UCP1_MESAU
ID UCP1_MESAU Reviewed; 307 AA.
AC P04575;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 110.
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:0000303|PubMed:6819159};
GN Name=UCP1 {ECO:0000250|UniProtKB:P25874};
GN Synonyms=SLC25A7 {ECO:0000250|UniProtKB:P25874},
GN UCP {ECO:0000303|PubMed:3000775};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brown adipose tissue;
RA Raimbault S., Prieto S., Rial E., Bouillaud F.;
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-307.
RX PubMed=3000775; DOI=10.1002/j.1460-2075.1985.tb03941.x;
RA Aquila H., Link T.A., Klingenberg M.;
RT "The uncoupling protein from brown fat mitochondria is related to the
RT mitochondrial ADP/ATP carrier. Analysis of sequence homologies and of
RT folding of the protein in the membrane.";
RL EMBO J. 4:2369-2376(1985).
RN [3]
RP PROTEIN SEQUENCE OF 257-307, AND SUBUNIT.
RX PubMed=1730236; DOI=10.1111/j.1432-1033.1992.tb19859.x;
RA Winkler E., Klingenberg M.;
RT "Photoaffinity labeling of the nucleotide-binding site of the uncoupling
RT protein from hamster brown adipose tissue.";
RL Eur. J. Biochem. 203:295-304(1992).
RN [4]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=6819159; DOI=10.1016/0014-5793(82)81319-7;
RA Cannon B., Hedin A., Nedergaard J.;
RT "Exclusive occurrence of thermogenin antigen in brown adipose tissue.";
RL FEBS Lett. 150:129-132(1982).
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 (By similarity). However, has also been
CC suggested to function as a homodimer or a homotetramer
CC (PubMed:1730236). Tightly associates with cardiolipin in the
CC mitochondrion inner membrane; may stabilize and regulate its activity
CC (By similarity). {ECO:0000250|UniProtKB:W5PSH7,
CC ECO:0000269|PubMed:1730236}.
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:6819159}.
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; X73138; CAA51653.1; -; mRNA.
DR PIR; S34268; S34268.
DR RefSeq; NP_001268261.1; NM_001281332.1.
DR AlphaFoldDB; P04575; -.
DR SMR; P04575; -.
DR GeneID; 101835783; -.
DR CTD; 7350; -.
DR OrthoDB; 984118at2759; -.
DR Proteomes; UP000189706; 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: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 1: Evidence at protein level;
KW Direct protein sequencing; Ion channel; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Oxidation; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3000775"
FT CHAIN 2..307
FT /note="Mitochondrial brown fat uncoupling protein 1"
FT /id="PRO_0000090658"
FT TOPO_DOM 2..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..116
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT TRANSMEM 117..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..178
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT TRANSMEM 179..195
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..212
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT TRANSMEM 213..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..266
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT TRANSMEM 267..289
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..307
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P04633"
FT REPEAT 11..102
FT /note="Solcar 1"
FT REPEAT 111..201
FT /note="Solcar 2"
FT REPEAT 210..295
FT /note="Solcar 3"
FT MOD_RES 254
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250|UniProtKB:P12242"
FT CONFLICT 129
FT /note="F -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 33347 MW; FD42E002B82CAE53 CRC64;
MVNPTTSEVH PTMGVKIFSA GVAACLADII TFPLDTAKVR LQIQGEGQIS STIRYKGVLG
TITTLAKTEG LPKLYSGLPA GIQRQISFAS LRIGLYDTVQ EYFSSGKETP PTLGNRISAG
LMTGGVAVFI GQPTEVVKVR LQAQSHLHGI KPRYTGTYNA YRIIATTESF STLWKGTTPN
LLRNVIINCV ELVTYDLMKG ALVNNQILAD DVPCHLLSAF VAGFCTTFLA SPADVVKTRF
INSLPGQYPS VPSCAMTMLT KEGPTAFFKG FVPSFLRLAS WNVIMFVCFE QLKKELSKSR
QTVDCTT
