ID UCP1_RABIT Reviewed; 306 AA.
AC P14271;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 27-MAR-2024, entry version 126.
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:2730654};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=2730654; DOI=10.1016/0006-291x(89)91574-x;
RA Balogh A.G., Ridley R.G., Patel H.V., Freeman K.B.;
RT "Rabbit brown adipose tissue uncoupling protein mRNA: use of only one of
RT two polyadenylation signals in its processing.";
RL Biochem. Biophys. Res. Commun. 161:156-161(1989).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000250|UniProtKB:P25874};
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 Despite lacking canonical translational encoding for selenocysteine, a
CC small pool of the protein has been observed to selectively incorporate
CC selenocysteine at 'Cys-253'. Selenocysteine-modified protein is highly
CC sensitive to redox modification and may constitute a pool of protein
CC highly sensitive to activation by elevated levels of reactive oxygen
CC species (ROS). {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 -!- TISSUE SPECIFICITY: Brown adipose tissue. {ECO:0000269|PubMed:2730654}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X14696; CAA32826.1; -; mRNA.
DR PIR; A32446; A32446.
DR RefSeq; NP_001164548.1; NM_001171077.1.
DR AlphaFoldDB; P14271; -.
DR SMR; P14271; -.
DR STRING; 9986.ENSOCUP00000001977; -.
DR PaxDb; 9986-ENSOCUP00000001977; -.
DR GeneID; 100328618; -.
DR KEGG; ocu:100328618; -.
DR CTD; 7350; -.
DR eggNOG; KOG0753; Eukaryota.
DR InParanoid; P14271; -.
DR OrthoDB; 1832865at2759; -.
DR Proteomes; UP000001811; Unplaced.
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: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:1902600; P:proton transmembrane transport; ISS:UniProtKB.
DR GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
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; Mitochondrial carrier domain; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45618:SF19; MITOCHONDRIAL BROWN FAT UNCOUPLING PROTEIN 1; 1.
DR PANTHER; PTHR45618; MITOCHONDRIAL DICARBOXYLATE CARRIER-RELATED; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00784; MTUNCOUPLING.
DR SUPFAM; SSF103506; Mitochondrial carrier; 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..306
FT /note="Mitochondrial brown fat uncoupling protein 1"
FT /id="PRO_0000090661"
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..73
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT TRANSMEM 74..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..115
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT TRANSMEM 116..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..177
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT TRANSMEM 178..194
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..211
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT TRANSMEM 212..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..265
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT TRANSMEM 266..288
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..306
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT REPEAT 11..102
FT /note="Solcar 1"
FT REPEAT 110..200
FT /note="Solcar 2"
FT REPEAT 209..294
FT /note="Solcar 3"
FT BINDING 56
FT /ligand="fatty acid 16:0"
FT /ligand_id="ChEBI:CHEBI:78123"
FT /evidence="ECO:0000250|UniProtKB:P25874"
FT BINDING 268
FT /ligand="fatty acid 16:0"
FT /ligand_id="ChEBI:CHEBI:78123"
FT /evidence="ECO:0000250|UniProtKB:P25874"
FT MOD_RES 253
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250|UniProtKB:P12242"
SQ SEQUENCE 306 AA; 33083 MW; 58343CAD94C910F1 CRC64;
MVGTTTTDVP PTMGVKIFSA GVAACLADVI TFPLDTAKVR QQIQGEFPIT SGIRYKGVLG
TITTLAKTEG PLKLYSGLPA GLQRQISFAS LRIGLYDTVQ EFFTSGEETP SLGSKISAGL
TTGGVAVFIG QPTEVVKVRL QAQSHLHGLK PRYTGTYNAY RIIATTESLT SLWKGTTPNL
LRNVIINCTE LVTYDLMKGA LVRNEILADD VPCHFVSALI AGFCTTLLSS PVDVVKTRFI
NSPPGQYASV PNCAMTMFTK EGPTAFFKGF VPSFLRLGSW NVIMFVCFEK LKGELMRSRQ
TVDCAT
//
