ID UCP5_MOUSE Reviewed; 325 AA. AC Q9Z2B2; Q9ESI8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 19-DEC-2001, sequence version 2. DT 27-MAR-2024, entry version 168. DE RecName: Full=Brain mitochondrial carrier protein 1 {ECO:0000303|PubMed:9852133}; DE Short=BMCP-1; DE AltName: Full=Mitochondrial uncoupling protein 5 {ECO:0000303|PubMed:10928996}; DE Short=UCP 5; DE AltName: Full=Solute carrier family 25 member 14; GN Name=Slc25a14 {ECO:0000312|MGI:MGI:1330823}; GN Synonyms=Bmcp1 {ECO:0000303|PubMed:9852133}, Ucp5 GN {ECO:0000303|PubMed:10928996}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=9852133; DOI=10.1074/jbc.273.51.34611; RA Sanchis D., Fleury C., Chomiki N., Goubern M., Huang Q., Neverova M., RA Gregoire F., Easlick J., Raimbault S., Levi-Meyrueis C., Miroux B., RA Collins S., Seldin M., Richard D., Warden C., Bouillaud F., Ricquier D.; RT "BMCP1, a novel mitochondrial carrier with high expression in the central RT nervous system of humans and rodents, and respiration uncoupling activity RT in recombinant yeast."; RL J. Biol. Chem. 273:34611-34615(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX PubMed=10928996; DOI=10.1096/fj.14.11.1611; RA Yu X.X., Mao W., Zhong A., Schow P., Brush J., Sherwood S.W., Adams S.H., RA Pan G.; RT "Characterization of novel UCP5/BMCP1 isoforms and differential regulation RT of UCP4 and UCP5 expression through dietary or temperature manipulation."; RL FASEB J. 14:1611-1618(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryo; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=11701769; DOI=10.1046/j.1471-4159.2001.00604.x; RA Kim-Han J.S., Reichert S.A., Quick K.L., Dugan L.L.; RT "BMCP1: a mitochondrial uncoupling protein in neurons which regulates RT mitochondrial function and oxidant production."; RL J. Neurochem. 79:658-668(2001). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Transports inorganic anions (sulfate, sulfite, thiosulfate CC and phosphate) and, to a lesser extent, a variety of dicarboxylates CC (e.g. malonate, malate and citramalate) and, even more so, aspartate CC and glutamate and tricarboxylates. May catalyze the export of sulfite CC and thiosulfate (the hydrogen sulfide degradation products) from the CC mitochondria, thereby modulating the level of the hydrogen sulfide. CC Also can mediate a very low unidirectional transport of anions CC including sulfate, phosphate, (S)-malate, citrate, L-aspartate and L- CC glutamate. Maintains oxidative balance (through uncoupling activities) CC and ATP production (by modifying mitochondrial membrane potential). Is CC able to transport protons across lipid membranes. Also exhibits CC transmembrane chloride transport activity to a lesser extent (By CC similarity). May modify mitochondrial respiratory efficiency and CC mitochondrial oxidant production (PubMed:11701769). CC {ECO:0000250|UniProtKB:O95258, ECO:0000269|PubMed:11701769}. CC -!- CATALYTIC ACTIVITY: CC Reaction=sulfate(out) + sulfite(in) = sulfate(in) + sulfite(out); CC Xref=Rhea:RHEA:73207, ChEBI:CHEBI:16189, ChEBI:CHEBI:17359; CC Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=sulfate(out) + thiosulfate(in) = sulfate(in) + CC thiosulfate(out); Xref=Rhea:RHEA:73215, ChEBI:CHEBI:16189, CC ChEBI:CHEBI:33542; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate(in) + sulfate(out) = phosphate(out) + sulfate(in); CC Xref=Rhea:RHEA:71631, ChEBI:CHEBI:16189, ChEBI:CHEBI:43474; CC Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=oxalate(in) + sulfate(out) = oxalate(out) + sulfate(in); CC Xref=Rhea:RHEA:72275, ChEBI:CHEBI:16189, ChEBI:CHEBI:30623; CC Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=malonate(in) + sulfate(out) = malonate(out) + sulfate(in); CC Xref=Rhea:RHEA:73195, ChEBI:CHEBI:15792, ChEBI:CHEBI:16189; CC Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=maleate(in) + sulfate(out) = maleate(out) + sulfate(in); CC Xref=Rhea:RHEA:73199, ChEBI:CHEBI:16189, ChEBI:CHEBI:30780; CC Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate(in) + sulfate(out) = (S)-malate(out) + sulfate(in); CC Xref=Rhea:RHEA:71615, ChEBI:CHEBI:15589, ChEBI:CHEBI:16189; CC Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3S)-citramalate(in) + sulfate(out) = (3S)-citramalate(out) + CC sulfate(in); Xref=Rhea:RHEA:73223, ChEBI:CHEBI:16189, CC ChEBI:CHEBI:30936; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3R)-citramalate(in) + sulfate(out) = (3R)-citramalate(out) + CC sulfate(in); Xref=Rhea:RHEA:73227, ChEBI:CHEBI:16189, CC ChEBI:CHEBI:30934; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=succinate(in) + sulfate(out) = succinate(out) + sulfate(in); CC Xref=Rhea:RHEA:73411, ChEBI:CHEBI:16189, ChEBI:CHEBI:30031; CC Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(S,S)-tartrate(in) + sulfate(out) = (S,S)-tartrate(out) + CC sulfate(in); Xref=Rhea:RHEA:73407, ChEBI:CHEBI:16189, CC ChEBI:CHEBI:30927; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R,3R)-tartrate(in) + sulfate(out) = (2R,3R)-tartrate(out) + CC sulfate(in); Xref=Rhea:RHEA:73403, ChEBI:CHEBI:16189, CC ChEBI:CHEBI:30924; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-aspartate(in) + sulfate(out) = D-aspartate(out) + CC sulfate(in); Xref=Rhea:RHEA:73399, ChEBI:CHEBI:16189, CC ChEBI:CHEBI:29990; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate(in) + sulfate(out) = L-aspartate(out) + CC sulfate(in); Xref=Rhea:RHEA:73395, ChEBI:CHEBI:16189, CC ChEBI:CHEBI:29991; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=sulfate(in) = sulfate(out); Xref=Rhea:RHEA:34983, CC ChEBI:CHEBI:16189; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823, CC ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate(out) = (S)-malate(in); Xref=Rhea:RHEA:74555, CC ChEBI:CHEBI:15589; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=citrate(in) = citrate(out); Xref=Rhea:RHEA:33183, CC ChEBI:CHEBI:16947; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate(out) = L-aspartate(in); Xref=Rhea:RHEA:66332, CC ChEBI:CHEBI:29991; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336, CC ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; CC Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, CC ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:O95258}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O95258}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000305|PubMed:11701769}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=UCP5L; CC IsoId=Q9Z2B2-1; Sequence=Displayed; CC Name=2; Synonyms=UCP5S; CC IsoId=Q9Z2B2-2; Sequence=VSP_003274; CC -!- TISSUE SPECIFICITY: Mainly expressed in brain, particularly abundant in CC cortex, hippocampus thalamus, amygdala and hypothalamus CC (PubMed:10928996). Highly expressed in heart and kidney, but not liver CC or lung (at protein level) (PubMed:11701769). In the nervous system, CC expressed in cortex, basal ganglia, substantia nigra, cerebellum, and CC spinal cord (at protein level) (PubMed:11701769). CC {ECO:0000269|PubMed:10928996, ECO:0000269|PubMed:11701769}. CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF076981; AAD03674.1; -; mRNA. DR EMBL; AF155812; AAG29585.1; -; mRNA. DR EMBL; AF155813; AAG29586.1; -; mRNA. DR