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UCP1_DICGR
ID   UCP1_DICGR              Reviewed;         307 AA.
AC   Q8K404;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 71.
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:12075603};
GN   Synonyms=SLC25A7 {ECO:0000250|UniProtKB:P25874};
OS   Dicrostonyx groenlandicus (Northern collared lemming).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Arvicolinae; Dicrostonyx.
OX   NCBI_TaxID=85953;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12075603; DOI=10.1038/oby.2002.73;
RA   Powell C.S., Blaylock M.L., Wang R., Hunter H.L., Johanning G.L.,
RA   Nagy T.R.;
RT   "Effects of energy expenditure and Ucp1 on photoperiod-induced weight gain
RT   in collared lemmings.";
RL   Obes. Res. 10:541-550(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; AF515781; AAM49148.1; -; mRNA.
DR   AlphaFoldDB; Q8K404; -.
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..307
FT                   /note="Mitochondrial brown fat uncoupling protein 1"
FT                   /id="PRO_0000090656"
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..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"
SQ   SEQUENCE   307 AA;  33530 MW;  78D492FD26D4897A CRC64;
     MVSLTTSEVH PTMGVKTFSA GISACLADII TFPLDTAKVR LQIQGEGQTS STIRYKGVLG
     TITTLAKTEG WPKLYSGLPA GIQRQISFAS LRIGLYDTVQ EYFSSGKETP PTLGNRISAG
     LMTGGVAVFI GQPTEVVKVR LQAQSHLHGI KPRYTGTYNA YRIIATTESF STLWKGTTPN
     LMRNVIINRT ELVTYDLMKG ALVNNQILAD DVPCHLLSAL VAGFCTTFLA SPADVVKTRF
     INSLPGQYPS VPSCAMTMLT KEGPTAFFKG FVPSFLRLAS WNVIMFVCFE QLKKELMKSR
     QTMDCTT
 
 
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