AB25B_ARATH
ID AB25B_ARATH Reviewed; 728 AA.
AC Q9LVM1; Q9LF78;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=ABC transporter B family member 25, mitochondrial;
DE Short=ABC transporter ABCB.25;
DE Short=AtABCB25;
DE AltName: Full=ABC transporter of the mitochondrion 3;
DE Short=AtATM3;
DE Short=Iron-sulfur clusters transporter ATM3;
DE AltName: Full=Protein STARIK 1;
DE Flags: Precursor;
GN Name=ABCB25; Synonyms=ATM3, STA1; OrderedLocusNames=At5g58270;
GN ORFNames=MCK7.14;
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, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11158531; DOI=10.2307/3871155;
RA Kushnir S., Babiychuk E., Storozhenko S., Davey M.W., Papenbrock J.,
RA De Rycke R., Engler G., Stephan U.W., Lange H., Kispal G., Lill R.,
RA Van Montagu M.;
RT "A mutation of the mitochondrial ABC transporter Sta1 leads to dwarfism and
RT chlorosis in the Arabidopsis mutant starik.";
RL Plant Cell 13:89-100(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=17517886; DOI=10.1074/jbc.m702383200;
RA Chen S., Sanchez-Fernandez R., Lyver E.R., Dancis A., Rea P.A.;
RT "Functional characterization of AtATM1, AtATM2, and AtATM3, a subfamily of
RT Arabidopsis half-molecule ATP-binding cassette transporters implicated in
RT iron homeostasis.";
RL J. Biol. Chem. 282:21561-21571(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [4]
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 [5]
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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [7]
RP GENE FAMILY.
RX PubMed=11855639; DOI=10.1007/s004250100661;
RA Martinoia E., Klein M., Geisler M., Bovet L., Forestier C.,
RA Kolukisaoglu H.U., Mueller-Roeber B., Schulz B.;
RT "Multifunctionality of plant ABC transporters -- more than just
RT detoxifiers.";
RL Planta 214:345-355(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY CADMIUM AND LEAD.
RX PubMed=16461380; DOI=10.1104/pp.105.074146;
RA Kim D.-Y., Bovet L., Kushnir S., Noh E.W., Martinoia E., Lee Y.;
RT "AtATM3 is involved in heavy metal resistance in Arabidopsis.";
RL Plant Physiol. 140:922-932(2006).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-612.
RX PubMed=19710232; DOI=10.1104/pp.109.143651;
RA Bernard D.G., Cheng Y., Zhao Y., Balk J.;
RT "An allelic mutant series of ATM3 reveals its key role in the biogenesis of
RT cytosolic iron-sulfur proteins in Arabidopsis.";
RL Plant Physiol. 151:590-602(2009).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20164445; DOI=10.1105/tpc.109.068478;
RA Teschner J., Lachmann N., Schulze J., Geisler M., Selbach K.,
RA Santamaria-Araujo J., Balk J., Mendel R.R., Bittner F.;
RT "A novel role for Arabidopsis mitochondrial ABC transporter ATM3 in
RT molybdenum cofactor biosynthesis.";
RL Plant Cell 22:468-480(2010).
CC -!- FUNCTION: Performs an essential function in the generation of
CC cytoplasmic iron-sulfur proteins by mediating export of Fe/S cluster
CC precursors synthesized by NFS1 and other mitochondrial proteins. Not
CC required for mitochondrial and plastid Fe-S enzymes. Probably involved
CC in the export of cyclic pyranopterin monophosphate (cPMP) from
CC mitochondria into the cytosol. Mediates glutathione-dependent
CC resistance to heavy metals such as cadmium and lead, as well as their
CC transport from roots to leaves. Regulates nonprotein thiols (NPSH) and
CC the cellular level of glutathione (GSH). {ECO:0000269|PubMed:11158531,
CC ECO:0000269|PubMed:16461380, ECO:0000269|PubMed:17517886,
CC ECO:0000269|PubMed:19710232, ECO:0000269|PubMed:20164445}.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11158531, ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:17517886}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:11158531,
CC ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17517886}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in roots, leaves, stems,
CC flowers and siliques. {ECO:0000269|PubMed:17517886}.
CC -!- INDUCTION: In roots by cadmium and lead. {ECO:0000269|PubMed:16461380}.
CC -!- DISRUPTION PHENOTYPE: Plants exhibit an enhanced sensitivity to
CC cadmium, dwarfism and chlorosis, with an altered morphology of leaf and
CC cell nuclei. Mitochondria accumulate nonheme, nonprotein iron.
CC Decreased levels of molybdenum cofactor (MOCO) and reduced activities
CC of cytosolic Fe-S proteins. Reduced ability to produce abscisic acid
CC under normal conditions and in response to drought stress. Male
CC sterility when homozygous. {ECO:0000269|PubMed:11158531,
CC ECO:0000269|PubMed:16461380, ECO:0000269|PubMed:19710232,
CC ECO:0000269|PubMed:20164445}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
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DR EMBL; AJ272202; CAB97048.1; -; mRNA.
