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Q94523

- SDHA_DROME

UniProt

Q94523 - SDHA_DROME

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Protein

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Gene

SdhA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

FAD.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei272 – 2721FADBy similarity
Binding sitei293 – 2931SubstrateBy similarity
Binding sitei305 – 3051SubstrateBy similarity
Active sitei337 – 3371Proton acceptorBy similarity
Binding sitei404 – 4041SubstrateBy similarity
Binding sitei438 – 4381FADBy similarity
Binding sitei449 – 4491SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi65 – 706FADBy similarity
Nucleotide bindingi88 – 10316FADBy similarityAdd
BLAST
Nucleotide bindingi454 – 4552FADBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC

GO - Biological processi

  1. electron transport chain Source: UniProtKB
  2. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_207898. Respiratory electron transport.
REACT_218888. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
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 namesi
Name:SdhA
Synonyms:Scs-fp
ORF Names:CG17246
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0261439. SdhA.

Subcellular locationi

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

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-KW
  2. mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141MitochondrionSequence AnalysisAdd
BLAST
Chaini42 – 661620Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialPRO_0000010340Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961Tele-8alpha-FAD histidineBy similarity

Proteomic databases

PaxDbiQ94523.
PRIDEiQ94523.

Expressioni

Gene expression databases

BgeeiQ94523.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi62892. 11 interactions.
DIPiDIP-19386N.
MINTiMINT-972926.

Structurei

3D structure databases

ProteinModelPortaliQ94523.
SMRiQ94523. Positions 51-661.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1053.
GeneTreeiENSGT00390000010046.
InParanoidiQ94523.
KOiK00234.
OMAiRDGPILQ.
OrthoDBiEOG7MH0XJ.
PhylomeDBiQ94523.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProiIPR003953. 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]
PfamiPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q94523-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGIMRVPSI LAKNAVASMQ RAAAVGVQRS YHITHGRQQA SAANPDKISK
60 70 80 90 100
QYPVVDHAYD AIVVGAGGAG LRAAFGLVAE GFRTAVITKL FPTRSHTIAA
110 120 130 140 150
QGGINAALGN MEEDDWKWHM YDTVKGSDWL GDQDAIHYMT REAPKAVIEL
160 170 180 190 200
ENYGMPFSRT QDGKIYQRAF GGQSLKFGKG GQAHRCCAVA DRTGHSLLHT
210 220 230 240 250
LYGQSLSYDC NYFVEYFALD LIFEDGECRG VLALNLEDGT LHRFRAKNTV
260 270 280 290 300
IATGGYGRAF FSCTSAHTCT GDGTAMVARQ GLPSQDLEFV QFHPTGIYGA
310 320 330 340 350
GCLITEGCRG EGGYLINGNG ERFMERYAPV AKDLASRDVV SRSMTIEIME
360 370 380 390 400
GRGAGPEKDH VYLQLHHLPP KQLAERLPGI SETAMIFAGV DVTREPIPVL
410 420 430 440 450
PTVHYNMGGV PTNYRGQVIT IDKDGKDVIV PGLYAAGEAA SSSVHGANRL
460 470 480 490 500
GANSLLDLVV FGRACAKTIA ELNKPGAPAP TLKENAGEAS VANLDKLRHA
510 520 530 540 550
NGQITTADLR LKMQKTMQHH AAVFRDGPIL QDGVNKMKEI YKQFKDIKVV
560 570 580 590 600
DRSLIWNSDL VETLELQNLL ANAQMTIVSA EARKESRGAH AREDFKVRED
610 620 630 640 650
EYDFSKPLDG QQKKPMDQHW RKHTLSWVCN DNGDITLDYR NVIDTTLDNE
660
VSTVPPAIRS Y
Length:661
Mass (Da):72,343
Last modified:February 21, 2001 - v3
Checksum:i301B578C7F765011
GO

Sequence cautioni

The sequence CAA70285.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071S → N in CAA70285. (PubMed:10071211)Curated
Sequence conflicti251 – 2511I → L in CAA70285. (PubMed:10071211)Curated
Sequence conflicti503 – 5031Q → L in CAA70285. (PubMed:10071211)Curated
Sequence conflicti520 – 5201H → L in CAA70285. (PubMed:10071211)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_477210.1. NM_057862.5.
NP_725881.1. NM_166343.3.
NP_725882.1. NM_166344.3.
UniGeneiDm.4591.

Genome annotation databases

EnsemblMetazoaiFBtr0086552; FBpp0085736; FBgn0261439.
FBtr0086553; FBpp0085737; FBgn0261439.
FBtr0086554; FBpp0085738; FBgn0261439.
GeneIDi37228.
KEGGidme:Dmel_CG17246.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqi NP_477210.1. NM_057862.5.
NP_725881.1. NM_166343.3.
NP_725882.1. NM_166344.3.
UniGenei Dm.4591.

3D structure databases

ProteinModelPortali Q94523.
SMRi Q94523. Positions 51-661.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 62892. 11 interactions.
DIPi DIP-19386N.
MINTi MINT-972926.

Proteomic databases

PaxDbi Q94523.
PRIDEi Q94523.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0086552 ; FBpp0085736 ; FBgn0261439 .
FBtr0086553 ; FBpp0085737 ; FBgn0261439 .
FBtr0086554 ; FBpp0085738 ; FBgn0261439 .
GeneIDi 37228.
KEGGi dme:Dmel_CG17246.

Organism-specific databases

CTDi 6389.
FlyBasei FBgn0261439. SdhA.

Phylogenomic databases

eggNOGi COG1053.
GeneTreei ENSGT00390000010046.
InParanoidi Q94523.
KOi K00234.
OMAi RDGPILQ.
OrthoDBi EOG7MH0XJ.
PhylomeDBi Q94523.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01006 .
Reactomei REACT_207898. Respiratory electron transport.
REACT_218888. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSi SdhA. drosophila.
GenomeRNAii 37228.
NextBioi 802625.
PROi Q94523.

Gene expression databases

Bgeei Q94523.

Family and domain databases

Gene3Di 1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProi IPR003953. 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 ]
Pfami PF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view ]
SUPFAMi SSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsi TIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEi PS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. 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.

Entry informationi

Entry nameiSDHA_DROME
AccessioniPrimary (citable) accession number: Q94523
Secondary accession number(s): A4UZP5
, C7LA77, Q0E918, Q9I7G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 21, 2001
Last modified: October 29, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3