ID A0A0D9S102_CHLSB Unreviewed; 307 AA.
AC A0A0D9S102;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Mitochondrial brown fat uncoupling protein 1 {ECO:0000256|ARBA:ARBA00019874, ECO:0000256|RuleBase:RU367074};
DE Short=UCP 1 {ECO:0000256|RuleBase:RU367074};
GN Name=UCP1 {ECO:0000313|Ensembl:ENSCSAP00000014541.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014541.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014541.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000014541.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AQIB01017419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007998048.1; XM_007999857.1.
DR AlphaFoldDB; A0A0D9S102; -.
DR STRING; 60711.ENSCSAP00000014541; -.
DR Ensembl; ENSCSAT00000001539.1; ENSCSAP00000014541.1; ENSCSAG00000003508.1.
DR GeneID; 103236297; -.
DR KEGG; csab:103236297; -.
DR CTD; 7350; -.
DR eggNOG; KOG0753; Eukaryota.
DR GeneTree; ENSGT00940000160382; -.
DR OMA; NCAMKMF; -.
DR OrthoDB; 1832865at2759; -.
DR BioGRID-ORCS; 103236297; 1 hit in 16 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 7.
DR Bgee; ENSCSAG00000003508; Expressed in pituitary gland and 1 other cell type or tissue.
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:0015078; F:proton transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0032555; F:purine ribonucleotide binding; IEA:Ensembl.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0070417; P:cellular response to cold; IEA:Ensembl.
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:0002024; P:diet induced thermogenesis; IEA:Ensembl.
DR GO; GO:1990542; P:mitochondrial transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
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 3: Inferred from homology;
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU367074};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW 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};
KW Oxidation {ECO:0000256|ARBA:ARBA00023097, ECO:0000256|RuleBase:RU367074};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT REPEAT 11..102
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 111..201
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 210..295
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 307 AA; 33298 MW; E8C2E812BDB94A7A CRC64;
MGGLTASDVH PTLGIQLFSA GIAACLADVI TFPLDTAKVR LQIQGERPTS SAIRYKGVLG
TITTLVKTEG RMKLYSGLPA GLQRQISSTS LRIGLYDTVQ EFLSAGKETT PSLGSKILAG
LMTGGVAVFI GQPTEVVKVR LQAQSHLHGI KPRYTGTYNA YRIIATTEGL TGLWKGTTPN
LMRSVIINCT ELVTYDLMKE AFVKNNILAD EVPCHLVSAL IAGFCATAMS SPVDVVKTRF
VNSPPGQYRS VPNCAMKMFT NEGLTAFFKG LVPSFLRLGS WNIIMFVCFE QLKRELSKSR
QTMDCTT
//
