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MC3R_MOUSE
ID   MC3R_MOUSE              Reviewed;         323 AA.
AC   P33033;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Melanocortin receptor 3;
DE            Short=MC3-R;
GN   Name=Mc3r;
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 [GENOMIC DNA].
RX   PubMed=8172596; DOI=10.1042/bj2990367;
RA   Desarnaud F., Labbe O., Eggerickx D., Vassart G., Parmentier M.;
RT   "Molecular cloning, functional expression and pharmacological
RT   characterization of a mouse melanocortin receptor gene.";
RL   Biochem. J. 299:367-373(1994).
RN   [2]
RP   FUNCTION.
RX   PubMed=19036988; DOI=10.1523/jneurosci.3615-08.2008;
RA   Sutton G.M., Perez-Tilve D., Nogueiras R., Fang J., Kim J.K., Cone R.D.,
RA   Gimble J.M., Tschop M.H., Butler A.A.;
RT   "The melanocortin-3 receptor is required for entrainment to meal intake.";
RL   J. Neurosci. 28:12946-12955(2008).
CC   -!- FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. This
CC       receptor is mediated by G proteins which activate adenylate cyclase.
CC       Required for expression of anticipatory patterns of activity and
CC       wakefulness during periods of limited nutrient availability and for the
CC       normal regulation of circadian clock activity in the brain
CC       (PubMed:19036988). {ECO:0000269|PubMed:19036988}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X74983; CAA52918.1; -; Genomic_DNA.
DR   CCDS; CCDS17127.1; -.
DR   PIR; S43850; S43850.
DR   RefSeq; NP_032587.1; NM_008561.3.
DR   AlphaFoldDB; P33033; -.
DR   SMR; P33033; -.
DR   BioGRID; 201340; 1.
DR   STRING; 10090.ENSMUSP00000047358; -.
DR   BindingDB; P33033; -.
DR   ChEMBL; CHEMBL4774; -.
DR   GuidetoPHARMACOLOGY; 284; -.
DR   GlyGen; P33033; 3 sites.
DR   PaxDb; P33033; -.
DR   PRIDE; P33033; -.
DR   Antibodypedia; 2935; 346 antibodies from 37 providers.
DR   DNASU; 17201; -.
DR   Ensembl; ENSMUST00000038532; ENSMUSP00000047358; ENSMUSG00000038537.
DR   GeneID; 17201; -.
DR   KEGG; mmu:17201; -.
DR   UCSC; uc008ocl.1; mouse.
DR   CTD; 4159; -.
DR   MGI; MGI:96929; Mc3r.
DR   VEuPathDB; HostDB:ENSMUSG00000038537; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234510; -.
DR   HOGENOM; CLU_009579_13_0_1; -.
DR   InParanoid; P33033; -.
DR   OMA; TCMKGAV; -.
DR   OrthoDB; 1037679at2759; -.
DR   PhylomeDB; P33033; -.
DR   TreeFam; TF332646; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   BioGRID-ORCS; 17201; 2 hits in 73 CRISPR screens.
DR   PRO; PR:P33033; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P33033; protein.
DR   Bgee; ENSMUSG00000038537; Expressed in gastrula and 22 other tissues.
DR   ExpressionAtlas; P33033; baseline and differential.
DR   Genevisible; P33033; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0004977; F:melanocortin receptor activity; ISO:MGI.
DR   GO; GO:0004980; F:melanocyte-stimulating hormone receptor activity; IDA:MGI.
DR   GO; GO:0042923; F:neuropeptide binding; ISO:MGI.
DR   GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0042309; P:homoiothermy; ISO:MGI.
DR   GO; GO:0045475; P:locomotor rhythm; IMP:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
DR   GO; GO:0060259; P:regulation of feeding behavior; IMP:UniProtKB.
DR   GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
DR   GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR   GO; GO:0055078; P:sodium ion homeostasis; IEA:Ensembl.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001908; MC3-5R.
DR   InterPro; IPR002122; Mcort_3_rcpt.
DR   InterPro; IPR001671; Melcrt_ACTH_rcpt.
DR   PANTHER; PTHR22750:SF4; PTHR22750:SF4; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00534; MCRFAMILY.
DR   PRINTS; PR00535; MELNOCORTINR.
DR   PRINTS; PR01061; MELNOCORTN3R.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
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   Biological rhythms; Cell membrane; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..323
FT                   /note="Melanocortin receptor 3"
FT                   /id="PRO_0000069719"
FT   TOPO_DOM        1..37
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..63
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..75
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..100
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..118
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..140
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..160
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..186
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..210
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..245
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..268
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        269..277
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..301
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..323
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           315
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        16
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   323 AA;  35806 MW;  F4B7B02FA4A87B7B CRC64;
     MNSSCCLSSV SPMLPNLSEH PAAPPASNRS GSGFCEQVFI KPEVFLALGI VSLMENILVI
     LAVVRNGNLH SPMYFFLCSL AAADMLVSLS NSLETIMIAV INSDSLTLED QFIQHMDNIF
     DSMICISLVA SICNLLAIAI DRYVTIFYAL RYHSIMTVRK ALTLIGVIWV CCGICGVMFI
     IYSESKMVIV CLITMFFAMV LLMGTLYIHM FLFARLHVQR IAVLPPAGVV APQQHSCMKG
     AVTITILLGV FIFCWAPFFL HLVLIITCPT NPYCICYTAH FNTYLVLIMC NSVIDPLIYA
     FRSLELRNTF KEILCGCNSM NLG
 
 
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