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Q94523

- SDHA_DROME

UniProt

Q94523 - SDHA_DROME

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
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (21 Feb 2001)
      Previous versions | rss
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    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

    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-SubCell
    2. mitochondrion Source: FlyBase

    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

    MSGIMRVPSI LAKNAVASMQ RAAAVGVQRS YHITHGRQQA SAANPDKISK    50
    QYPVVDHAYD AIVVGAGGAG LRAAFGLVAE GFRTAVITKL FPTRSHTIAA 100
    QGGINAALGN MEEDDWKWHM YDTVKGSDWL GDQDAIHYMT REAPKAVIEL 150
    ENYGMPFSRT QDGKIYQRAF GGQSLKFGKG GQAHRCCAVA DRTGHSLLHT 200
    LYGQSLSYDC NYFVEYFALD LIFEDGECRG VLALNLEDGT LHRFRAKNTV 250
    IATGGYGRAF FSCTSAHTCT GDGTAMVARQ GLPSQDLEFV QFHPTGIYGA 300
    GCLITEGCRG EGGYLINGNG ERFMERYAPV AKDLASRDVV SRSMTIEIME 350
    GRGAGPEKDH VYLQLHHLPP KQLAERLPGI SETAMIFAGV DVTREPIPVL 400
    PTVHYNMGGV PTNYRGQVIT IDKDGKDVIV PGLYAAGEAA SSSVHGANRL 450
    GANSLLDLVV FGRACAKTIA ELNKPGAPAP TLKENAGEAS VANLDKLRHA 500
    NGQITTADLR LKMQKTMQHH AAVFRDGPIL QDGVNKMKEI YKQFKDIKVV 550
    DRSLIWNSDL VETLELQNLL ANAQMTIVSA EARKESRGAH AREDFKVRED 600
    EYDFSKPLDG QQKKPMDQHW RKHTLSWVCN DNGDITLDYR NVIDTTLDNE 650
    VSTVPPAIRS Y 661
    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_057862.4.
    NP_725881.1. NM_166343.2.
    NP_725882.1. NM_166344.2.
    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_057862.4.
    NP_725881.1. NM_166343.2.
    NP_725882.1. NM_166344.2.
    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

    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 1, 2014
    This is version 143 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