLAVAD FLFNVFLPVH IAYAALDYHW VFGTAMCKIS NFLLIHNMFT
SVFLLTVISF DRCVSVLLPV WSQNHRSVRL AYTACLVIWV LAFFLSSPSL VFRDTARLHG
KISCFNNFSL SAAVSSPWPA HPQVDPVGSG RHKVVTITRF LCGFLVPGLI TTACYLTIVY
KLQRSRLAKT KKPFKIILTI IVTFFLCWCP YHAFYLLELR RGSVPPSVFS LGVPLATAIA
IANSCMNPIL YVFMGQDFKK FRVALFSRLV NALSEDTGHS SYPSHRSFTK MSSMNERETG
ML
