Reviewed, UniProtKB/Swiss-Prot Q8K2B3 (DHSA_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	664 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Catalytic activity	Succinate + ubiquinone = fumarate + ubiquinol.
Cofactor	FAD By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
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 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.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro succinate dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 43	43	Mitochondrion By similarity
	Chain	44 – 664	621	Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial		PRO_0000010337
Regions
	Nucleotide binding	91 – 106	16	FAD By similarity
Sites
	Active site	340	1	Proton acceptor By similarity
	Binding site	296	1	Substrate By similarity
	Binding site	308	1	Substrate By similarity
	Binding site	407	1	Substrate By similarity
	Binding site	451	1	Substrate By similarity
Amino acid modifications
	Modified residue	99	1	Tele-8alpha-FAD histidine By similarity
	Modified residue	179	1	N6-acetyllysine Ref.6
	Modified residue	252	1	Phosphothreonine Ref.7
	Modified residue	423	1	N6-acetyllysine Ref.6
	Modified residue	485	1	N6-acetyllysine Ref.6
	Modified residue	498	1	N6-acetyllysine Ref.6
	Modified residue	538	1	N6-acetyllysine Ref.6
	Modified residue	547	1	N6-acetyllysine Ref.6
Experimental info
	Sequence conflict	69	1	A → V in BAE26754. Ref.1
	Sequence conflict	246	1	R → Q in BAE26754. Ref.1
	Sequence conflict	428	1	Q → R in BAE26754. Ref.1
	Sequence conflict	501	1	F → L in ABD77308. Ref.4
	Sequence conflict	517	1	K → M in ABD77308. Ref.4
	Sequence conflict	571	1	L → M in ABD77308. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8K2B3-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: DDCE1535163C9449	FASTA	664	72,585
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 16141072] [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: 15489334] [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: 16751257] [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: 16916647] [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
EMBLGenBankDDBJ	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.
IPI	IPI00230351.
RefSeq	NP_075770.1.
UniGene	Mm.158231
3D structure databases
HSSP	HSSP built from PDB template 1NEK based on UniProtKB P10444.
ModBase	Search...
PTM databases
PhosphoSite	Q8K2B3.
2-D gel databases
REPRODUCTION-2DPAGE	Q8K2B3.
Proteomic databases
PRIDE	Q8K2B3.
Genome annotation databases
Ensembl	ENSMUSG00000021577. Mus musculus. [Contig view]
GeneID	66945.
KEGG	mmu:66945.
NMPDR	fig|10090.3.peg.28133.
Organism-specific databases
MGI	MGI:1914195. Sdha.
Phylogenomic databases
HOVERGEN	Q8K2B3.
OMA	Q8K2B3. TLEFDNL.
Enzyme and pathway databases
BRENDA	1.3.5.1. 244.
Gene expression databases
ArrayExpress	Q8K2B3.
Bgee	Q8K2B3.
GermOnline	ENSMUSG00000021577. Mus musculus.
Family and domain databases
InterPro	IPR003953. FAD_bind2_N. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR003952. FRD_SDH_FAD_BS. IPR004112. Fum_Rdtase/Succ_DH_flav_C. IPR011281. Succ_DH_flav_su_fwd. IPR014006. Succ_Dhase_frdA_Gneg. [Graphical view]
Pfam	PF00890. FAD_binding_2. 1 hit. PF02910. Succ_DH_flav_C. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
TIGRFAMs	TIGR01816. sdhA_forward. 1 hit. TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITE	PS00504. FRD_SDH_FAD_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	323092.
SOURCE	Search...

Entry information

Entry name

DHSA_MOUSE

Accession

Primary (citable) accession number: Q8K2B3
Secondary accession number(s): Q0QF19 , Q3UH25, Q3UKP7, Q3V4B1, Q921P5, Q9Z1Z4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)