ID Q2LDH5_UROPR Unreviewed; 119 AA.
AC Q2LDH5;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Mitochondrial brown fat uncoupling protein 1 {ECO:0000256|RuleBase:RU367074};
DE Short=UCP 1 {ECO:0000256|RuleBase:RU367074};
DE Flags: Fragment;
OS Urocitellus parryii (Arctic ground squirrel) (Spermophilus parryii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Urocitellus.
OX NCBI_TaxID=9999 {ECO:0000313|EMBL:ABC59800.1};
RN [1] {ECO:0000313|EMBL:ABC59800.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16464973; DOI=10.1152/physiolgenomics.00260.2005;
RA Yan J., Burman A., Nichols C., Alila L., Showe L.C., Showe M.K.,
RA Boyer B.B., Barnes B.M., Marr T.G.;
RT "Detection of differential gene expression in brown adipose tissue of
RT hibernating arctic ground squirrels with mouse microarrays.";
RL Physiol. Genomics 25:346-353(2006).
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:0000256|RuleBase:RU367074}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|RuleBase:RU367074}; Multi-pass membrane
CC protein {ECO:0000256|RuleBase:RU367074}.
CC -!- PTM: May undergo ubiquitin-mediated proteasomal degradation.
CC {ECO:0000256|RuleBase:RU367074}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375, ECO:0000256|RuleBase:RU000488}.
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DR EMBL; DQ334042; ABC59800.1; -; mRNA.
DR AlphaFoldDB; Q2LDH5; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1901612; F:cardiolipin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036041; F:long-chain fatty acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017077; F:oxidative phosphorylation uncoupler activity; IEA:UniProtKB-UniRule.
DR GO; GO:1990845; P:adaptive thermogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0071398; P:cellular response to fatty acid; IEA:UniProtKB-UniRule.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEA:UniProtKB-UniRule.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:UniProtKB-UniRule.
DR GO; GO:1990542; P:mitochondrial transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0031667; P:response to nutrient levels; IEA:UniProtKB-UniRule.
DR GO; GO:0009266; P:response to temperature stimulus; IEA:UniProtKB-UniRule.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
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; 2.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS50920; SOLCAR; 2.
PE 2: Evidence at transcript level;
KW Ion channel {ECO:0000256|RuleBase:RU367074};
KW Ion transport {ECO:0000256|RuleBase:RU367074};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU367074};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|RuleBase:RU367074}; Oxidation {ECO:0000256|RuleBase:RU367074};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transport {ECO:0000256|RuleBase:RU000488}.
FT REPEAT 1..59
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 67..119
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABC59800.1"
FT NON_TER 119
FT /evidence="ECO:0000313|EMBL:ABC59800.1"
SQ SEQUENCE 119 AA; 12697 MW; 0BB67C10E65D0ABE CRC64;
QGEFPVSSGI TYKGVLGTIT TLAKTEGPMK LYSGLPAGLQ RQISFASLRI GLYDSVQEYF
TSGNETPSLG SKISAGLTTG GVAVFIGQPT EVVKVRLQAQ SHLHGLKPRY TGTYNAYRI
//
