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UCP1_BOVIN
ID   UCP1_BOVIN              Reviewed;         309 AA.
AC   P10861; F1MTU3;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 3.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Mitochondrial brown fat uncoupling protein 1 {ECO:0000305};
DE            Short=UCP 1 {ECO:0000305};
DE   AltName: Full=Solute carrier family 25 member 7 {ECO:0000250|UniProtKB:P25874};
DE   AltName: Full=Thermogenin {ECO:0000250|UniProtKB:P04575};
GN   Name=UCP1 {ECO:0000250|UniProtKB:P25874};
GN   Synonyms=SLC25A7 {ECO:0000250|UniProtKB:P25874},
GN   UCP {ECO:0000303|PubMed:2928121};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-309.
RC   STRAIN=Friesian;
RX   PubMed=2928121; DOI=10.1093/nar/17.5.2131;
RA   Casteilla L., Bouillaud F., Forest C., Ricquier D.;
RT   "Nucleotide sequence of a cDNA encoding bovine brown fat uncoupling
RT   protein. Homology with ADP binding site of ADP/ATP carrier.";
RL   Nucleic Acids Res. 17:2131-2131(1989).
RN   [3]
RP   SEQUENCE REVISION.
RA   Bouillaud F.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mitochondrial protein responsible for thermogenic
CC       respiration, a specialized capacity of brown adipose tissue and beige
CC       fat that participates in non-shivering adaptive thermogenesis to
CC       temperature and diet variations and more generally to the regulation of
CC       energy balance. Functions as a long-chain fatty acid/LCFA and proton
CC       symporter, simultaneously transporting one LCFA and one proton through
CC       the inner mitochondrial membrane. However, LCFAs remaining associated
CC       with the transporter via their hydrophobic tails, it results in an
CC       apparent transport of protons activated by LCFAs. Thereby, dissipates
CC       the mitochondrial proton gradient and converts the energy of substrate
CC       oxydation into heat instead of ATP. Regulates the production of
CC       reactive oxygen species/ROS by mitochondria.
CC       {ECO:0000250|UniProtKB:P12242}.
CC   -!- ACTIVITY REGULATION: Has no constitutive proton transporter activity
CC       and has to be activated by long-chain fatty acids/LCFAs. Inhibited by
CC       purine nucleotides. Both purine nucleotides and LCFAs bind the
CC       cytosolic side of the transporter and directly compete to activate or
CC       inhibit it. Activated by noradrenaline and reactive oxygen species.
CC       {ECO:0000250|UniProtKB:P12242}.
CC   -!- SUBUNIT: Most probably functions as a monomer. Binds one purine
CC       nucleotide per monomer. However, has also been suggested to function as
CC       a homodimer or a homotetramer. Tightly associates with cardiolipin in
CC       the mitochondrion inner membrane; may stabilize and regulate its
CC       activity. {ECO:0000250|UniProtKB:P25874, ECO:0000250|UniProtKB:W5PSH7}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P12242}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P04633}.
CC   -!- PTM: May undergo sulfenylation upon cold exposure. May increase the
CC       sensitivity of UCP1 thermogenic function to the activation by
CC       noradrenaline probably through structural effects.
CC       {ECO:0000250|UniProtKB:P12242}.
CC   -!- PTM: May undergo ubiquitin-mediated proteasomal degradation.
CC       {ECO:0000250|UniProtKB:P04633}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; DAAA02044420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02044421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X14064; CAA32227.1; -; mRNA.
DR   PIR; S03603; S03603.
DR   RefSeq; NP_001160000.1; NM_001166528.1.
DR   AlphaFoldDB; P10861; -.
DR   STRING; 9913.ENSBTAP00000006097; -.
DR   TCDB; 2.A.29.3.1; the mitochondrial carrier (mc) family.
DR   PaxDb; P10861; -.
DR   Ensembl; ENSBTAT00000006097; ENSBTAP00000006097; ENSBTAG00000004647.
DR   GeneID; 281561; -.
