UCP1_CANLF
ID UCP1_CANLF Reviewed; 309 AA.
AC Q9GMZ1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
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:0000303|PubMed:11959030};
GN Synonyms=SLC25A7 {ECO:0000250|UniProtKB:P25874};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle;
RX PubMed=11959030; DOI=10.1016/s1096-4959(02)00004-0;
RA Ishioka K., Kanehira K., Sasaki N., Kitamura H., Kimura K., Saito M.;
RT "Canine mitochondrial uncoupling proteins: structure and mRNA expression of
RT three isoforms in adult beagles.";
RL Comp. Biochem. Physiol. 131B:483-489(2002).
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; AB046106; BAB11684.1; -; mRNA.
DR RefSeq; NP_001003046.1; NM_001003046.1.
DR AlphaFoldDB; Q9GMZ1; -.
DR SMR; Q9GMZ1; -.
DR STRING; 9612.ENSCAFP00000005489; -.
DR PaxDb; Q9GMZ1; -.
DR GeneID; 403574; -.
DR KEGG; cfa:403574; -.
DR CTD; 7350; -.
DR eggNOG; KOG0753; Eukaryota.
DR InParanoid; Q9GMZ1; -.
DR OrthoDB; 984118at2759; -.
DR Proteomes; UP000002254; Unplaced.
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: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:1990542; P:mitochondrial transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006839; P:mitochondrial transport; IEA:InterPro.
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: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_0000090655"
FT TOPO_DOM 1..10
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT TRANSMEM 11..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..75
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT TRANSMEM 76..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..118
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P04633"
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:0000250|UniProtKB:P04633"
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:0000250|UniProtKB:P04633"
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:0000250|UniProtKB:P04633"
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:0000250|UniProtKB:P04633"
FT REPEAT 11..104
FT /note="Solcar 1"
FT REPEAT 113..203
FT /note="Solcar 2"
FT REPEAT 212..297
FT /note="Solcar 3"
FT MOD_RES 256
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250|UniProtKB:P12242"
SQ 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
