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UCP2_RAT
ID   UCP2_RAT                Reviewed;         309 AA.
AC   P56500; O70178; O88183; Q6GST1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Mitochondrial uncoupling protein 2;
DE            Short=UCP 2;
DE   AltName: Full=Solute carrier family 25 member 8;
GN   Name=Ucp2; Synonyms=Slc25a8;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=White adipose tissue;
RA   Strobel A., Strosberg A.D., Issad T.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brown adipose tissue;
RX   PubMed=9414126; DOI=10.1016/s0014-5793(97)01381-1;
RA   Matsuda J., Hosoda K., Itoh H., Son C., Doi K., Tanaka T., Fukunaga Y.,
RA   Inoue G., Nishimura H., Yoshimasa Y., Yamori Y., Nakao K.;
RT   "Cloning of rat uncoupling protein-3 and uncoupling protein-2 cDNAs: their
RT   gene expression in rats fed high-fat diet.";
RL   FEBS Lett. 418:200-204(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Spleen;
RA   Yamazaki K., Yoshitomi H., Tanaka I.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Brain;
RX   PubMed=9512646; DOI=10.1016/s0005-2760(97)00188-4;
RA   Hidaka S., Kakuma T., Yoshimatsu H., Yasunaga S., Kurokawa M., Sakata T.;
RT   "Molecular cloning of rat uncoupling protein 2 cDNA and its expression in
RT   genetically obese Zucker fatty (fa/fa) rats.";
RL   Biochim. Biophys. Acta 1389:178-186(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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).
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; Multi-pass membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed in a variety of organs, with predominant
CC       expression in the heart, lung and spleen.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; AF039033; AAC98733.1; -; mRNA.
DR   EMBL; AB006613; BAA23383.1; -; mRNA.
DR   EMBL; AB010743; BAA25698.1; -; mRNA.
DR   EMBL; AB005143; BAA28832.1; -; mRNA.
DR   EMBL; BC062230; AAH62230.1; -; mRNA.
DR   RefSeq; NP_062227.2; NM_019354.3.
DR   AlphaFoldDB; P56500; -.
DR   BMRB; P56500; -.
DR   STRING; 10116.ENSRNOP00000024156; -.
DR   PhosphoSitePlus; P56500; -.
DR   PaxDb; P56500; -.
DR   PRIDE; P56500; -.
DR   Ensembl; ENSRNOT00000024156; ENSRNOP00000024156; ENSRNOG00000017854.
DR   GeneID; 54315; -.
DR   KEGG; rno:54315; -.
DR   UCSC; RGD:3932; rat.
DR   CTD; 7351; -.
DR   RGD; 3932; Ucp2.
DR   eggNOG; KOG0753; Eukaryota.
DR   GeneTree; ENSGT00940000159524; -.
DR   HOGENOM; CLU_015166_14_2_1; -.
DR   InParanoid; P56500; -.
DR   OMA; MMAANHS; -.
DR   OrthoDB; 1126848at2759; -.
DR   PhylomeDB; P56500; -.
DR   TreeFam; TF323211; -.
DR   Reactome; R-RNO-167826; The fatty acid cycling model.
DR   Reactome; R-RNO-167827; The proton buffering model.
DR   PRO; PR:P56500; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000017854; Expressed in spleen and 19 other tissues.
DR   Genevisible; P56500; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
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; IDA:RGD.
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; IEP:RGD.
DR   GO; GO:0034198; P:cellular response to amino acid starvation; IEP:RGD.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR   GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR   GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR   GO; GO:1990542; P:mitochondrial transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006839; P:mitochondrial transport; IDA:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR   GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:RGD.
DR   GO; GO:0009409; P:response to cold; IBA:GO_Central.
DR   GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR   GO; GO:0009749; P:response to glucose; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0000303; P:response to superoxide; IDA:RGD.
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   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..309
FT                   /note="Mitochondrial uncoupling protein 2"
FT                   /id="PRO_0000090667"
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        9
FT                   /note="V -> L (in Ref. 4; BAA28832)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        268
FT                   /note="A -> T (in Ref. 3; BAA25698 and 5; AAH62230)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   309 AA;  33377 MW;  3297935CF997AA0E CRC64;
     MVGFKATDVP PTATVKFLGA GTAACIADLI TFPLDTAKVR LQIQGESQGL ARTAASAQYR
     GVLGTILTMV RTEGPRSLYN GLVAGLQRQM SFASVRIGLY DSVKQFYTKG SEHAGIGSRL
     LAGSTTGALA VAVAQPTDVV KVRFQAQARA GGGRRYQSTV EAYKTIAREE GIRGLWKGTS
     PNVARNAIVN CTELVTYDLI KDTLLKANLM TDDLPCHFTS AFGAGFCTTV IASPVDVVKT
     RYMNSALGQY HSAGHCALTM LRKEGPRAFY KGFMPSFLRL GSWNVVMFVT YEQLKRALMA
     AYESREAPF
 
 
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