AB24B_ARATH
ID AB24B_ARATH Reviewed; 680 AA.
AC Q9M0G9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ABC transporter B family member 24, mitochondrial;
DE Short=ABC transporter ABCB.24;
DE Short=AtABCB24;
DE AltName: Full=ABC transporter of the mitochondrion 2;
DE Short=AtATM2;
DE Short=Iron-sulfur clusters transporter ATM2;
DE AltName: Full=Protein STARIK 3;
DE Flags: Precursor;
GN Name=ABCB24; Synonyms=ATM2, STA3; OrderedLocusNames=At4g28620;
GN ORFNames=T5F17.70;
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], TISSUE SPECIFICITY, INDUCTION BY IRON
RP DEPRIVATION, AND SUBCELLULAR 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 [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 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 [5]
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 [6]
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 [7]
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 [8]
RP DISRUPTION PHENOTYPE.
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 [9]
RP FUNCTION.
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 (By
CC similarity). Not involved in the export of cyclic pyranopterin
CC monophosphate (cPMP) from mitochondria to the cytosol. {ECO:0000250,
CC ECO:0000269|PubMed:20164445}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17517886}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17517886}.
CC -!- TISSUE SPECIFICITY: Mostly expressed at low levels in roots and
CC flowers. {ECO:0000269|PubMed:17517886}.
CC -!- INDUCTION: In leaves after iron deprivation.
CC {ECO:0000269|PubMed:17517886}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:19710232}.
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; AF287698; AAG09828.1; -; mRNA.
DR EMBL; AL161573; CAB81450.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85513.1; -; Genomic_DNA.
DR PIR; T10656; T10656.
DR RefSeq; NP_194591.1; NM_119004.1.
DR AlphaFoldDB; Q9M0G9; -.
DR SMR; Q9M0G9; -.
DR STRING; 3702.AT4G28620.1; -.
DR PaxDb; Q9M0G9; -.
DR PRIDE; Q9M0G9; -.
DR ProteomicsDB; 245101; -.
DR EnsemblPlants; AT4G28620.1; AT4G28620.1; AT4G28620.
DR GeneID; 828980; -.
DR Gramene; AT4G28620.1; AT4G28620.1; AT4G28620.
DR KEGG; ath:AT4G28620; -.
DR Araport; AT4G28620; -.
DR TAIR; locus:2139870; AT4G28620.
DR eggNOG; KOG0057; Eukaryota.
DR HOGENOM; CLU_000604_84_1_1; -.
DR InParanoid; Q9M0G9; -.
DR OMA; MNEAEND; -.
DR OrthoDB; 248727at2759; -.
DR PhylomeDB; Q9M0G9; -.
DR BioCyc; ARA:AT4G28620-MON; -.
DR PRO; PR:Q9M0G9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0G9; baseline and differential.
DR Genevisible; Q9M0G9; AT.
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: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; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0046686; P:response to cadmium ion; NAS:UniProtKB.
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 ATP-binding; Ion transport; Iron; Iron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..75
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 76..680
FT /note="ABC transporter B family member 24, mitochondrial"
FT /id="PRO_0000379133"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 108..402
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 439..673
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 472..483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 680 AA; 76050 MW; 42169C4319FBE880 CRC64;
MMRVSQLQLC RTSLSYRLRS GYHHHHHLHH SFFKLIKRNS ILESPPTNAS HQSPSPITPM
VNARVMFFST STSAPHPEKI NRTSSENILR MISSYLWMKD NPKLCFRVIS AFACLVGAKF
LNVQVPFLFK VAIDWLSSSS FVDSNPYLVA AFATPSSVLI GYGIARSGSS AFNELRTSVF
SKVALRTIRT ISRKVLSRLH DLDLRYHLNR DTGALNRIID RGSRAINTIL SAMVFNIMPT
ILEISMVSCI LAYKFGAVYA LITCLSVGSY IAFTLAMTQW RIKIRKAMNE AENDASTRAI
DSLINYETVK YFNNEDYEAR KYDQLHENYE DAALQSRKSF ALLNFGQSFI FSTALSTAMV
LCSQGIMNGQ MTVGDLVMVN GLLFQLSLPL YFLGVVYSDT VQGLVDMKSM FKFLEERSDI
GDKDIDRKLP PLVLKGGSIS FENVHFSYLP ERKILDGISF EVPAGKSVAI VGSSGSGKST
ILRMIFRFFD VDSGNVKIDG QDIKEVRLES LRSSIGVVPQ DTVLFNDTIF HNIHYGNLSA
TEEEVYNAAR RAAIHDTIMK FPDKYSTAVG ERGLMLSGGE KQRVALARAF LKSPAILLCD
EATSALDSKT EAEIMKTLRS LASNRTCIFI AHRLTTAMQC DEILVMEKGK VVEKGTHEVL
LGKSGRYAKL WTQQNSKLEV
