UCP1_OCHDA
ID UCP1_OCHDA Reviewed; 306 AA.
AC A0PC02;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 57.
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|Ref.1};
GN Synonyms=SLC25A7 {ECO:0000250|UniProtKB:P25874};
OS Ochotona dauurica (Daurian pika).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Ochotonidae; Ochotona.
OX NCBI_TaxID=130827;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kitao N., Yahata H., Matsumoto T., Okamastu Y.O., Omachi A., Saito M.,
RA Kimura K.;
RT "Ochotona daurica uncoupling protein 1 (UCP1) mRNA, complete CDS.";
RL Submitted (NOV-2006) 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; AB283043; BAF37006.1; -; mRNA.
DR AlphaFoldDB; A0PC02; -.
DR SMR; A0PC02; -.
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: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: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; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..306
FT /note="Mitochondrial brown fat uncoupling protein 1"
FT /id="PRO_0000281851"
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 MOD_RES 253
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250|UniProtKB:P12242"
SQ SEQUENCE 306 AA; 33105 MW; 4DB66A4DC05E617B CRC64;
MVGTTATDVA PTMGVKIFSA GVAACLADVI TFPLDTAKVR LQIQGECQTT SGIRYKGVLG
TITTLAKTEG PLKLYSGLPA GLQRQISFAS LRIGLYDTVQ EFWGGEEATP SLRSKICAGL
TTGGVAVFIG QPTEVVKVRL QAQSHLHGLK PRYTGTYNAY RIIATTESLS TLWKGTTPNL
LRNIIINCTE LVTYDLMKGA LVRNDILADD VPCHLLSALI AGFCTTLLSS PVDVVKTRFI
NSPQGQYTSV PSCAMSMLTK EGPTAFFKGF APSFLRLASW NVIMFVCFEK LKRELMKSRQ
TVDCAT
