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UniProtKB/Swiss-Prot entry Q8LB02


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHSB2_ARATH
Primary accession number Q8LB02
Secondary accession numbers Q9FM32 Q9G3L9
Integrated into Swiss-Prot on July 25, 2006
Sequence was last modified on July 25, 2006 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 49)
Name and origin of the protein
Protein name Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 2, mitochondrial [Precursor]
Synonyms EC 1.3.5.1
Iron-sulfur subunit of complex II
Ip
Gene name
Name: SDH2-2
OrderedLocusNames: At5g40650
ORFNames: MNF13.21, MNF13.170
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
DOI=10.1023/A:1010612506070; PubMed=11442063 [NCBI, ExPASy, EBI, Israel, Japan]
Figueroa P., Leon G., Elorza A., Holuigue L., Jordana X.;
"Three different genes encode the iron-sulphur subunit of succinate dehydrogenase in Arabidopsis thaliana.";
Plant Mol. Biol. 46:241-250(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/5.1.41; PubMed=9628582 [NCBI, ExPASy, EBI, Israel, Japan]
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
SUBUNIT, AND TISSUE SPECIFICITY.
DOI=10.1023/A:1019926301981; PubMed=12374303 [NCBI, ExPASy, EBI, Israel, Japan]
Figueroa P., Leon G., Elorza A., Holuigue L., Araya A., Jordana X.;
"The four subunits of mitochondrial respiratory complex II are encoded by multiple nuclear genes and targeted to mitochondria in Arabidopsis thaliana.";
Plant Mol. Biol. 50:725-734(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1105/tpc.016055; PubMed=14671022 [NCBI, ExPASy, EBI, Israel, Japan]
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins.";
Plant Cell 16:241-256(2004).
[7]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
DOI=10.1104/pp.104.049528; PubMed=15563621 [NCBI, ExPASy, EBI, Israel, Japan]
Elorza A., Leon G., Gomez I., Mouras A., Holuigue L., Araya A., Jordana X.;
"Nuclear SDH2-1 and SDH2-2 genes, encoding the iron-sulfur subunit of mitochondrial complex II in Arabidopsis, have distinct cell-specific expression patterns and promoter activities.";
Plant Physiol. 136:4072-4087(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ278911; CAC19856.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB009052; BAB08537.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY074299; AAL66996.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY123036; AAM67569.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087504; AAM65047.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_198881.1; -.
UniGene At.20145
3D structure databases
HSSP P07014; 1NEK. [HSSP ENTRY / PDB]
ModBase Q8LB02.
Organism-specific databases
GeneFarm 2169; 175.
TAIR At5g40650; -.
Gene expression databases
GermOnline AT5G40650; Arabidopsis thaliana.
Ontologies
GO
GO:0005743; Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051538; Molecular function: 3 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008177; Molecular function: succinate dehydrogenase (ubiquinone) activity (inferred from electronic annotation from EC).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006058; 2Fe2S_fd_BS.
IPR001450; 4Fe4S_Fe_S_bd.
IPR012675; b-grasp_ferredoxin-like.
IPR001041; Ferredoxin.
IPR012285; Fum_reductase_C.
IPR004489; Succ_DHase/fum_Rdtase_Fe-S.
Graphical view of domain structure.
Gene3D G3DSA:3.10.20.30; Ferredoxin_fold; 1.
G3DSA:1.10.1060.10; Fum_reductase_C; 1.
Pfam PF00111; Fer2; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00384; dhsB; 1.
PROSITE PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS00198; 4FE4S_FER_1; 1.
PS51379; 4FE4S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8LB02.
Genome annotation databases
GeneID 834065; -.
GenomeReviews BA000015_GR; AT5G40650.
KEGG ath:AT5G40650; -.
NMPDR fig|3702.1.peg.25769; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; 3Fe-4S; 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Transit peptide; Transport; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    28  28     Mitochondrion (Potential). 
CHAIN   29   280  252     Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 2, mitochondrial. PRO_0000247596
DOMAIN   51   140  90     2Fe-2S ferredoxin-type. 
DOMAIN   183   213  31     4Fe-4S ferredoxin-type. 
METAL   101   101        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   106   106        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   109   109        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   121   121        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   193   193        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   196   196        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   199   199        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   203   203        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   250   250        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   256   256        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   260   260        Iron-sulfur 2 (4Fe-4S) (By similarity). 
BINDING   208   208        Ubiquinone; shared with DHSD (By similarity). 
CONFLICT   14    14        S -> P (in Ref. 1 and 4). 
CONFLICT   31    31        T -> K (in Ref. 1 and 4). 
CONFLICT   127   127        S -> F (in Ref. 1; CAC19856). 
Sequence information
Length: 280 AA [This is the length of the unprocessed precursor] Molecular weight: 31141 Da [This is the MW of the unprocessed precursor] CRC64: 1F505A8C7D68DACD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAFGLIGRVV GTKSSRLSTA ARLIPARWTS TGSEAQSKAS TGGGGASLKT FQIYRWNPDN 

        70         80         90        100        110        120 
PGKPELQDYK IDLKDCGPMV LDALIKIKNE MDPSLTFRRS CREGICGSCA MNIDGCNGLA 

       130        140        150        160        170        180 
CLTKIESGSK ETTITPLPHM FVIKDLVVDM TNFYNQYKSI EPWLKRKNPA SVPGKEILQS 

       190        200        210        220        230        240 
KKDRAKLDGM YECILCACCS TSCPSYWWNP ESYLGPAALL HANRWISDSR DEYTKERLEA 

       250        260        270        280 
IDDEFKLYRC HTILNCARAC PKGLNPGKQI THIKQLQKSG 

Q8LB02 in FASTA format

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