Q94523 (DHSA_DROME) Reviewed, UniProtKB/Swiss-Prot

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
Succinyl coenzyme A synthetase flavoprotein subunit

Gene names

Name:	SdhA
Synonyms:	Scs-fp
ORF Names:	CG17246

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	661 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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). Maintaining electron transport chain function is required to prevent neurodegenerative changes seen in both early- and late-onset disorders. Ref.7
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: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit By similarity.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.
Disruption phenotype	Disruption of mitochondrial function has no effect on the initial stages of photoreceptor development (R cells develop normally, adopt the correct cell fates, innervate the appropriate synaptic partners, and assemble synapses normally). However, beginning around the time of eclosion, R cells degenerate, progressively losing expression of synaptic markers and undergoing extensive morphological changes. Synapse loss is caused by reactive oxygen species (ROS) production, not energy depletion, as photoreceptor ATP levels are normal. Ref.7
Sequence similarities	Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
Sequence caution	The sequence CAA70285.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from mutant phenotype Ref.7. Source: UniProtKB tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 16212416. Source: FlyBase
Molecular_function	flavin adenine dinucleotide binding 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 – 41	41	Mitochondrion Potential
	Chain	42 – 661	620	Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial		PRO_0000010340
Regions
	Nucleotide binding	65 – 70	6	FAD By similarity
	Nucleotide binding	88 – 103	16	FAD By similarity
	Nucleotide binding	454 – 455	2	FAD By similarity
Sites
	Active site	337	1	Proton acceptor By similarity
	Binding site	272	1	FAD By similarity
	Binding site	293	1	Substrate By similarity
	Binding site	305	1	Substrate By similarity
	Binding site	404	1	Substrate By similarity
	Binding site	438	1	FAD By similarity
	Binding site	449	1	Substrate By similarity
Amino acid modifications
	Modified residue	96	1	Tele-8alpha-FAD histidine By similarity
Experimental info
	Sequence conflict	207	1	S → N in CAA70285. Ref.5
	Sequence conflict	251	1	I → L in CAA70285. Ref.5
	Sequence conflict	503	1	Q → L in CAA70285. Ref.5
	Sequence conflict	520	1	H → L in CAA70285. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q94523 [UniParc]. Last modified February 21, 2001. Version 3. Checksum: 301B578C7F765011	FASTA	661	72,343
	10 20 30 40 50 60 MSGIMRVPSI LAKNAVASMQ RAAAVGVQRS YHITHGRQQA SAANPDKISK QYPVVDHAYD 70 80 90 100 110 120 AIVVGAGGAG LRAAFGLVAE GFRTAVITKL FPTRSHTIAA QGGINAALGN MEEDDWKWHM 130 140 150 160 170 180 YDTVKGSDWL GDQDAIHYMT REAPKAVIEL ENYGMPFSRT QDGKIYQRAF GGQSLKFGKG 190 200 210 220 230 240 GQAHRCCAVA DRTGHSLLHT LYGQSLSYDC NYFVEYFALD LIFEDGECRG VLALNLEDGT 250 260 270 280 290 300 LHRFRAKNTV IATGGYGRAF FSCTSAHTCT GDGTAMVARQ GLPSQDLEFV QFHPTGIYGA 310 320 330 340 350 360 GCLITEGCRG EGGYLINGNG ERFMERYAPV AKDLASRDVV SRSMTIEIME GRGAGPEKDH 370 380 390 400 410 420 VYLQLHHLPP KQLAERLPGI SETAMIFAGV DVTREPIPVL PTVHYNMGGV PTNYRGQVIT 430 440 450 460 470 480 IDKDGKDVIV PGLYAAGEAA SSSVHGANRL GANSLLDLVV FGRACAKTIA ELNKPGAPAP 490 500 510 520 530 540 TLKENAGEAS VANLDKLRHA NGQITTADLR LKMQKTMQHH AAVFRDGPIL QDGVNKMKEI 550 560 570 580 590 600 YKQFKDIKVV DRSLIWNSDL VETLELQNLL ANAQMTIVSA EARKESRGAH AREDFKVRED 610 620 630 640 650 660 EYDFSKPLDG QQKKPMDQHW RKHTLSWVCN DNGDITLDYR NVIDTTLDNE VSTVPPAIRS Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." 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. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." 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. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." 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. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[4]	Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Identification of nuclear genes encoding mitochondrial proteins: isolation of a collection of D. melanogaster cDNAs homologous to sequences in the Human Gene Index database." Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R., Barsanti P. Mol. Gen. Genet. 261:64-70(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-527. Tissue: Ovary.
[6]	"Comparison of the oxidative phosphorylation (OXPHOS) nuclear genes in the genomes of Drosophila melanogaster, Drosophila pseudoobscura and Anopheles gambiae." Tripoli G., D'Elia D., Barsanti P., Caggese C. Genome Biol. 6:RESEARCH11.1-RESEARCH11.17(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[7]	"Reactive oxygen species act remotely to cause synapse loss in a Drosophila model of developmental mitochondrial encephalopathy." Mast J.D., Tomalty K.M., Vogel H., Clandinin T.R. Development 135:2669-2679(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013599 Genomic DNA. Translation: AAG22257.1. AE013599 Genomic DNA. Translation: AAN16127.1. AY051472 mRNA. Translation: AAK92896.1. BT099627 mRNA. Translation: ACU51771.1. Y09064 mRNA. Translation: CAA70285.1. Different initiation.
RefSeq	NP_477210.1. NM_057862.4. NP_725881.1. NM_166343.2. NP_725882.1. NM_166344.2.
UniGene	Dm.4591.
3D structure databases
ProteinModelPortal	Q94523.
SMR	Q94523. Positions 51-661.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-19386N.
MINT	MINT-972926.
Proteomic databases
PaxDb	Q94523.
PRIDE	Q94523.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0086552; FBpp0085736; FBgn0261439. FBtr0086553; FBpp0085737; FBgn0261439. FBtr0086554; FBpp0085738; FBgn0261439.
GeneID	37228.
KEGG	dme:Dmel_CG17246.
Organism-specific databases
CTD	6389.
FlyBase	FBgn0261439. SdhA.
Phylogenomic databases
eggNOG	COG1053.
GeneTree	ENSGT00390000010046.
InParanoid	Q94523.
KO	K00234.
OMA	CFTADAT.
OrthoDB	EOG4XKSP0.
PhylomeDB	Q94523.
Enzyme and pathway databases
UniPathway	UPA00223; UER01006.
Gene expression databases
Bgee	Q94523.
GermOnline	CG17246. Drosophila melanogaster.
Family and domain databases
Gene3D	1.20.58.100. 1 hit.
InterPro	IPR003953. FAD_bind_dom. IPR003952. FRD_SDH_FAD_BS. IPR015939. Fum_Rdtase/Succ_DH_flav-like_C. IPR011281. Succ_DH_flav_su_fwd. IPR014006. Succ_Dhase_FrdA_Gneg. [Graphical view]
PANTHER	PTHR11632:SF5. PTHR11632:SF5. 1 hit.
Pfam	PF00890. FAD_binding_2. 1 hit. PF02910. Succ_DH_flav_C. 1 hit. [Graphical view]
SUPFAM	SSF46977. Succ_DH_flav_C. 1 hit.
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
ChiTaRS	SdhA. drosophila.
GenomeRNAi	37228.
NextBio	802625.

Entry information

Entry name

DHSA_DROME

Accession

Primary (citable) accession number: Q94523
Secondary accession number(s): A4UZP5 , C7LA77, Q0E918, Q9I7G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 21, 2001
Last modified:	April 3, 2013
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project