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UniProtKB/Swiss-Prot entry Q8K2B3


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

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Entry information
Entry name DHSA_MOUSE
Primary accession number Q8K2B3
Secondary accession numbers Q0QF19 Q3UH25 Q3UKP7 Q3V4B1 Q921P5 Q9Z1Z4
Integrated into Swiss-Prot on September 27, 2004
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 60)
Name and origin of the protein
Protein name Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial [Precursor]
Synonyms EC 1.3.5.1
Flavoprotein subunit of complex II
Fp
Gene name
Name: Sdha
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Bone marrow, Egg, Heart, Pancreas, and Testis;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N;
TISSUE=Mammary gland, and Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 1-14; 47-92; 121-128; 196-207; 233-246; 251-282; 313-325; 380-418; 452-480; 486-498; 528-547; 601-615; 624-633 AND 637-647.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 59-609.
TISSUE=Liver;
DOI=10.1093/molbev/msl027; PubMed=16751257 [NCBI, ExPASy, EBI, Israel, Japan]
Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
"Housekeeping genes for phylogenetic analysis of eutherian relationships.";
Mol. Biol. Evol. 23:1493-1503(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 74-605.
TISSUE=Heart;
Weinreich D.M.;
"OXPHOS genes in mammals and the molecular clock.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 76-92; 233-246; 362-379 AND 452-465, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-423; LYS-485; LYS-498; LYS-538 AND LYS-547, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-252, AND MASS SPECTROMETRY.
TISSUE=Brain;
Lubec G., Kang S.;
Submitted (APR-2007) to UniProtKB.
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
AK029520; BAC26491.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK034928; BAC28884.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK049590; BAC33831.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK050475; BAC34276.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK075990; BAC36101.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK145923; BAE26754.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK147286; BAE27822.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK147624; BAE28032.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK153085; BAE31710.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK162148; BAE36754.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK169254; BAE41018.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK004362; BAE43173.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011301; AAH11301.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031849; AAH31849.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ402975; ABD77308.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF095938; AAC72373.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_075770.1; -.
UniGene Mm.158231
3D structure databases
HSSP P10444; 1NEK. [HSSP ENTRY / PDB]
ModBase Q8K2B3.
PTM databases
PhosphoSite Q8K2B3; -.
2D gel databases
REPRODUCTION-2DPAGE Q8K2B3; -.
Organism-specific databases
MGI MGI:1914195; Sdha.
Gene expression databases
ArrayExpress Q8K2B3; -.
GermOnline ENSMUSG00000021577; Mus musculus.
Ontologies
GO
GO:0005743; Cellular component: mitochondrial inner membrane (inferred from direct assay from MGI).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
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 IPR003953; FAD_bind2_N.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR003952; FRD_SDH_FAD_BS.
IPR004112; Fum_Rdtase/Succ_DHase_flav_C.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR011281; Succ_DHase_flav_su_fwd.
IPR014006; Succ_Dhase_frdA_Gneg.
Graphical view of domain structure.
Pfam PF00890; FAD_binding_2; 1.
PF02910; Succ_DH_flav_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00411; PNDRDTASEI.
TIGRFAMs TIGR01816; sdhA_forward; 1.
TIGR01812; sdhA_frdA_Gneg; 1.
PROSITE PS00504; FRD_SDH_FAD_BINDING; 1.
ProtoNet Q8K2B3.
Genome annotation databases
Ensembl ENSMUSG00000021577; Mus musculus. [Contig view]
GeneID 66945; -.
KEGG mmu:66945; -.
NMPDR fig|10090.3.peg.28133; -.
Phylogenomic databases
HOVERGEN Q8K2B3; -.
Other
NextBio 323092; -.
SOURCE Sdha; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein; Transit peptide; Transport; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    43  43     Mitochondrion (By similarity). 
CHAIN   44   664  621     Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial. PRO_0000010337
NP_BIND   91   106  16     FAD (By similarity). 
ACT_SITE   340   340        Proton acceptor (By similarity). 
BINDING   296   296        Substrate (By similarity). 
BINDING   308   308        Substrate (By similarity). 
BINDING   407   407        Substrate (By similarity). 
BINDING   451   451        Substrate (By similarity). 
MOD_RES   99    99        Tele-8alpha-FAD histidine (By similarity). 
MOD_RES   179   179        N6-acetyllysine. 
MOD_RES   252   252        Phosphothreonine. 
MOD_RES   423   423        N6-acetyllysine. 
MOD_RES   485   485        N6-acetyllysine. 
MOD_RES   498   498        N6-acetyllysine. 
MOD_RES   538   538        N6-acetyllysine. 
MOD_RES   547   547        N6-acetyllysine. 
CONFLICT   69    69        A -> V (in Ref. 1; BAE26754). 
CONFLICT   246   246        R -> Q (in Ref. 1; BAE26754). 
CONFLICT   428   428        Q -> R (in Ref. 1; BAE26754). 
CONFLICT   501   501        F -> L (in Ref. 4; ABD77308). 
CONFLICT   517   517        K -> M (in Ref. 4; ABD77308). 
CONFLICT   571   571        L -> M (in Ref. 4; ABD77308). 
Sequence information
Length: 664 AA [This is the length of the unprocessed precursor] Molecular weight: 72585 Da [This is the MW of the unprocessed precursor] CRC64: DDCE1535163C9449 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGVGAVSRL LRGRRLALTG AWPGTLQKQT CGFHFSVGEN KKASAKVSDA ISTQYPVVDH 

        70         80         90        100        110        120 
EFDAVVVGAG GAGLRAAFGL SEAGFNTACL TKLFPTRSHT VAAQGGINAA LGNMEEDNWR 

       130        140        150        160        170        180 
WHFYDTVKGS DWLGDQDAIH YMTEQAPASV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF 

       190        200        210        220        230        240 
GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE 

       250        260        270        280        290        300 
DGSIHRIRAK NTVIATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI 

       310        320        330        340        350        360 
YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE 

       370        380        390        400        410        420 
KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ 

       430        440        450        460        470        480 
VLKHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IAESCRPGDK 

       490        500        510        520        530        540 
VPSIKANAGE ESVMNLDKLR FADGSIRTSE LRLNMQKSMQ NHAAVFRVGS VLQEGCEKIS 

       550        560        570        580        590        600 
QLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR 

       610        620        630        640        650        660 
VDEYDYSKPI QGQQKKPFGE HWRKHTLSYV DIKTGKVTLE YRPVIDKTLN EADCATVPPA 


IRSY 

Q8K2B3 in FASTA format

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