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P97468 (CML1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chemokine-like receptor 1
Alternative name(s):
G-protein coupled receptor DEZ
Gene names
Name:Cmklr1
Synonyms:Dez, Gpcr27
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for the chemoattractant adipokine chemerin/RARRES2 and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with RARRES2 induces activation of intracellular signaling molecules, such as SKY, MAPK1/3 (ERK1/2), MAPK14/P38MAPK and PI3K leading to multifunctional effects, like reduction of immune responses, enhancing of adipogenesis and angionesis. Resolvin E1 down-regulates cytokine production in macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-kappa-B By similarity. Positively regulates adipogenesis and adipocyte metabolism. Ref.2 Ref.3 Ref.5

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.3.

Tissue specificity

Expressed in the differentiated adipocytes (at protein level). Ubiquitous. Highly expressed in adipose tissue and immature plasmacytoid dendritic cells (DCs) and at lower levels in myeloid DCs, macrophages, and NK cells. Expressed on macrophages isolated from different tissues, including peritoneal cavities, pleural cavities and spleen. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7

Developmental stage

Expressed during bone development and in adult parathyroid glands. Expressed at day E11 in the caudal part of the tongue and the umbilical cord and the expression in the tongue was maintained throughout adulthood. Expression increases in bone and cartilaginous forming zones of embryo up to stage E14.5 and at E16.5 expression is seen in the lung. Ref.1

Induction

Down-regulated by bacterial lipopolysaccharide (LPS), IFN-alpha and TNF on macrophages. Ref.3

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 371371Chemokine-like receptor 1
PRO_0000069308

Regions

Topological domain1 – 3939Extracellular Potential
Transmembrane40 – 6223Helical; Name=1; Potential
Topological domain63 – 7311Cytoplasmic Potential
Transmembrane74 – 9522Helical; Name=2; Potential
Topological domain96 – 11217Extracellular Potential
Transmembrane113 – 13321Helical; Name=3; Potential
Topological domain134 – 15219Cytoplasmic Potential
Transmembrane153 – 17422Helical; Name=4; Potential
Topological domain175 – 22248Extracellular Potential
Transmembrane223 – 24321Helical; Name=5; Potential
Topological domain244 – 25916Cytoplasmic Potential
Transmembrane260 – 28021Helical; Name=6; Potential
Topological domain281 – 29818Extracellular Potential
Transmembrane299 – 31820Helical; Name=7; Potential
Topological domain319 – 37153Cytoplasmic Potential

Amino acid modifications

Glycosylation71N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Disulfide bond110 ↔ 187 Potential

Sequences

Sequence LengthMass (Da)Tools
P97468 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: CDBE19305244C0B3

FASTA37141,815
        10         20         30         40         50         60 
MEYDAYNDSG IYDDEYSDGF GYFVDLEEAS PWEAKVAPVF LVVIYSLVCF LGLLGNGLVI 

        70         80         90        100        110        120 
VIATFKMKKT VNTVWFVNLA VADFLFNIFL PMHITYAAMD YHWVFGKAMC KISNFLLSHN 

       130        140        150        160        170        180 
MYTSVFLLTV ISFDRCISVL LPVWSQNHRS IRLAYMTCSA VWVLAFFLSS PSLVFRDTAN 

       190        200        210        220        230        240 
IHGKITCFNN FSLAAPESSP HPAHSQVVST GYSRHVAVTV TRFLCGFLIP VFIITACYLT 

       250        260        270        280        290        300 
IVFKLQRNRL AKNKKPFKII ITIIITFFLC WCPYHTLYLL ELHHTAVPSS VFSLGLPLAT 

       310        320        330        340        350        360 
AVAIANSCMN PILYVFMGHD FRKFKVALFS RLANALSEDT GPSSYPSHRS FTKMSSLNEK 

       370 
ASVNEKETST L 

« Hide

References

[1]"A novel G protein-coupled receptor with homology to neuropeptide and chemoattractant receptors expressed during bone development."
Methner A., Hermey G., Schinke B., Hermans-Borgmeyer I.
Biochem. Biophys. Res. Commun. 233:336-342(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
Tissue: Brain.
[2]"Stereochemical assignment, antiinflammatory properties, and receptor for the omega-3 lipid mediator resolvin E1."
Arita M., Bianchini F., Aliberti J., Sher A., Chiang N., Hong S., Yang R., Petasis N.A., Serhan C.N.
J. Exp. Med. 201:713-722(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: LIGAND-BINDING, FUNCTION.
[3]"Chemokine-like receptor 1 expression by macrophages in vivo: regulation by TGF-beta and TLR ligands."
Zabel B.A., Ohyama T., Zuniga L., Kim J.Y., Johnston B., Allen S.J., Guido D.G., Handel T.M., Butcher E.C.
Exp. Hematol. 34:1106-1114(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Chemerin--a new adipokine that modulates adipogenesis via its own receptor."
Roh S.G., Song S.H., Choi K.C., Katoh K., Wittamer V., Parmentier M., Sasaki S.
Biochem. Biophys. Res. Commun. 362:1013-1018(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"Chemerin, a novel adipokine that regulates adipogenesis and adipocyte metabolism."
Goralski K.B., McCarthy T.C., Hanniman E.A., Zabel B.A., Butcher E.C., Parlee S.D., Muruganandan S., Sinal C.J.
J. Biol. Chem. 282:28175-28188(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[6]"Chemerin enhances insulin signaling and potentiates insulin-stimulated glucose uptake in 3T3-L1 adipocytes."
Takahashi M., Takahashi Y., Takahashi K., Zolotaryov F.N., Hong K.S., Kitazawa R., Iida K., Okimura Y., Kaji H., Kitazawa S., Kasuga M., Chihara K.
FEBS Lett. 582:573-578(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Mouse ChemR23 is expressed in dendritic cell subsets and macrophages, and mediates an anti-inflammatory activity of chemerin in a lung disease model."
Luangsay S., Wittamer V., Bondue B., De Henau O., Rouger L., Brait M., Franssen J.D., de Nadai P., Huaux F., Parmentier M.
J. Immunol. 183:6489-6499(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U79525 mRNA. Translation: AAB53789.1.
CCDSCCDS19551.1.
PIRJC5498.
RefSeqNP_032179.1. NM_008153.3.
XP_006530227.1. XM_006530164.1.
XP_006530228.1. XM_006530165.1.
XP_006530229.1. XM_006530166.1.
XP_006530230.1. XM_006530167.1.
UniGeneMm.5196.

3D structure databases

ProteinModelPortalP97468.
SMRP97468. Positions 36-322.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY79.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP97468.

Proteomic databases

PRIDEP97468.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047936; ENSMUSP00000036316; ENSMUSG00000042190.
GeneID14747.
KEGGmmu:14747.
UCSCuc012ebo.1. mouse.

Organism-specific databases

CTD1240.
MGIMGI:109603. Cmklr1.

Phylogenomic databases

eggNOGNOG150376.
HOGENOMHOG000234122.
HOVERGENHBG107927.
InParanoidP97468.
KOK04245.
OMAACYLTIV.
OrthoDBEOG7SR4MM.
PhylomeDBP97468.
TreeFamTF330976.

Gene expression databases

ArrayExpressP97468.
BgeeP97468.
CleanExMM_CMKLR1.
GenevestigatorP97468.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000355. Chemokine_rcpt.
IPR002258. DEZorph_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24227. PTHR24227. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR01126. DEZORPHANR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCMKLR1. mouse.
NextBio286807.
PROP97468.
SOURCESearch...

Entry information

Entry nameCML1_MOUSE
AccessionPrimary (citable) accession number: P97468
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries