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Mitochondrial brown fat uncoupling protein 1 (UCP 1) (Solute carrier family 25 member 7) (Thermogenin)

 UCP1_CANLF              Reviewed;         309 AA.
Q9GMZ1;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-APR-2018, entry version 87.
RecName: Full=Mitochondrial brown fat uncoupling protein 1 {ECO:0000305};
Short=UCP 1 {ECO:0000305};
AltName: Full=Solute carrier family 25 member 7 {ECO:0000250|UniProtKB:P25874};
AltName: Full=Thermogenin {ECO:0000250|UniProtKB:P04575};
Name=UCP1 {ECO:0000303|PubMed:11959030};
Synonyms=SLC25A7 {ECO:0000250|UniProtKB:P25874};
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Beagle;
PubMed=11959030; DOI=10.1016/S1096-4959(02)00004-0;
Ishioka K., Kanehira K., Sasaki N., Kitamura H., Kimura K., Saito M.;
"Canine mitochondrial uncoupling proteins: structure and mRNA
expression of three isoforms in adult beagles.";
Comp. Biochem. Physiol. 131B:483-489(2002).
-!- FUNCTION: Mitochondrial protein responsible for thermogenic
respiration, a specialized capacity of brown adipose tissue and
beige fat that participates to non-shivering adaptive
thermogenesis to temperature and diet variations and more
generally to the regulation of energy balance. Functions as a
long-chain fatty acid/LCFA and proton symporter, simultaneously
transporting one LCFA and one proton through the inner
mitochondrial membrane. However, LCFAs remaining associated with
the transporter via their hydrophobic tails, it results in an
apparent transport of protons activated by LCFAs. Thereby,
dissipates the mitochondrial proton gradient and converts the
energy of substrate oxydation into heat instead of ATP. Regulates
the production of reactive oxygen species/ROS by mitochondria.
{ECO:0000250|UniProtKB:P12242}.
-!- ENZYME REGULATION: Has no constitutive proton transporter activity
and has to be activated by long-chain fatty acids/LCFAs. Inhibited
by purine nucleotides. Both purine nucleotides and LCFAs bind the
cytosolic side of the transporter and directly compete to activate
or inhibit it. Activated by noradrenaline and reactive oxygen
species. {ECO:0000250|UniProtKB:P12242}.
-!- SUBUNIT: Most probably functions as a monomer. Binds one purine
nucleotide per monomer. However, has also been suggested to
function as a homodimer or a homotetramer. Tightly associates with
cardiolipin in the mitochondrion inner membrane; may stabilize and
regulate its activity. {ECO:0000250|UniProtKB:P25874,
ECO:0000250|UniProtKB:W5PSH7}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000250|UniProtKB:P12242}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P04633}.
-!- PTM: May undergo sulfenylation upon cold exposure. May increase
the sensitivity of UCP1 thermogenic function to the activation by
noradrenaline probably through structural effects.
{ECO:0000250|UniProtKB:P12242}.
-!- PTM: May undergo ubiquitin-mediated proteasomal degradation.
{ECO:0000250|UniProtKB:P04633}.
-!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29)
family. {ECO:0000305}.
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EMBL; AB046106; BAB11684.1; -; mRNA.
RefSeq; NP_001003046.1; NM_001003046.1.
UniGene; Cfa.91; -.
ProteinModelPortal; Q9GMZ1; -.
STRING; 9615.ENSCAFP00000005489; -.
PaxDb; Q9GMZ1; -.
GeneID; 403574; -.
KEGG; cfa:403574; -.
CTD; 7350; -.
eggNOG; KOG0753; Eukaryota.
eggNOG; ENOG410XRV1; LUCA.
HOGENOM; HOG000165140; -.
HOVERGEN; HBG009528; -.
InParanoid; Q9GMZ1; -.
KO; K08769; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:1901612; F:cardiolipin binding; ISS:UniProtKB.
GO; GO:0036041; F:long-chain fatty acid binding; ISS:UniProtKB.
GO; GO:0017077; F:oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
GO; GO:0032555; F:purine ribonucleotide binding; ISS:UniProtKB.
GO; GO:1990845; P:adaptive thermogenesis; ISS:UniProtKB.
GO; GO:0071398; P:cellular response to fatty acid; ISS:UniProtKB.
GO; GO:0032870; P:cellular response to hormone stimulus; ISS:UniProtKB.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISS:UniProtKB.
GO; GO:1990542; P:mitochondrial transmembrane transport; ISS:UniProtKB.
GO; GO:0006839; P:mitochondrial transport; IBA:GO_Central.
GO; GO:1902600; P:proton transmembrane transport; ISS:UniProtKB.
GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
GO; GO:0009409; P:response to cold; IBA:GO_Central.
GO; GO:0031667; P:response to nutrient levels; ISS:UniProtKB.
GO; GO:0009266; P:response to temperature stimulus; ISS:UniProtKB.
Gene3D; 1.50.40.10; -; 1.
InterPro; IPR002030; Mit_uncoupling_UCP-like.
InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
InterPro; IPR023395; Mt_carrier_dom_sf.
Pfam; PF00153; Mito_carr; 3.
PRINTS; PR00784; MTUNCOUPLING.
SUPFAM; SSF103506; SSF103506; 1.
PROSITE; PS50920; SOLCAR; 3.
2: Evidence at transcript level;
Complete proteome; Ion channel; Ion transport; Membrane;
Mitochondrion; Mitochondrion inner membrane; Oxidation;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 309 Mitochondrial brown fat uncoupling
protein 1.
/FTId=PRO_0000090655.
TOPO_DOM 1 10 Mitochondrial intermembrane.
{ECO:0000250|UniProtKB:P04633}.
TRANSMEM 11 32 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 33 75 Mitochondrial matrix.
{ECO:0000250|UniProtKB:P04633}.
TRANSMEM 76 98 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 99 118 Mitochondrial intermembrane.
{ECO:0000250|UniProtKB:P04633}.
TRANSMEM 119 135 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 136 180 Mitochondrial matrix.
{ECO:0000250|UniProtKB:P04633}.
TRANSMEM 181 197 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 198 214 Mitochondrial intermembrane.
{ECO:0000250|UniProtKB:P04633}.
TRANSMEM 215 234 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 235 268 Mitochondrial matrix.
{ECO:0000250|UniProtKB:P04633}.
TRANSMEM 269 291 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 292 309 Mitochondrial intermembrane.
{ECO:0000250|UniProtKB:P04633}.
REPEAT 11 104 Solcar 1.
REPEAT 113 203 Solcar 2.
REPEAT 212 297 Solcar 3.
MOD_RES 256 256 Cysteine sulfenic acid (-SOH).
{ECO:0000250|UniProtKB:P12242}.
SEQUENCE 309 AA; 33280 MW; C4D33E2A3B08F16E CRC64;
MLRAPGSDAP PTLSVRIAAA AGAACLADMI TFPLDTAKVR LQIQGEGQGQ PPRAPRYRGV
LGTVATLART EGLQKLYSGL PAGLQRQVGF ASLRIGLYDS VREWLSPGQG AAASLGSRIS
AGVMTGGAAV FIGQPTEVVK VRLQAQSHLH GRKPRYTGTY NAYRIIATTE GLTGLWKGTT
PNLMRNVIIN CTELVTYDLM KEALVKNHLL ADDLPCHFLS ALVAGFCTTV LSSPVDVVKT
RFVNSVPEQY TSVPNCAMTM LTKEGPLAFF KGFVPSFLRL GSWNVIMFVC FEQLKRELMK
SGRTVDCAT


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