NDUS4_ARATH
ID NDUS4_ARATH Reviewed; 154 AA.
AC Q9FJW4; Q8LC28;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;
DE AltName: Full=Protein FROSTBITE1;
DE Flags: Precursor;
GN Name=FRO1; OrderedLocusNames=At5g67590; ORFNames=K9I9.16;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12084824; DOI=10.1105/tpc.010433;
RA Lee B.H., Lee H., Xiong L., Zhu J.K.;
RT "A mitochondrial complex I defect impairs cold-regulated nuclear gene
RT expression.";
RL Plant Cell 14:1235-1251(2002).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19675153; DOI=10.1104/pp.109.141770;
RA Meyer E.H., Tomaz T., Carroll A.J., Estavillo G., Delannoy E., Tanz S.K.,
RA Small I.D., Pogson B.J., Millar A.H.;
RT "Remodeled respiration in ndufs4 with low phosphorylation efficiency
RT suppresses Arabidopsis germination and growth and alters control of
RT metabolism at night.";
RL Plant Physiol. 151:603-619(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-24.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed not to be
CC involved in catalysis. Complex I functions in the transfer of electrons
CC from NADH to the respiratory chain. The immediate electron acceptor for
CC the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12084824, ECO:0000269|PubMed:19675153}.
CC -!- SUBUNIT: Complex I is composed of at least 49 different subunits. This
CC is a component of the iron-sulfur (IP) fragment of the enzyme.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:12084824, ECO:0000305|PubMed:25732537}; Peripheral
CC membrane protein {ECO:0000269|PubMed:12084824}; Matrix side
CC {ECO:0000269|PubMed:12084824}.
CC -!- INDUCTION: By cold. {ECO:0000269|PubMed:12084824}.
CC -!- DISRUPTION PHENOTYPE: Leaves have a reduced capacity for cold
CC acclimation, appear water-soaked, leak electrolytes, and accumulate
CC reactive oxygen species constitutively. Sugar-sensitive germination,
CC delayed growth, modified respiration pathway, and altered stress
CC responses. {ECO:0000269|PubMed:12084824, ECO:0000269|PubMed:19675153}.
CC -!- SIMILARITY: Belongs to the complex I NDUFS4 subunit family.
CC {ECO:0000305}.
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DR EMBL; AB013390; BAB08467.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98364.1; -; Genomic_DNA.
DR EMBL; AK118663; BAC43258.1; -; mRNA.
DR EMBL; BT003675; AAO39903.1; -; mRNA.
DR EMBL; AY086840; AAM63888.1; -; mRNA.
DR RefSeq; NP_201560.1; NM_126159.4.
DR PDB; 7A23; EM; 3.70 A; O=1-154.
DR PDB; 7A24; EM; 3.80 A; O=1-154.
DR PDB; 7AQR; EM; 2.91 A; Q=1-154.
DR PDB; 7AR7; EM; 3.72 A; Q=35-153.
DR PDB; 7AR8; EM; 3.53 A; Q=1-154.
DR PDB; 7ARB; EM; 3.41 A; Q=1-154.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQR; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; Q9FJW4; -.
DR SMR; Q9FJW4; -.
DR BioGRID; 22137; 2.
DR IntAct; Q9FJW4; 2.
DR STRING; 3702.AT5G67590.1; -.
DR TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR iPTMnet; Q9FJW4; -.
DR PaxDb; Q9FJW4; -.
DR PRIDE; Q9FJW4; -.
DR ProteomicsDB; 251052; -.
DR EnsemblPlants; AT5G67590.1; AT5G67590.1; AT5G67590.
DR GeneID; 836895; -.
DR Gramene; AT5G67590.1; AT5G67590.1; AT5G67590.
DR KEGG; ath:AT5G67590; -.
DR Araport; AT5G67590; -.
DR TAIR; locus:2158621; AT5G67590.
DR eggNOG; KOG3389; Eukaryota.
DR HOGENOM; CLU_077196_1_0_1; -.
DR OMA; HCKKMGW; -.
DR OrthoDB; 1507807at2759; -.
DR PhylomeDB; Q9FJW4; -.
DR BioCyc; ARA:AT5G67590-MON; -.
DR BioCyc; MetaCyc:AT5G67590-MON; -.
DR PRO; PR:Q9FJW4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJW4; baseline and differential.
DR Genevisible; Q9FJW4; AT.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:TAIR.
DR GO; GO:0009631; P:cold acclimation; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR Gene3D; 3.30.160.190; -; 1.
DR InterPro; IPR006885; NADH_UbQ_FeS_4_mit.
DR InterPro; IPR038532; NDUFS4-like_sf.
DR PANTHER; PTHR12219; PTHR12219; 1.
DR Pfam; PF04800; ETC_C1_NDUFA4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transit peptide; Transport.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 25..154
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 4, mitochondrial"
FT /id="PRO_0000410791"
FT CONFLICT 4
FT /note="C -> R (in Ref. 4; AAM63888)"
FT /evidence="ECO:0000305"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:7ARB"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:7AQR"
SQ SEQUENCE 154 AA; 17134 MW; CA4D5A5CFAF5D71E CRC64;
MALCATTQRT IRIAATLRRV ARPFATDAVV ESDYKRGEIG KVSGIPEEHL SRKVIIYSPA
RTATQSGSGK LGKWKINFVS TLKWENPLMG WTSTGDPYAN VGDSALAFDS EEAAKSFAER
HGWDYKVKKP NTPLLKVKSY SDNFKWKGNP QPEN
