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UCP3_MOUSE
ID   UCP3_MOUSE              Reviewed;         308 AA.
AC   P56501; O88293;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Mitochondrial uncoupling protein 3;
DE            Short=UCP 3;
DE   AltName: Full=Solute carrier family 25 member 9;
GN   Name=Ucp3; Synonyms=Slc25a9;
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 [MRNA].
RC   STRAIN=BALB/cJ;
RA   Sanchis D., Fleury C., Bouillaud F., Ricquier D.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster; TISSUE=Embryo;
RX   PubMed=9666083; DOI=10.1016/s0378-1119(98)00279-0;
RA   Yoshitomi H., Yamazaki K., Tanaka I.;
RT   "Cloning of mouse uncoupling protein 3 cDNA and 5'-flanking region, and its
RT   genetic map.";
RL   Gene 215:77-84(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RA   Grujic D., Zhan C.-Y., Sleiker L.J., Lowell B.B.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RA   Son C., Hosoda K., Matsuda J., Nakao K.;
RT   "Cloning of mouse UCP3 cDNA.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10066417; DOI=10.1006/bbrc.1999.0239;
RA   Gong D.W., He Y., Reitman M.L.;
RT   "Genomic organization and regulation by dietary fat of the uncoupling
RT   protein 3 and 2 genes.";
RL   Biochem. Biophys. Res. Commun. 256:27-32(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 84-180.
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RX   PubMed=9600108; DOI=10.1006/bbrc.1998.8600;
RA   Shimokawa T., Kato M., Ezaki O., Hashimoto S.;
RT   "Transcriptional regulation of muscle-specific genes during myoblast
RT   differentiation.";
RL   Biochem. Biophys. Res. Commun. 246:287-292(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 162-252.
RA   Yan X., Ramsay T.G.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, and Heart;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: UCP are mitochondrial transporter proteins that create proton
CC       leaks across the inner mitochondrial membrane, thus uncoupling
CC       oxidative phosphorylation. As a result, energy is dissipated in the
CC       form of heat. May play a role in the modulation of tissue respiratory
CC       control. Participates in thermogenesis and energy balance (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; AF032902; AAB87084.1; -; mRNA.
DR   EMBL; AB010742; BAA25697.1; -; mRNA.
DR   EMBL; AF030164; AAD01892.1; -; mRNA.
DR   EMBL; AB008216; BAA33502.1; -; mRNA.
DR   EMBL; AF053352; AAC28328.1; -; mRNA.
DR   EMBL; AB013132; BAA31989.1; -; mRNA.
DR   EMBL; AF019883; AAB71543.1; -; mRNA.
DR   CCDS; CCDS21497.1; -.
DR   RefSeq; NP_033490.1; NM_009464.3.
DR   AlphaFoldDB; P56501; -.
DR   CORUM; P56501; -.
DR   STRING; 10090.ENSMUSP00000032958; -.
DR   iPTMnet; P56501; -.
DR   PhosphoSitePlus; P56501; -.
DR   MaxQB; P56501; -.
DR   PaxDb; P56501; -.
DR   PRIDE; P56501; -.
DR   ProteomicsDB; 298428; -.
DR   Antibodypedia; 4388; 285 antibodies from 33 providers.
DR   DNASU; 22229; -.
DR   Ensembl; ENSMUST00000032958; ENSMUSP00000032958; ENSMUSG00000032942.
DR   Ensembl; ENSMUST00000107059; ENSMUSP00000102674; ENSMUSG00000032942.
DR   GeneID; 22229; -.
DR   KEGG; mmu:22229; -.
DR   UCSC; uc009ina.1; mouse.
DR   CTD; 7352; -.
DR   MGI; MGI:1099787; Ucp3.
DR   VEuPathDB; HostDB:ENSMUSG00000032942; -.
DR   eggNOG; KOG0753; Eukaryota.
DR   GeneTree; ENSGT00940000161030; -.
DR   HOGENOM; CLU_015166_14_2_1; -.
DR   InParanoid; P56501; -.
DR   OMA; DCMLKLV; -.
DR   OrthoDB; 984118at2759; -.
DR   PhylomeDB; P56501; -.
DR   TreeFam; TF323211; -.
DR   Reactome; R-MMU-167826; The fatty acid cycling model.
DR   Reactome; R-MMU-167827; The proton buffering model.
DR   BioGRID-ORCS; 22229; 5 hits in 73 CRISPR screens.
DR   ChiTaRS; Ucp3; mouse.
DR   PRO; PR:P56501; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P56501; protein.
DR   Bgee; ENSMUSG00000032942; Expressed in hindlimb stylopod muscle and 92 other tissues.
DR   ExpressionAtlas; P56501; baseline and differential.
DR   Genevisible; P56501; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IMP:MGI.
DR   GO; GO:0017077; F:oxidative phosphorylation uncoupler activity; IMP:MGI.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:1990845; P:adaptive thermogenesis; IBA:GO_Central.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR   GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
DR   GO; GO:1990542; P:mitochondrial transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006839; P:mitochondrial transport; IEA:InterPro.
DR   GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR   GO; GO:0009409; P:response to cold; IBA:GO_Central.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR   GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR   GO; GO:0000303; P:response to superoxide; IMP:MGI.
DR   Gene3D; 1.50.40.10; -; 1.
DR   InterPro; IPR002030; Mit_uncoupling_UCP-like.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00784; MTUNCOUPLING.
DR   SUPFAM; SSF103506; SSF103506; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..308
FT                   /note="Mitochondrial uncoupling protein 3"
FT                   /id="PRO_0000090673"
FT   TRANSMEM        11..32
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..96
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..133
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..196
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..233
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..290
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          11..102
FT                   /note="Solcar 1"
FT   REPEAT          111..202
FT                   /note="Solcar 2"
FT   REPEAT          211..296
FT                   /note="Solcar 3"
FT   REGION          275..297
FT                   /note="Purine nucleotide binding"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        179
FT                   /note="W -> L (in Ref. 6; BAA31989)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   308 AA;  33911 MW;  12CAD7674DF7D0C3 CRC64;
     MVGLQPSEVP PTTVVKFLGA GTAACFADLL TFPLDTAKVR LQIQGENPGA QSVQYRGVLG
     TILTMVRTEG PRSPYSGLVA GLHRQMSFAS IRIGLYDSVK QFYTPKGADH SSVAIRILAG
     CTTGAMAVTC AQPTDVVKVR FQAMIRLGTG GERKYRGTMD AYRTIAREEG VRGLWKGTWP
     NITRNAIVNC AEMVTYDIIK EKLLESHLFT DNFPCHFVSA FGAGFCATVV ASPVDVVKTR
     YMNAPLGRYR SPLHCMLKMV AQEGPTAFYK GFVPSFLRLG AWNVMMFVTY EQLKRALMKV
     QVLRESPF
 
 
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