NDA8B_ARATH
ID NDA8B_ARATH Reviewed; 106 AA.
AC Q8LGE7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8-B;
GN OrderedLocusNames=At5g18800; ORFNames=F17K4.50;
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=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 [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=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 [4]
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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 -!- SUBUNIT: Complex I is composed of at least 49 different subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion
CC intermembrane space {ECO:0000250}.
CC -!- DOMAIN: Contains four C-X9-C motifs that are predicted to form a helix-
CC coil-helix structure, permitting the formation of intramolecular
CC disulfide bonds. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA8 subunit family.
CC {ECO:0000305}.
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DR EMBL; AC068655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92613.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92614.1; -; Genomic_DNA.
DR EMBL; BT004782; AAO44048.1; -; mRNA.
DR EMBL; AK227889; BAE99861.1; -; mRNA.
DR EMBL; AY084313; AAM60901.1; -; mRNA.
DR RefSeq; NP_197381.1; NM_121885.4.
DR RefSeq; NP_850849.1; NM_180518.4.
DR PDB; 7A23; EM; 3.70 A; Y=1-106.
DR PDB; 7A24; EM; 3.80 A; Y=1-106.
DR PDB; 7AQQ; EM; 3.06 A; X=1-106.
DR PDB; 7AR7; EM; 3.72 A; X=10-105.
DR PDB; 7AR8; EM; 3.53 A; X=1-106.
DR PDB; 7ARB; EM; 3.41 A; X=1-106.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQQ; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; Q8LGE7; -.
DR SMR; Q8LGE7; -.
DR BioGRID; 17274; 2.
DR IntAct; Q8LGE7; 2.
DR STRING; 3702.AT5G18800.1; -.
DR TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR iPTMnet; Q8LGE7; -.
DR PaxDb; Q8LGE7; -.
DR PRIDE; Q8LGE7; -.
DR ProteomicsDB; 251143; -.
DR EnsemblPlants; AT5G18800.1; AT5G18800.1; AT5G18800.
DR EnsemblPlants; AT5G18800.2; AT5G18800.2; AT5G18800.
DR GeneID; 831998; -.
DR Gramene; AT5G18800.1; AT5G18800.1; AT5G18800.
DR Gramene; AT5G18800.2; AT5G18800.2; AT5G18800.
DR KEGG; ath:AT5G18800; -.
DR Araport; AT5G18800; -.
DR TAIR; locus:2144935; AT5G18800.
DR eggNOG; KOG3458; Eukaryota.
DR HOGENOM; CLU_156825_0_0_1; -.
DR InParanoid; Q8LGE7; -.
DR OMA; REVETNC; -.
DR OrthoDB; 1526152at2759; -.
DR PhylomeDB; Q8LGE7; -.
DR PRO; PR:Q8LGE7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LGE7; baseline and differential.
DR Genevisible; Q8LGE7; AT.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
DR InterPro; IPR010625; CHCH.
DR InterPro; IPR016680; NDUFA8.
DR PANTHER; PTHR13344; PTHR13344; 1.
DR Pfam; PF06747; CHCH; 1.
DR PROSITE; PS51808; CHCH; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disulfide bond; Electron transport;
KW Mitochondrion; Reference proteome; Repeat; Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..106
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 8-B"
FT /id="PRO_0000410933"
FT DOMAIN 26..67
FT /note="CHCH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DOMAIN 68..106
FT /note="CHCH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 29..39
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 49..59
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 71..81
FT /note="Cx9C motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 92..103
FT /note="Cx10C motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 29..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 39..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 71..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 81..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 50..70
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:7AQQ"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:7AQQ"
SQ SEQUENCE 106 AA; 11968 MW; 64C7CB50A0FF323E CRC64;
MSSAVDATGN PIPTSAVLTA SAKHIGMRCM PENVAFLKCK KNDPNPEKCL DKGRDVTRCV
LGLLKDLHQK CQKEMDDYVG CMYYYTNEFD LCRKEQEAFE KVCPLK
