ID F6W4N8_ORNAN Unreviewed; 309 AA.
AC F6W4N8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Dicarboxylate carrier SLC25A8 {ECO:0000256|ARBA:ARBA00039677};
DE AltName: Full=Mitochondrial uncoupling protein 2 {ECO:0000256|ARBA:ARBA00042647};
DE AltName: Full=Solute carrier family 25 member 8 {ECO:0000256|ARBA:ARBA00042368};
GN Name=UCP2 {ECO:0000313|Ensembl:ENSOANP00000011474.2};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000011474.2, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000011474.2, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000011474.2,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000011474.2}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000011474.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(out) + H(+)(in) + phosphate(in) = (S)-malate(in) +
CC H(+)(out) + phosphate(out); Xref=Rhea:RHEA:73299, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15589, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000256|ARBA:ARBA00036339};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(out) = (S)-malate(in); Xref=Rhea:RHEA:74555,
CC ChEBI:CHEBI:15589; Evidence={ECO:0000256|ARBA:ARBA00036759};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-aspartate(out) + phosphate(in) = H(+)(out) + L-
CC aspartate(in) + phosphate(out); Xref=Rhea:RHEA:73307,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000256|ARBA:ARBA00036689};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + malonate(out) + phosphate(in) = H(+)(out) +
CC malonate(in) + phosphate(out); Xref=Rhea:RHEA:73387,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15792, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000256|ARBA:ARBA00036922};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + oxaloacetate(out) + phosphate(in) = H(+)(out) +
CC oxaloacetate(in) + phosphate(out); Xref=Rhea:RHEA:73303,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000256|ARBA:ARBA00035983};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + phosphate(in) + sulfate(out) = H(+)(out) +
CC phosphate(out) + sulfate(in); Xref=Rhea:RHEA:73391,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000256|ARBA:ARBA00036897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000256|ARBA:ARBA00024169};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate(out) = L-aspartate(in); Xref=Rhea:RHEA:66332,
CC ChEBI:CHEBI:29991; Evidence={ECO:0000256|ARBA:ARBA00035830};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000256|ARBA:ARBA00024167};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000256|ARBA:ARBA00036616};
CC -!- SUBUNIT: Homotetramer. Adopts an asymmetrical dimer of dimers
CC functional form. {ECO:0000256|ARBA:ARBA00038614}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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 AlphaFoldDB; F6W4N8; -.
DR STRING; 9258.ENSOANP00000011474; -.
DR Ensembl; ENSOANT00000011476.3; ENSOANP00000011474.2; ENSOANG00000007210.3.
DR eggNOG; KOG0753; Eukaryota.
DR GeneTree; ENSGT00940000159524; -.
DR HOGENOM; CLU_015166_14_2_1; -.
DR OMA; CSTIDAY; -.
DR OrthoDB; 1832865at2759; -.
DR TreeFam; TF323211; -.
DR Proteomes; UP000002279; Chromosome 20.
DR Bgee; ENSOANG00000007210; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
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; MITOCHONDRIAL DICARBOXYLATE CARRIER-RELATED; 1.
DR PANTHER; PTHR45618:SF1; MITOCHONDRIAL UNCOUPLING PROTEIN 2; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000002279};
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..106
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 114..203
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 212..297
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 309 AA; 32767 MW; 2B5708697007DA9C CRC64;
MVGFKPTDVP PTATVKFLSA GTAACIADLI TFPLDTAKVR LQVQGESRGP SRVPAGPQYR
GVLGTILTVA RTEGPGSLYS GLVAGLQRQM SFASVRIGLY DSVKQFYTKG SEHAGVGSRL
LAGCTTGALA VGLAQPTDVV KVRFQAQARA AGSRRYQGTV DAYKTIAREE GLRGLWKGTS
PNVARNAIVN CAELVTYDLI KDALLRGGLM ADDLPCHLTS AFGAGFCTTV IASPVDVVKT
RYMNSASGQY GGAVHCALTM LRKEGPRAFY KGFMPSFLRL GSWNVVMFVT YEQLKRAITA
ARAASVAPC
//