DR EMBL; AF287699; AAG09829.1; -; mRNA.
DR EMBL; AB019228; BAA96918.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97027.1; -; Genomic_DNA.
DR EMBL; AF360334; AAK26044.1; -; mRNA.
DR EMBL; AY142686; AAN13224.1; -; mRNA.
DR RefSeq; NP_200635.1; NM_125212.3.
DR PDB; 7N58; EM; 3.40 A; A/B=1-728.
DR PDB; 7N59; EM; 3.60 A; A/B=1-728.
DR PDB; 7N5A; EM; 3.95 A; A/B=1-728.
DR PDB; 7N5B; EM; 3.80 A; A/B=1-728.
DR PDBsum; 7N58; -.
DR PDBsum; 7N59; -.
DR PDBsum; 7N5A; -.
DR PDBsum; 7N5B; -.
DR AlphaFoldDB; Q9LVM1; -.
DR SMR; Q9LVM1; -.
DR BioGRID; 21183; 7.
DR IntAct; Q9LVM1; 4.
DR STRING; 3702.AT5G58270.1; -.
DR TCDB; 3.A.1.210.8; the atp-binding cassette (abc) superfamily.
DR MetOSite; Q9LVM1; -.
DR PaxDb; Q9LVM1; -.
DR PRIDE; Q9LVM1; -.
DR ProteomicsDB; 244536; -.
DR EnsemblPlants; AT5G58270.1; AT5G58270.1; AT5G58270.
DR GeneID; 835939; -.
DR Gramene; AT5G58270.1; AT5G58270.1; AT5G58270.
DR KEGG; ath:AT5G58270; -.
DR Araport; AT5G58270; -.
DR TAIR; locus:2161183; AT5G58270.
DR eggNOG; KOG0057; Eukaryota.
DR HOGENOM; CLU_000604_84_1_1; -.
DR InParanoid; Q9LVM1; -.
DR OMA; VTEWRTH; -.
DR OrthoDB; 248727at2759; -.
DR PhylomeDB; Q9LVM1; -.
DR BioCyc; ARA:AT5G58270-MON; -.
DR UniPathway; UPA00344; -.
DR PRO; PR:Q9LVM1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVM1; baseline and differential.
DR Genevisible; Q9LVM1; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0051276; P:chromosome organization; IMP:TAIR.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0050790; P:regulation of catalytic activity; IMP:TAIR.
DR GO; GO:0010380; P:regulation of chlorophyll biosynthetic process; IMP:TAIR.
DR GO; GO:0046686; P:response to cadmium ion; IMP:TAIR.
DR GO; GO:0010288; P:response to lead ion; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ion transport; Iron; Iron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..97
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 98..728
FT /note="ABC transporter B family member 25, mitochondrial"
FT /id="PRO_0000379134"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 143..445
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 479..713
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 89..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 512..523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 612
FT /note="R->K: Resistant to sirtinol and reduced chlorophyll
FT content."
FT /evidence="ECO:0000269|PubMed:19710232"
FT CONFLICT 328
FT /note="R -> S (in Ref. 1; CAB97048)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="A -> D (in Ref. 1; CAB97048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 80420 MW; A1FDD5C518E11B50 CRC64;
MSRGSRFVRA PGLLLCRVNL QPQPKIPSFS YSLRSDYRLH NGFSNYIRRN SIRTSPVINA
FLSDNSPSPS PSPSPIRFVQ RSSMLNGRLF STSTPNPDQT TTKTKEIKTT SSDSDSAMAD
MKILRTLAGY LWMRDNPEFR FRVIAALGFL VGAKVLNVQV PFLFKLAVDW LASATGTGAS
LTTFAATNPT LLTVFATPAA VLIGYGIART GSSAFNELRT AVFSKVALRT IRSVSRKVFS
HLHDLDLRYH LSRETGGLNR IIDRGSRAIN FILSAMVFNV VPTILEISMV SGILAYKFGA
AFAWITSLSV GSYIVFTLAV TQWRTKFRKA MNKADNDAST RAIDSLINYE TVKYFNNEGY
EAEKYDQFLK KYEDAALQTQ RSLAFLNFGQ SIIFSTALST AMVLCSQGIM NGQMTVGDLV
MVNGLLFQLS LPLNFLGSVY RETIQSLVDM KSMFQLLEEK SDITNTSDAK PLVLKGGNIE
FENVHFSYLP ERKILDGISF VVPAGKSVAI VGTSGSGKST ILRMLFRFFD TDSGNIRIDG
QDIKEVRLDS LRSSIGVVPQ DTVLFNDTIF HNIHYGRLSA TEEEVYEAAR RAAIHETISN
FPDKYSTIVG ERGLKLSGGE KQRVALARTF LKSPAILLCD EATSALDSTT EAEILNALKA
LASNRTSIFI AHRLTTAMQC DEIVVLENGK VVEQGPHDEL LGKSGRYAQL WTQQNSSVDM
LDAAIKLE
