CML1_PIG
ID CML1_PIG Reviewed; 363 AA.
AC B1PHQ8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Chemerin-like receptor 1 {ECO:0000305};
DE AltName: Full=Chemokine-like receptor 1;
GN Name=CMLKR1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=20663411; DOI=10.5483/bmbrep.2010.43.7.491;
RA Huang J., Zhang J., Lei T., Chen X., Zhang Y., Zhou L., Yu A., Chen Z.,
RA Zhou R., Yang Z.;
RT "Cloning of porcine chemerin, ChemR23 and GPR1 and their involvement in
RT regulation of lipogenesis.";
RL BMB Rep. 43:491-498(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang J., Yang G.-Y., Li H.-J., Wang W.-J., Zhang Z.-Q., Zang M., Tai Y.-L.,
RA Wang Y.-L.;
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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: Predominantly expressed in spleen and temperately
CC in adipose tissue. {ECO:0000269|PubMed:20663411}.
CC -!- SIMILARITY: Belongs to the chemokine-like receptor (CMKLR) family.
CC {ECO:0000305}.
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DR EMBL; EU660866; ACD31687.1; -; Genomic_DNA.
DR EMBL; EU421950; ACA42765.1; -; mRNA.
DR RefSeq; NP_001116572.1; NM_001123100.1.
DR AlphaFoldDB; B1PHQ8; -.
DR SMR; B1PHQ8; -.
DR STRING; 9823.ENSSSCP00000010614; -.
DR PaxDb; B1PHQ8; -.
DR PRIDE; B1PHQ8; -.
DR Ensembl; ENSSSCT00000044992; ENSSSCP00000049260; ENSSSCG00000031346.
DR Ensembl; ENSSSCT00000055789; ENSSSCP00000055388; ENSSSCG00000031346.
DR Ensembl; ENSSSCT00000058690; ENSSSCP00000059035; ENSSSCG00000031346.
DR Ensembl; ENSSSCT00000068909; ENSSSCP00000067510; ENSSSCG00000031346.
DR Ensembl; ENSSSCT00025037188; ENSSSCP00025015575; ENSSSCG00025027435.
DR Ensembl; ENSSSCT00025037226; ENSSSCP00025015586; ENSSSCG00025027435.
DR Ensembl; ENSSSCT00025037277; ENSSSCP00025015617; ENSSSCG00025027435.
DR Ensembl; ENSSSCT00025037314; ENSSSCP00025015635; ENSSSCG00025027435.
DR Ensembl; ENSSSCT00035100825; ENSSSCP00035042854; ENSSSCG00035074277.
DR Ensembl; ENSSSCT00035100840; ENSSSCP00035042862; ENSSSCG00035074277.
DR Ensembl; ENSSSCT00035100853; ENSSSCP00035042870; ENSSSCG00035074277.
DR Ensembl; ENSSSCT00035100869; ENSSSCP00035042879; ENSSSCG00035074277.
DR Ensembl; ENSSSCT00040006019; ENSSSCP00040002353; ENSSSCG00040004518.
DR Ensembl; ENSSSCT00040006021; ENSSSCP00040002354; ENSSSCG00040004518.
DR Ensembl; ENSSSCT00040006022; ENSSSCP00040002355; ENSSSCG00040004518.
DR Ensembl; ENSSSCT00040006025; ENSSSCP00040002358; ENSSSCG00040004518.
DR Ensembl; ENSSSCT00045034722; ENSSSCP00045024083; ENSSSCG00045020371.
DR Ensembl; ENSSSCT00045034778; ENSSSCP00045024121; ENSSSCG00045020371.
DR Ensembl; ENSSSCT00045034808; ENSSSCP00045024143; ENSSSCG00045020371.
DR Ensembl; ENSSSCT00045034843; ENSSSCP00045024168; ENSSSCG00045020371.
DR Ensembl; ENSSSCT00050051205; ENSSSCP00050021481; ENSSSCG00050037975.
DR Ensembl; ENSSSCT00050051210; ENSSSCP00050021482; ENSSSCG00050037975.
DR Ensembl; ENSSSCT00050051213; ENSSSCP00050021485; ENSSSCG00050037975.
DR Ensembl; ENSSSCT00050051214; ENSSSCP00050021486; ENSSSCG00050037975.
DR Ensembl; ENSSSCT00055013166; ENSSSCP00055010339; ENSSSCG00055006809.
DR Ensembl; ENSSSCT00055013185; ENSSSCP00055010355; ENSSSCG00055006809.
DR Ensembl; ENSSSCT00055013206; ENSSSCP00055010373; ENSSSCG00055006809.
DR Ensembl; ENSSSCT00055013219; ENSSSCP00055010386; ENSSSCG00055006809.
DR Ensembl; ENSSSCT00065031725; ENSSSCP00065012981; ENSSSCG00065023832.
DR Ensembl; ENSSSCT00065031727; ENSSSCP00065012983; ENSSSCG00065023832.
DR Ensembl; ENSSSCT00065031730; ENSSSCP00065012985; ENSSSCG00065023832.
DR Ensembl; ENSSSCT00065031732; ENSSSCP00065012986; ENSSSCG00065023832.
DR Ensembl; ENSSSCT00070004682; ENSSSCP00070003836; ENSSSCG00070002505.
DR Ensembl; ENSSSCT00070004689; ENSSSCP00070003842; ENSSSCG00070002505.
DR Ensembl; ENSSSCT00070004693; ENSSSCP00070003846; ENSSSCG00070002505.
DR GeneID; 780421; -.
DR KEGG; ssc:780421; -.
DR CTD; 1240; -.
DR VGNC; VGNC:86800; CMKLR1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230438; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; B1PHQ8; -.
DR OMA; TACVVIW; -.
DR OrthoDB; 910274at2759; -.
DR TreeFam; TF330976; -.
DR Reactome; R-SSC-373076; Class A/1 (Rhodopsin-like receptors).
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Chromosome 14.
DR Bgee; ENSSSCG00000031346; Expressed in lung and 36 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..363
FT /note="Chemerin-like receptor 1"
FT /id="PRO_0000411103"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 337..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 338
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35786"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 363 AA; 41384 MW; 9A821FB879CA6C4D CRC64;
MDFEDYNSTY EDSYTDDFDT IVALEEFSPL EGRVVRIFLV VVYSIICFLG ILGNGLVIVI
ATFKMKKTVN TVWFLNLAVA DFLFNVFLPI HIAYAAMDYH WVFGTAMCKI SNFLLIHNMY
TSVFLLTVIS FDRCISVLLP VWSQNHRSIR LAYMACVVIW VLAFFLSSPS LVFRDTAHLH
GKISCFNNFS LSATSSSSWP THPQMDTVGF GRQMVVTITR FLCGFLVPVL IISACYFTIV
YKLRRNRLAK TKKPFKIIVT IIITFFLCWC PYHTLYLLEL HHRAMPGSVF SLGVPLATAI
AIANSCMNPI LYVFMGQDFK KFKVALFSRL VNALSEDTGH SSYPSHRSFT KMSSMNERET
SML
