PUMP4_ARATH
ID PUMP4_ARATH Reviewed; 313 AA.
AC Q9SB52;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Mitochondrial uncoupling protein 4;
DE Short=AtPUMP4;
DE AltName: Full=Mitochondrial dicarboxylate carrier 2;
GN Name=PUMP4; Synonyms=DIC2, UCP4; OrderedLocusNames=At4g24570;
GN ORFNames=F22K18.230;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=18039180; DOI=10.1042/bj20070867;
RA Palmieri L., Picault N., Arrigoni R., Besin E., Palmieri F., Hodges M.;
RT "Molecular identification of three Arabidopsis thaliana mitochondrial
RT dicarboxylate carrier isoforms: organ distribution, bacterial expression,
RT reconstitution into liposomes and functional characterization.";
RL Biochem. J. 410:621-629(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, INDUCTION BY COLD, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16473895; DOI=10.1093/jxb/erj070;
RA Borecky J., Nogueira F.T., de Oliveira K.A., Maia I.G., Vercesi A.E.,
RA Arruda P.;
RT "The plant energy-dissipating mitochondrial systems: depicting the genomic
RT structure and the expression profiles of the gene families of uncoupling
RT protein and alternative oxidase in monocots and dicots.";
RL J. Exp. Bot. 57:849-864(2006).
CC -!- FUNCTION: PUMPS are mitochondrial transporter proteins that create
CC proton leaks across the inner mitochondrial membrane, thus uncoupling
CC oxidative phosphorylation. This leads to a decrease in the efficiency
CC of oxidative phosphorylation and an increase in heat production. May be
CC involved in protecting plant cells against oxidative stress damage (By
CC similarity). Recombinant PUMP4, reconstituted into liposomes,
CC transports a wide range of dicarboxylic acids including malate,
CC oxaloacetate and succinate as well as phosphate, sulfate and
CC thiosulfate. However, it is unknown if these transports are of any
CC biological significance in vivo. {ECO:0000250,
CC ECO:0000269|PubMed:18039180}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:16473895, ECO:0000269|PubMed:18039180}.
CC -!- INDUCTION: By cold stress. {ECO:0000269|PubMed:16473895}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AM236863; CAJ86455.1; -; mRNA.
DR EMBL; AL035356; CAA23006.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79367.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84927.1; -; Genomic_DNA.
DR EMBL; AY042859; AAK68799.1; -; mRNA.
DR EMBL; BT008712; AAP42725.1; -; mRNA.
DR EMBL; AY084853; AAM61418.1; -; mRNA.
DR PIR; T05577; T05577.
DR RefSeq; NP_194188.1; NM_118590.2.
DR AlphaFoldDB; Q9SB52; -.
DR SMR; Q9SB52; -.
DR BioGRID; 13848; 1.
DR STRING; 3702.AT4G24570.1; -.
DR iPTMnet; Q9SB52; -.
DR PaxDb; Q9SB52; -.
DR PRIDE; Q9SB52; -.
DR ProteomicsDB; 226125; -.
DR EnsemblPlants; AT4G24570.1; AT4G24570.1; AT4G24570.
DR GeneID; 828559; -.
DR Gramene; AT4G24570.1; AT4G24570.1; AT4G24570.
DR KEGG; ath:AT4G24570; -.
DR Araport; AT4G24570; -.
DR TAIR; locus:2121974; AT4G24570.
DR eggNOG; KOG0759; Eukaryota.
DR HOGENOM; CLU_015166_14_1_1; -.
DR InParanoid; Q9SB52; -.
DR OMA; VWSNIIC; -.
DR OrthoDB; 892773at2759; -.
DR PhylomeDB; Q9SB52; -.
DR PRO; PR:Q9SB52; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SB52; baseline and differential.
DR Genevisible; Q9SB52; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR GO; GO:0005310; F:dicarboxylic acid transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015140; F:malate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015131; F:oxaloacetate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015117; F:thiosulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0071423; P:malate transmembrane transport; IBA:GO_Central.
DR GO; GO:0006839; P:mitochondrial transport; IDA:TAIR.
DR GO; GO:0015729; P:oxaloacetate transport; IBA:GO_Central.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0071422; P:succinate transmembrane transport; IBA:GO_Central.
DR GO; GO:0008272; P:sulfate transport; IBA:GO_Central.
DR GO; GO:0015709; P:thiosulfate transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Stress response; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..313
FT /note="Mitochondrial uncoupling protein 4"
FT /id="PRO_0000420258"
FT TRANSMEM 6..26
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 4..115
FT /note="Solcar 1"
FT REPEAT 124..215
FT /note="Solcar 2"
FT REPEAT 224..309
FT /note="Solcar 3"
SQ SEQUENCE 313 AA; 32873 MW; B6B418A3C8393C92 CRC64;
MGVKSFVEGG IASVIAGCST HPLDLIKVRL QLHGEAPSTT TVTLLRPALA FPNSSPAAFL
ETTSSVPKVG PISLGINIVK SEGAAALFSG VSATLLRQTL YSTTRMGLYE VLKNKWTDPE
SGKLNLSRKI GAGLVAGGIG AAVGNPADVA MVRMQADGRL PLAQRRNYAG VGDAIRSMVK
GEGVTSLWRG SALTINRAMI VTAAQLASYD QFKEGILENG VMNDGLGTHV VASFAAGFVA
SVASNPVDVI KTRVMNMKVG AYDGAWDCAV KTVKAEGAMA LYKGFVPTVC RQGPFTVVLF
VTLEQVRKLL RDF