DR   KEGG; bta:281561; -.
DR   CTD; 7350; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004647; -.
DR   VGNC; VGNC:36640; UCP1.
DR   eggNOG; KOG0753; Eukaryota.
DR   GeneTree; ENSGT00940000160382; -.
DR   InParanoid; P10861; -.
DR   OMA; YTSVPNC; -.
DR   OrthoDB; 984118at2759; -.
DR   TreeFam; TF323211; -.
DR   Proteomes; UP000009136; Chromosome 17.
DR   Bgee; ENSBTAG00000004647; Expressed in semen and 12 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:1901612; F:cardiolipin binding; ISS:UniProtKB.
DR   GO; GO:0036041; F:long-chain fatty acid binding; ISS:UniProtKB.
DR   GO; GO:0017077; F:oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
DR   GO; GO:0032555; F:purine ribonucleotide binding; ISS:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:1990845; P:adaptive thermogenesis; ISS:UniProtKB.
DR   GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0070417; P:cellular response to cold; IEA:Ensembl.
DR   GO; GO:0071398; P:cellular response to fatty acid; ISS:UniProtKB.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; ISS:UniProtKB.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; ISS:UniProtKB.
DR   GO; GO:0002024; P:diet induced thermogenesis; IEA:Ensembl.
DR   GO; GO:1990542; P:mitochondrial transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006839; P:mitochondrial transport; IEA:InterPro.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR   GO; GO:1902600; P:proton transmembrane transport; ISS:UniProtKB.
DR   GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0009409; P:response to cold; IBA:GO_Central.
DR   GO; GO:0031667; P:response to nutrient levels; ISS:UniProtKB.
DR   GO; GO:0009266; P:response to temperature stimulus; ISS:UniProtKB.
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   InterPro; IPR040011; UCP1.
DR   PANTHER; PTHR45618:SF19; PTHR45618:SF19; 1.
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   Ion channel; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidation; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..309
FT                   /note="Mitochondrial brown fat uncoupling protein 1"
FT                   /id="PRO_0000090654"
FT   TOPO_DOM        2..10
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        11..32
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..77
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        78..100
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..118
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        119..135
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..180
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        181..197
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..214
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        215..234
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..268
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        269..291
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..309
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   REPEAT          11..106
FT                   /note="Solcar 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT   REPEAT          113..203
FT                   /note="Solcar 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT   REPEAT          212..297
FT                   /note="Solcar 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT   MOD_RES         256
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000250|UniProtKB:P12242"
FT   CONFLICT        43..46
FT                   /note="Missing (in Ref. 2; CAA32227)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92
FT                   /note="F -> L (in Ref. 2; CAA32227)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="T -> S (in Ref. 2; CAA32227)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185
FT                   /note="R -> T (in Ref. 2; CAA32227)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        250
FT                   /note="Y -> N (in Ref. 2; CAA32227)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285
FT                   /note="Missing (in Ref. 2; CAA32227)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293
FT                   /note="Q -> R (in Ref. 2; CAA32227)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        301
FT                   /note="S -> C (in Ref. 2; CAA32227)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   309 AA;  33360 MW;  CF085EC5834F7F63 CRC64;
     MVGHTESDVP PTMAVKIFSA GVAACVADII TFPLDTAKVR LQVGSAIQGE CLISSAIRYK
     GVLGTIITLA KTEGPVKLYS GLPAGLQRQI SFASLRIGLY DTVQEFFTTG KEASLGSKIS
     AGLMTGGVAV FIGQPTEVVK VRLQAQSHLH GPKPRYTGTY NAYRIIATTE GLTGLWKGTT
     PNLTRNVIIN CTELVTYDLM KEALVKNKLL ADDVPCHFVS AVVAGFCTTV LSSPVDVVKT
     RFVNSSPGQY TSVPNCAMMM LTREGPSAFF KGFVPSFLRL GSWNIIMFVC FEQLKQELMK
     SRHTMDCAT
 
 
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