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UniProtKB/Swiss-Prot entry P21914


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

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Entry information
Entry name DHSB_DROME
Primary accession number P21914
Secondary accession number Q9V9A0
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on February 1, 1995 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 90)
Name and origin of the protein
Protein name Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial [Precursor]
Synonyms EC 1.3.5.1
Iron-sulfur subunit of complex II
Ip
Gene name
Name: SdhB
Synonyms: SDH
ORFNames: CG3283
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
DOI=10.1016/0378-1119(94)90158-9; PubMed=7958999 [NCBI, ExPASy, EBI, Israel, Japan]
Au H.C., Scheffler I.E.;
"Characterization of the gene encoding the iron-sulfur protein subunit of succinate dehydrogenase from Drosophila melanogaster.";
Gene 149:261-265(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
PRELIMINARY NUCLEOTIDE SEQUENCE OF 113-258.
PubMed=2494655 [NCBI, ExPASy, EBI, Israel, Japan]
Gould S.J., Subramani S., Scheffler I.E.;
"Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species.";
Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989).
[6]
ERRATUM.
Gould S.J., Subramani S., Scheffler I.E.;
Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993).
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
L27705; AAA61925.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013599; AAF57396.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY118923; AAM50783.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_477101.1; -.
UniGene Dm.497
3D structure databases
HSSP P07014; 1NEK. [HSSP ENTRY / PDB]
SMR P21914; 45-280.
ModBase P21914.
Protein-protein interaction databases
DIP DIP:20115N; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-003098-MON; -.
Organism-specific databases
FlyBase FBgn0014028; SdhB.
Gene expression databases
ArrayExpress P21914; -.
GermOnline CG3283; Drosophila melanogaster.
Ontologies
GO
GO:0006121; Biological process: mitochondrial electron transport, succinate to ubiquinone (inferred from direct assay from FlyBase).
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.
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).
BLOCKS P21914.
Genome annotation databases
Ensembl CG3283; Drosophila melanogaster. [Contig view]
GeneID 35590; -.
KEGG dme:Dmel_CG3283; -.
NMPDR fig|7227.3.peg.3517; -.
Phylogenomic databases
HOGENOM P21914; -.
Other
ProtoNet P21914.
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     ?        Mitochondrion (Potential). 
CHAIN   ?   297        Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial. PRO_0000010357
DOMAIN   47   140  94     2Fe-2S ferredoxin-type. 
DOMAIN   185   215  31     4Fe-4S ferredoxin-type. 
METAL   100   100        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   105   105        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   108   108        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   120   120        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   195   195        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   198   198        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   201   201        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   205   205        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   252   252        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   258   258        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   262   262        Iron-sulfur 2 (4Fe-4S) (By similarity). 
BINDING   210   210        Ubiquinone; shared with DHSD (By similarity). 
Sequence information
Length: 297 AA [This is the length of the unprocessed precursor] Molecular weight: 33741 Da [This is the MW of the unprocessed precursor] CRC64: 892380E8BAE08FFF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLATEARQIL SRVGSLVARN QMRAISNGTA QLEQQAQPKE AQEPQIKKFE IYRWNPDNAG 

        70         80         90        100        110        120 
EKPYMQTYEV DLRECGPMVL DALIKIKNEM DPTLTFRRSC REGICGSCAM NIGGTNTLAC 

       130        140        150        160        170        180 
ISKIDINTSK SLKVYPLPHM YVVRDLVPDM NNFYEQYRNI QPWLQRKNEA GEKKGKAQYL 

       190        200        210        220        230        240 
QSVEDRSKLD GLYECILCAC CSTSCPSYWW NAEKYLGPAV LMQAYRWIID SRDENSAERL 

       250        260        270        280        290 
NKLKDPFSVY RCHTIMNCTR TCPKGLNPGR AIAEIKKLLS GLASKPAPKL ETAALHK 

P21914 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
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