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Q8K2B3 (DHSA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
EC=1.3.5.1
Alternative name(s):
Flavoprotein subunit of complex II
Short name=Fp
Gene names
Name:Sdha
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) By similarity. Can act as a tumor suppressor By similarity.

Catalytic activity

Succinate + ubiquinone = fumarate + ubiquinol.

Cofactor

FAD By similarity.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.

Subunit structure

Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD. Interacts with SDHAF2/SDH5; interaction is required for FAD attachment By similarity.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.

Post-translational modification

Acetylation of Lys-498 and Lys-538 is observed in liver mitochondria from fasted mice but not from fed mice.

Miscellaneous

The complex, present in mitochondria, can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone.

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion By similarity
Chain44 – 664621Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
PRO_0000010337

Regions

Nucleotide binding68 – 736FAD By similarity
Nucleotide binding91 – 10616FAD By similarity
Nucleotide binding456 – 4572FAD By similarity

Sites

Active site3401Proton acceptor By similarity
Binding site2751FAD By similarity
Binding site2961Substrate By similarity
Binding site3081Substrate By similarity
Binding site4071Substrate By similarity
Binding site4401FAD By similarity
Binding site4511Substrate By similarity

Amino acid modifications

Modified residue991Tele-8alpha-FAD histidine By similarity
Modified residue1791N6-acetyllysine Ref.6
Modified residue2521Phosphothreonine Ref.7
Modified residue3351N6-acetyllysine By similarity
Modified residue4231N6-acetyllysine Ref.6
Modified residue4851N6-acetyllysine Ref.6
Modified residue4981N6-acetyllysine Ref.6
Modified residue5381N6-acetyllysine Ref.6
Modified residue5471N6-acetyllysine Ref.6
Modified residue6081N6-acetyllysine By similarity

Experimental info

Sequence conflict691A → V in BAE26754. Ref.1
Sequence conflict2461R → Q in BAE26754. Ref.1
Sequence conflict4281Q → R in BAE26754. Ref.1
Sequence conflict5011F → L in ABD77308. Ref.4
Sequence conflict5171K → M in ABD77308. Ref.4
Sequence conflict5711L → M in ABD77308. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8K2B3 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: DDCE1535163C9449

FASTA66472,585
        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

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow, Egg, Heart, Pancreas and Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II and FVB/N.
Tissue: Mammary gland and Mammary tumor.
[3]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-14; 47-92; 121-128; 196-207; 233-246; 251-282; 313-325; 362-418; 452-480; 486-498; 528-547; 601-615; 624-633 AND 637-647.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[4]"Housekeeping genes for phylogenetic analysis of eutherian relationships."
Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-609.
Tissue: Liver.
[5]"OXPHOS genes in mammals and the molecular clock."
Weinreich D.M.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-605.
Tissue: Heart.
[6]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
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.
Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-423; LYS-485; LYS-498; LYS-538 AND LYS-547, MASS SPECTROMETRY.
Tissue: Liver.
[7]Lubec G., Kang S.
Submitted (APR-2007) to UniProtKB
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-252, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK029520 mRNA. Translation: BAC26491.1.
AK034928 mRNA. Translation: BAC28884.1.
AK049590 mRNA. Translation: BAC33831.1.
AK050475 mRNA. Translation: BAC34276.1.
AK075990 mRNA. Translation: BAC36101.1.
AK145923 mRNA. Translation: BAE26754.1.
AK147286 mRNA. Translation: BAE27822.1.
AK147624 mRNA. Translation: BAE28032.1.
AK153085 mRNA. Translation: BAE31710.1.
AK162148 mRNA. Translation: BAE36754.1.
AK169254 mRNA. Translation: BAE41018.1.
AK004362 mRNA. Translation: BAE43173.1.
BC011301 mRNA. Translation: AAH11301.1.
BC031849 mRNA. Translation: AAH31849.1.
DQ402975 mRNA. Translation: ABD77308.1.
AF095938 mRNA. Translation: AAC72373.1.
IPIIPI00230351.
RefSeqNP_075770.1. NM_023281.1.
UniGeneMm.158231.

3D structure databases

ProteinModelPortalQ8K2B3.
SMRQ8K2B3. Positions 52-664.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8K2B3. 2 interactions.
MINTMINT-4122544.

PTM databases

PhosphoSiteQ8K2B3.

2D gel databases

REPRODUCTION-2DPAGEQ8K2B3.

Proteomic databases

PaxDbQ8K2B3.
PRIDEQ8K2B3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022062; ENSMUSP00000022062; ENSMUSG00000021577.
GeneID66945.
KEGGmmu:66945.
UCSCuc007rfa.1. mouse.

Organism-specific databases

CTD6389.
MGIMGI:1914195. Sdha.

Phylogenomic databases

eggNOGCOG1053.
GeneTreeENSGT00390000010046.
HOVERGENHBG001461.
InParanoidQ8K2B3.
KOK00234.
OMACFTADAT.
OrthoDBEOG47H5PJ.

Enzyme and pathway databases

UniPathwayUPA00223; UER01006.

Gene expression databases

ArrayExpressQ8K2B3.
BgeeQ8K2B3.
GenevestigatorQ8K2B3.
GermOnlineENSMUSG00000021577. Mus musculus.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PANTHERPTHR11632:SF5. PTHR11632:SF5. 1 hit.
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF56425. SSF56425. 1 hit.
SSF46977. Succ_DH_flav_C. 1 hit.
TIGRFAMsTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSdhA. mouse.
NextBio323092.
SOURCESearch...

Entry information

Entry nameDHSA_MOUSE
AccessionPrimary (citable) accession number: Q8K2B3
Secondary accession number(s): Q0QF19 expand/collapse secondary AC list , Q3UH25, Q3UKP7, Q3V4B1, Q921P5, Q9Z1Z4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: October 1, 2002
Last modified: May 29, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents