UCP2_MOUSE
ID UCP2_MOUSE Reviewed; 309 AA.
AC P70406; O88285;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Mitochondrial uncoupling protein 2;
DE Short=UCP 2;
DE AltName: Full=Solute carrier family 25 member 8;
DE AltName: Full=UCPH;
GN Name=Ucp2; Synonyms=Slc25a8;
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.
RC STRAIN=BALB/cJ; TISSUE=Muscle;
RA Raimbault S., Bouillaud F., Ricquier D.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Spleen;
RX PubMed=9133562; DOI=10.2337/diab.46.5.900;
RA Gimeno R.E., Dembski M., Weng X., Deng N., Shyjan A.W., Gimeno C.J.,
RA Iris F., Ellis S.J., Woolf E.A., Tartaglia L.A.;
RT "Cloning and characterization of an uncoupling protein homolog: a potential
RT molecular mediator of human thermogenesis.";
RL Diabetes 46:900-906(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6 X CBA;
RX PubMed=9710252; DOI=10.1016/s0014-5793(98)00835-7;
RA Yamada M., Hashida T., Shibusawa N., Iwasaki T., Murakami M., Monden T.,
RA Satoh T., Mori M.;
RT "Genomic organization and promoter function of the mouse uncoupling protein
RT 2 (UCP2) gene.";
RL FEBS Lett. 432:65-69(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, and Mammary gland;
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 [5]
RP STRUCTURE BY NMR OF 14-309, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=21785437; DOI=10.1038/nature10257;
RA Berardi M.J., Shih W.M., Harrison S.C., Chou J.J.;
RT "Mitochondrial uncoupling protein 2 structure determined by NMR molecular
RT fragment searching.";
RL Nature 476:109-113(2011).
CC -!- FUNCTION: UCP are mitochondrial transporter proteins that create proton
CC leaks across the inner mitochondrial membrane, thus uncoupling
CC oxidative phosphorylation from ATP synthesis. As a result, energy is
CC dissipated in the form of heat (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Acts as a dimer forming a proton channel. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:21785437}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21785437}.
CC -!- TISSUE SPECIFICITY: Highest in white adipose tissue, also detected in
CC brown adipose tissue, heart and kidney. 4-6 times higher levels are
CC detected in ob/ob and db/db mice.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; U69135; AAB17666.1; -; mRNA.
DR EMBL; U94593; AAB53092.1; -; mRNA.
DR EMBL; AB012159; BAA32532.1; -; Genomic_DNA.
DR EMBL; BC012697; AAH12697.1; -; mRNA.
DR EMBL; BC012967; AAH12967.1; -; mRNA.
DR CCDS; CCDS21498.1; -.
DR RefSeq; NP_035801.3; NM_011671.5.
DR RefSeq; XP_006507642.1; XM_006507579.2.
DR PDB; 2LCK; NMR; -; A=14-309.
DR PDBsum; 2LCK; -.
DR AlphaFoldDB; P70406; -.
DR BMRB; P70406; -.
DR SMR; P70406; -.
DR STRING; 10090.ENSMUSP00000120967; -.
DR PhosphoSitePlus; P70406; -.
DR EPD; P70406; -.
DR PaxDb; P70406; -.
DR PRIDE; P70406; -.
DR ProteomicsDB; 298427; -.
DR Antibodypedia; 31003; 415 antibodies from 40 providers.
DR DNASU; 22228; -.
DR Ensembl; ENSMUST00000126534; ENSMUSP00000120967; ENSMUSG00000033685.
DR GeneID; 22228; -.
DR KEGG; mmu:22228; -.
DR UCSC; uc009inb.3; mouse.
DR CTD; 7351; -.
DR MGI; MGI:109354; Ucp2.
DR VEuPathDB; HostDB:ENSMUSG00000033685; -.
DR eggNOG; KOG0753; Eukaryota.
DR GeneTree; ENSGT00940000159524; -.
DR HOGENOM; CLU_015166_14_2_1; -.
DR InParanoid; P70406; -.
DR OMA; MMAANHS; -.
DR OrthoDB; 1126848at2759; -.
DR PhylomeDB; P70406; -.
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; 22228; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Ucp2; mouse.
DR PRO; PR:P70406; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P70406; protein.
DR Bgee; ENSMUSG00000033685; Expressed in blood and 241 other tissues.
DR ExpressionAtlas; P70406; baseline and differential.
DR Genevisible; P70406; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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; HDA:MGI.
DR GO; GO:0017077; F:oxidative phosphorylation uncoupler activity; IBA:GO_Central.
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:0034198; P:cellular response to amino acid starvation; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:1990542; P:mitochondrial transmembrane transport; IBA:GO_Central.
DR GO; GO:0006839; P:mitochondrial transport; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL.
DR GO; GO:0009409; P:response to cold; IBA:GO_Central.
DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0000303; P:response to superoxide; ISO: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 3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..309
FT /note="Mitochondrial uncoupling protein 2"
FT /id="PRO_0000090665"
FT TOPO_DOM 1..10
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..77
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..119
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..180
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..197
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..214
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..234
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..268
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..291
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..309
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT REPEAT 11..106
FT /note="Solcar 1"
FT REPEAT 114..203
FT /note="Solcar 2"
FT REPEAT 212..297
FT /note="Solcar 3"
FT REGION 276..298
FT /note="Purine nucleotide binding"
FT /evidence="ECO:0000250"
FT CONFLICT 285
FT /note="V -> I (in Ref. 3; BAA32532)"
FT /evidence="ECO:0000305"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:2LCK"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 116..133
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:2LCK"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 172..202
FT /evidence="ECO:0007829|PDB:2LCK"
FT TURN 203..208
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 214..242
FT /evidence="ECO:0007829|PDB:2LCK"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 274..295
FT /evidence="ECO:0007829|PDB:2LCK"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:2LCK"
SQ SEQUENCE 309 AA; 33374 MW; 329794EEA99810E5 CRC64;
MVGFKATDVP PTATVKFLGA GTAACIADLI TFPLDTAKVR LQIQGESQGL VRTAASAQYR
GVLGTILTMV RTEGPRSLYN GLVAGLQRQM SFASVRIGLY DSVKQFYTKG SEHAGIGSRL
LAGSTTGALA VAVAQPTDVV KVRFQAQARA GGGRRYQSTV EAYKTIAREE GIRGLWKGTS
PNVARNAIVN CAELVTYDLI KDTLLKANLM TDDLPCHFTS AFGAGFCTTV IASPVDVVKT
RYMNSALGQY HSAGHCALTM LRKEGPRAFY KGFMPSFLRL GSWNVVMFVT YEQLKRALMA
AYQSREAPF
