INDH_ARATH
ID INDH_ARATH Reviewed; 313 AA.
AC O49472; Q8LEZ2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Iron-sulfur protein required for NADH dehydrogenase, mitochondrial {ECO:0000303|PubMed:24179128, ECO:0000303|PubMed:26801215};
DE AltName: Full=IND1 homolog {ECO:0000303|PubMed:24179128, ECO:0000303|PubMed:26801215};
DE AltName: Full=IND1-like protein {ECO:0000303|PubMed:26801215};
DE AltName: Full=Nucleotide-binding protein-like {ECO:0000303|PubMed:26801215};
DE Flags: Precursor;
GN Name=INDH {ECO:0000303|PubMed:24179128, ECO:0000303|PubMed:26801215};
GN Synonyms=INDL {ECO:0000303|PubMed:26801215},
GN NUBPL {ECO:0000303|PubMed:26801215};
GN OrderedLocusNames=At4g19540 {ECO:0000312|Araport:AT4G19540};
GN ORFNames=F24J7.100 {ECO:0000312|EMBL:CAA16931.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24179128; DOI=10.1105/tpc.113.117283;
RA Wydro M.M., Sharma P., Foster J.M., Bych K., Meyer E.H., Balk J.;
RT "The evolutionarily conserved iron-sulfur protein INDH is required for
RT complex I assembly and mitochondrial translation in Arabidopsis
RT [corrected].";
RL Plant Cell 25:4014-4027(2013).
RN [6]
RP REVIEW ON MITOCHONDRIAL COMPLEX I.
RX PubMed=26801215; DOI=10.1016/j.bbabio.2016.01.009;
RA Subrahmanian N., Remacle C., Hamel P.P.;
RT "Plant mitochondrial Complex I composition and assembly: A review.";
RL Biochim. Biophys. Acta 1857:1001-1014(2016).
CC -!- FUNCTION: Essential during early vegetative growth (PubMed:24179128).
CC Required for the assembly of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I) (PubMed:24179128). Involved in
CC mitochondrial translation activity (PubMed:24179128). May deliver of
CC one or more Fe-S clusters to complex I subunits (By similarity).
CC {ECO:0000250|UniProtKB:Q8TB37, ECO:0000269|PubMed:24179128}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q6CE48};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q6CE48};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:24179128}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutants are lethal, seeds failing to
CC germinate or arrested seedlings in early growth (PubMed:24179128). Loss
CC of mitochondrial complex I and low levels of a 650-kDa assembly
CC intermediate associated with a reduced mitochondrial translation
CC activity (PubMed:24179128). Heterozygous plants display delayed bolting
CC and flowering, with small and highly branched inflorescences; they also
CC have sporophytic defects in female and male gametophyte development
CC (PubMed:24179128). {ECO:0000269|PubMed:24179128}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC {ECO:0000305}.
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DR EMBL; AL021768; CAA16931.1; -; Genomic_DNA.
DR EMBL; AL161551; CAB78956.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84196.1; -; Genomic_DNA.
DR EMBL; AK229020; BAF00906.1; -; mRNA.
DR EMBL; AY085137; AAM61690.1; -; mRNA.
DR PIR; T06147; T06147.
DR RefSeq; NP_193689.1; NM_118074.2.
DR AlphaFoldDB; O49472; -.
DR SMR; O49472; -.
DR STRING; 3702.AT4G19540.1; -.
DR PaxDb; O49472; -.
DR PRIDE; O49472; -.
DR ProteomicsDB; 177582; -.
DR EnsemblPlants; AT4G19540.1; AT4G19540.1; AT4G19540.
DR GeneID; 827696; -.
DR Gramene; AT4G19540.1; AT4G19540.1; AT4G19540.
DR KEGG; ath:AT4G19540; -.
DR Araport; AT4G19540; -.
DR TAIR; locus:2122995; AT4G19540.
DR eggNOG; KOG3022; Eukaryota.
DR HOGENOM; CLU_024839_0_2_1; -.
DR InParanoid; O49472; -.
DR OMA; NMAYFTP; -.
DR OrthoDB; 1166096at2759; -.
DR PhylomeDB; O49472; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49472; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR044304; NUBPL-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR42961; PTHR42961; 1.
DR Pfam; PF10609; ParA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; ATP-binding; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..313
FT /note="Iron-sulfur protein required for NADH dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000454914"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 19
FT /note="H -> P (in Ref. 4; AAM61690)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="E -> D (in Ref. 4; AAM61690)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 33426 MW; E47E985D3E738B93 CRC64;
MATVALLRSL RRRELHAAHI SAYKFSSASA GGRTTELRLH GVKDIIAVAS GKGGVGKSST
AVNLAVALAN KCELKIGLLD ADVYGPSVPI MMNINQKPQV NQDMKMIPVE NYGVKCMSMG
LLVEKDAPLV WRGPMVMSAL AKMTKGVDWG DLDILVVDMP PGTGDAQISI SQNLKLSGAV
IVSTPQDVAL ADANRGISMF DKVRVPILGL VENMSCFVCP HCNEPSFIFG KEGARRTAAK
KGLKLIGEIP LEMSIREGSD EGVPVVVSSP GSIVSKAYQD LAQNVVKGLK ELRENPDNEI
QMKLNVPHSS HSS
