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NDUS7_ARATH
ID   NDUS7_ARATH             Reviewed;         218 AA.
AC   Q42577;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;
DE            EC=7.1.1.2;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g11770; ORFNames=T22P22_160;
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].
RC   STRAIN=cv. C24;
RX   PubMed=8914535; DOI=10.1007/bf00040836;
RA   Heiser V., Grohmann L., Brennicke A.;
RT   "The plant mitochondrial 22 kDa (PSST) subunit of respiratory chain complex
RT   I is encoded by a nuclear gene with enhanced transcript levels in
RT   flowers.";
RL   Plant Mol. Biol. 31:1195-1204(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
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   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).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) that is believed to belong to the
CC       minimal assembly required for catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The immediate
CC       electron acceptor for the enzyme is believed to be ubiquinone (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
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 {ECO:0000269|PubMed:14671022}.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X84078; CAA58887.1; -; mRNA.
DR   EMBL; AL163814; CAB87695.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91719.1; -; Genomic_DNA.
DR   EMBL; AF428300; AAL16132.1; -; mRNA.
DR   EMBL; AY056182; AAL07031.1; -; mRNA.
DR   EMBL; AY099848; AAM20699.1; -; mRNA.
DR   EMBL; AY128912; AAM91312.1; -; mRNA.
DR   EMBL; AY085120; AAM61674.1; -; mRNA.
DR   PIR; S52286; S52286.
DR   RefSeq; NP_196738.1; NM_121215.4.
DR   PDB; 7A24; EM; 3.80 A; E=1-218.
DR   PDB; 7AQR; EM; 2.91 A; B=1-218.
DR   PDB; 7AR7; EM; 3.72 A; B=62-218.
DR   PDB; 7AR8; EM; 3.53 A; B=1-218.
DR   PDB; 7ARB; EM; 3.41 A; B=1-218.
DR   PDBsum; 7A24; -.
DR   PDBsum; 7AQR; -.
DR   PDBsum; 7AR7; -.
DR   PDBsum; 7AR8; -.
DR   PDBsum; 7ARB; -.
DR   AlphaFoldDB; Q42577; -.
DR   SMR; Q42577; -.
DR   BioGRID; 16327; 17.
DR   IntAct; Q42577; 2.
DR   STRING; 3702.AT5G11770.1; -.
DR   TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   iPTMnet; Q42577; -.
DR   PaxDb; Q42577; -.
DR   PRIDE; Q42577; -.
DR   ProteomicsDB; 238873; -.
DR   EnsemblPlants; AT5G11770.1; AT5G11770.1; AT5G11770.
DR   GeneID; 831049; -.
DR   Gramene; AT5G11770.1; AT5G11770.1; AT5G11770.
DR   KEGG; ath:AT5G11770; -.
DR   Araport; AT5G11770; -.
DR   TAIR; locus:2181885; AT5G11770.
DR   eggNOG; KOG1687; Eukaryota.
DR   HOGENOM; CLU_055737_1_2_1; -.
DR   InParanoid; Q42577; -.
DR   OMA; AGWVRKS; -.
DR   OrthoDB; 1278656at2759; -.
DR   PhylomeDB; Q42577; -.
DR   BioCyc; ARA:AT5G11770-MON; -.
DR   BioCyc; MetaCyc:AT5G11770-MON; -.
DR   PRO; PR:Q42577; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q42577; baseline and differential.
DR   Genevisible; Q42577; AT.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IBA:GO_Central.
DR   HAMAP; MF_01356; NDH1_NuoB; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome; Respiratory chain;
KW   Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..218
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   7, mitochondrial"
FT                   /id="PRO_0000020033"
FT   REGION          34..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         93
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         94
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         158
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         188
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   HELIX           65..82
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   HELIX           94..101
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   HELIX           108..111
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   HELIX           119..121
FT                   /evidence="ECO:0007829|PDB:7ARB"
FT   STRAND          123..129
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   TURN            133..135
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   HELIX           136..144
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   STRAND          151..155
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   HELIX           156..161
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   HELIX           163..165
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   HELIX           192..207
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   HELIX           211..216
FT                   /evidence="ECO:0007829|PDB:7AQR"
SQ   SEQUENCE   218 AA;  24044 MW;  D4FC0E15A4029908 CRC64;
     MAMITRNTAT RLPLLLQSQR AVAAASVSHL HTSLPALSPS TSPTSYTRPG PPSTSPPPPG
     LSKAAEFVIS KVDDLMNWAR TGSIWPMTFG LACCAVEMMH TGAARYDLDR FGIIFRPSPR
     QSDCMIVAGT LTNKMAPALR KVYDQMPEPR WVISMGSCAN GGGYYHYSYS VVRGCDRIVP
     VDIYVPGCPP TAEALLYGLL QLQKKINRRK DFLHWWNK
 
 
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