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CML2_MOUSE
ID   CML2_MOUSE              Reviewed;         353 AA.
AC   Q8K087;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 139.
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|MGI:MGI:2385324};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=24895415; DOI=10.1530/joe-14-0069;
RA   Rourke J.L., Muruganandan S., Dranse H.J., McMullen N.M., Sinal C.J.;
RT   "Gpr1 is an active chemerin receptor influencing glucose homeostasis in
RT   obese mice.";
RL   J. Endocrinol. 222:201-215(2014).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=29799787; DOI=10.1096/fj.201800020rrr;
RA   Zheng C., Chen D., Zhang Y., Bai Y., Huang S., Zheng D., Liang W., She S.,
RA   Peng X., Wang P., Mo X., Song Q., Lv P., Huang J., Ye R.D., Wang Y.;
RT   "FAM19A1 is a new ligand for GPR1 that modulates neural stem-cell
RT   proliferation and differentiation.";
RL   FASEB J. 0:0-0(2018).
CC   -!- FUNCTION: Receptor for chemoattractant adipokine chemerin/RARRES2
CC       suggesting a role for this receptor in the regulation of inflammation
CC       and energy homesotasis (PubMed:24895415). 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 (PubMed:29799787).
CC       {ECO:0000269|PubMed:24895415, ECO:0000269|PubMed:29799787}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29799787};
CC       Multi-pass membrane protein {ECO:0000255}. Note=Internalizes in
CC       presence of its ligand, TAFA1 (PubMed:29799787). Internalizes
CC       efficiently in response to RARRES2 (By similarity).
CC       {ECO:0000250|UniProtKB:P46091, ECO:0000269|PubMed:29799787}.
CC   -!- TISSUE SPECIFICITY: High expressed in white adipose tissue and skeletal
CC       muscle (PubMed:24895415). Expressed in hippocampus and cortex
CC       (PubMed:29799787). {ECO:0000269|PubMed:24895415,
CC       ECO:0000269|PubMed:29799787}.
CC   -!- DISRUPTION PHENOTYPE: Deficient mice have normal body weight, adipose
CC       development, and tissue inflammation under physiologic conditions.
CC       However, when fed on a high-fat diet, Cmklr2 knockout mice develop
CC       heightened glucose intolerance, compared with WT, with no effect on
CC       body weight, percent body fat, or energy expenditure due to consumption
CC       of significantly less food. Moreover, mice lacking Cmklr2 exhibited
CC       reduced glucose-stimulated insulin levels and elevated glucose levels
CC       in a pyruvate tolerance test. {ECO:0000269|PubMed:24895415}.
CC   -!- SIMILARITY: Belongs to the chemokine-like receptor (CMKLR) family.
CC       {ECO:0000305}.
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DR   EMBL; AL645950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC032934; AAH32934.1; -; mRNA.
DR   CCDS; CCDS14998.1; -.
DR   RefSeq; NP_666362.1; NM_146250.2.
DR   RefSeq; XP_006496043.1; XM_006495980.2.
DR   RefSeq; XP_006496044.1; XM_006495981.2.
DR   RefSeq; XP_011236820.1; XM_011238518.2.
DR   RefSeq; XP_011236821.1; XM_011238519.2.
DR   AlphaFoldDB; Q8K087; -.
DR   SMR; Q8K087; -.
DR   STRING; 10090.ENSMUSP00000051417; -.
DR   GlyGen; Q8K087; 1 site.
DR   PhosphoSitePlus; Q8K087; -.
DR   PaxDb; Q8K087; -.
DR   PRIDE; Q8K087; -.
DR   Antibodypedia; 1410; 242 antibodies from 31 providers.
DR   DNASU; 241070; -.
DR   Ensembl; ENSMUST00000050536; ENSMUSP00000051417; ENSMUSG00000046856.
DR   GeneID; 241070; -.
DR   KEGG; mmu:241070; -.
DR   UCSC; uc007bga.3; mouse.
DR   CTD; 241070; -.
DR   MGI; MGI:2385324; Gpr1.
DR   VEuPathDB; HostDB:ENSMUSG00000046856; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000160642; -.
DR   HOGENOM; CLU_009579_8_0_1; -.
DR   InParanoid; Q8K087; -.
DR   OMA; ISSKHFW; -.
DR   OrthoDB; 910274at2759; -.
DR   PhylomeDB; Q8K087; -.
DR   TreeFam; TF330976; -.
DR   BioGRID-ORCS; 241070; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Gpr1; mouse.
DR   PRO; PR:Q8K087; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8K087; protein.
DR   Bgee; ENSMUSG00000046856; Expressed in primary oocyte and 57 other tissues.
DR   Genevisible; Q8K087; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IMP: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   2: Evidence at transcript level;
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_0000069508"
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"
SQ   SEQUENCE   353 AA;  40951 MW;  A7793FEC0409C0A2 CRC64;
     MEVSKEMLFE ELDNYSYALD YYSQESDPEE KVYLGLVHWI SLFLYALAFV LGIPGNAIVI
     WLMGFKWKKT VTTLWFLNLA IADFIFVLFL PLYISYVALS FHWPFGLWLC KVNSFIAQLN
     MFSSVFFLTV ISLDRYIHLL HPGLSHRHRT LKSSLVVVIL VWLLASLLGG PTLYFRDTME
     VNNHIICYNN FQEHELTLMR HHVLTWVKFL FGYLFPLLTM SSCYLCLIFK MKKRNILISR
     KHLWMILSVV IAFLVCWTPY HLFSIWELSI HHNSSFQNVL QGGIPLSTGL AFLNSCLNPI
     LYVLISKTFQ ARFRASVAEV LKRSLWEASC SGTVSEQLRS AETKSLSLLE TAQ
 
 
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