EMBL; AL669901; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL672042; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC048692; AAH48692.1; -; mRNA. DR CCDS; CCDS30112.1; -. [Q9Z2B2-2] DR CCDS; CCDS53066.1; -. [Q9Z2B2-1] DR RefSeq; NP_001159922.1; NM_001166450.2. [Q9Z2B2-1] DR RefSeq; NP_001277634.1; NM_001290705.1. DR RefSeq; NP_035528.1; NM_011398.3. [Q9Z2B2-2] DR RefSeq; XP_017173930.1; XM_017318441.1. DR AlphaFoldDB; Q9Z2B2; -. DR SMR; Q9Z2B2; -. DR STRING; 10090.ENSMUSP00000110586; -. DR PhosphoSitePlus; Q9Z2B2; -. DR MaxQB; Q9Z2B2; -. DR PaxDb; 10090-ENSMUSP00000033431; -. DR ProteomicsDB; 297864; -. [Q9Z2B2-1] DR ProteomicsDB; 297865; -. [Q9Z2B2-2] DR Pumba; Q9Z2B2; -. DR Antibodypedia; 16263; 104 antibodies from 26 providers. DR DNASU; 20523; -. DR Ensembl; ENSMUST00000033431.14; ENSMUSP00000033431.8; ENSMUSG00000031105.17. [Q9Z2B2-2] DR Ensembl; ENSMUST00000114936.8; ENSMUSP00000110586.2; ENSMUSG00000031105.17. [Q9Z2B2-1] DR Ensembl; ENSMUST00000177710.2; ENSMUSP00000136140.2; ENSMUSG00000031105.17. [Q9Z2B2-1] DR GeneID; 20523; -. DR KEGG; mmu:20523; -. DR UCSC; uc009tco.3; mouse. [Q9Z2B2-2] DR UCSC; uc009tcp.3; mouse. [Q9Z2B2-1] DR AGR; MGI:1330823; -. DR CTD; 9016; -. DR MGI; MGI:1330823; Slc25a14. DR VEuPathDB; HostDB:ENSMUSG00000031105; -. DR eggNOG; KOG0753; Eukaryota. DR GeneTree; ENSGT00940000159471; -. DR InParanoid; Q9Z2B2; -. DR OrthoDB; 1832865at2759; -. DR PhylomeDB; Q9Z2B2; -. DR TreeFam; TF323211; -. DR Reactome; R-MMU-167826; The fatty acid cycling model. DR Reactome; R-MMU-167827; The proton buffering model. DR BioGRID-ORCS; 20523; 1 hit in 76 CRISPR screens. DR PRO; PR:Q9Z2B2; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; Q9Z2B2; Protein. DR Bgee; ENSMUSG00000031105; Expressed in substantia nigra and 221 other cell types or tissues. DR ExpressionAtlas; Q9Z2B2; baseline and differential. DR GO; GO:0005740; C:mitochondrial envelope; IDA:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0015078; F:proton transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; ISS:UniProtKB. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015698; P:inorganic anion transport; ISS:UniProtKB. DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; IDA:UniProtKB. 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:SF20; BRAIN MITOCHONDRIAL CARRIER 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. DR Genevisible; Q9Z2B2; MM. PE 1: Evidence at protein level; KW Alternative splicing; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..325 FT /note="Brain mitochondrial carrier protein 1" FT /id="PRO_0000090678" FT TRANSMEM 38..54 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TRANSMEM 112..128 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TRANSMEM 145..165 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TRANSMEM 199..215 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TRANSMEM 240..256 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TRANSMEM 298..315 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT REPEAT 42..131 FT /note="Solcar 1" FT REPEAT 139..224 FT /note="Solcar 2" FT REPEAT 233..323 FT /note="Solcar 3" FT VAR_SEQ 23..25 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9852133" FT /id="VSP_003274" SQ SEQUENCE 325 AA; 36286 MW; 19BF01EF12809D83 CRC64; MGIFPGIILI FLRVKFATAA VIVSGHQKSS TLSHEMSGLN WKPFVYGGLA SIVAEFGTFP VDLTKTRLQV QGQSIDVRFK EIKYRGMFHA LFRIYKEEGI LALYSGIAPA LLRQASYGTI KIGIYQSLKR LFVERLEDET LLINMICGVV SGVISSTIAN PTDVLKIRMQ AQGSLFQGSM IGSFIDIYQQ EGTRGLWRGV VPTAQRAAIV VGVELPVYDI TKKHLIVSGM LGDTILTHFV SSFTCGLAGA LASNPVDVVR TRMMNQRAIV GHVDLYKGTL DGILKMWKHE GFFALYKGFW PNWLRLGPWN IIFFITYEQL KRLQI //