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Database: UniProt/SWISS-PROT
Entry: SDHA_DROME
LinkDB: SDHA_DROME
Original site: SDHA_DROME 
ID   SDHA_DROME              Reviewed;         661 AA.
AC   Q94523; A4UZP5; C7LA77; Q0E918; Q9I7G3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 3.
DT   16-JAN-2019, entry version 180.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE            EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE   AltName: Full=Flavoprotein subunit of complex II;
DE            Short=FP;
DE   AltName: Full=Succinyl coenzyme A synthetase flavoprotein subunit;
DE   Flags: Precursor;
GN   Name=SdhA; Synonyms=Scs-fp; ORFNames=CG17246;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C.,
RA   Celniker S.E.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-527.
RC   TISSUE=Ovary;
RX   PubMed=10071211; DOI=10.1007/s004380050942;
RA   Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V.,
RA   Caizzi R., Barsanti P.;
RT   "Identification of nuclear genes encoding mitochondrial proteins:
RT   isolation of a collection of D. melanogaster cDNAs homologous to
RT   sequences in the Human Gene Index database.";
RL   Mol. Gen. Genet. 261:64-70(1999).
RN   [6]
RP   IDENTIFICATION.
RX   PubMed=15693940; DOI=10.1186/gb-2005-6-2-r11;
RA   Tripoli G., D'Elia D., Barsanti P., Caggese C.;
RT   "Comparison of the oxidative phosphorylation (OXPHOS) nuclear genes in
RT   the genomes of Drosophila melanogaster, Drosophila pseudoobscura and
RT   Anopheles gambiae.";
RL   Genome Biol. 6:RESEARCH11.1-RESEARCH11.17(2005).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18599508; DOI=10.1242/dev.020644;
RA   Mast J.D., Tomalty K.M., Vogel H., Clandinin T.R.;
RT   "Reactive oxygen species act remotely to cause synapse loss in a
RT   Drosophila model of developmental mitochondrial encephalopathy.";
RL   Development 135:2669-2679(2008).
CC   -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase
CC       (SDH) that is involved in complex II of the mitochondrial electron
CC       transport chain and is responsible for transferring electrons from
CC       succinate to ubiquinone (coenzyme Q). Maintaining electron
CC       transport chain function is required to prevent neurodegenerative
CC       changes seen in both early- and late-onset disorders.
CC       {ECO:0000269|PubMed:18599508}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC         Evidence={ECO:0000250|UniProtKB:P31040};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q0QF01};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       fumarate from succinate (eukaryal route): step 1/1.
CC       {ECO:0000250|UniProtKB:P31040}.
CC   -!- SUBUNIT: Component of complex II composed of four subunits: a
CC       flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
CC       composed of a large and a small subunit.
CC       {ECO:0000250|UniProtKB:Q0QF01}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q0QF01}; Matrix side
CC       {ECO:0000250|UniProtKB:Q0QF01}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of mitochondrial function has no
CC       effect on the initial stages of photoreceptor development (R cells
CC       develop normally, adopt the correct cell fates, innervate the
CC       appropriate synaptic partners, and assemble synapses normally).
CC       However, beginning around the time of eclosion, R cells
CC       degenerate, progressively losing expression of synaptic markers
CC       and undergoing extensive morphological changes. Synapse loss is
CC       caused by reactive oxygen species (ROS) production, not energy
CC       depletion, as photoreceptor ATP levels are normal.
CC       {ECO:0000269|PubMed:18599508}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA70285.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AE013599; AAG22257.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAN16127.1; -; Genomic_DNA.
DR   EMBL; AY051472; AAK92896.1; -; mRNA.
DR   EMBL; BT099627; ACU51771.1; -; mRNA.
DR   EMBL; Y09064; CAA70285.1; ALT_INIT; mRNA.
DR   RefSeq; NP_477210.1; NM_057862.5.
DR   RefSeq; NP_725881.1; NM_166343.3.
DR   RefSeq; NP_725882.1; NM_166344.3.
DR   UniGene; Dm.4591; -.
DR   ProteinModelPortal; Q94523; -.
DR   SMR; Q94523; -.
DR   BioGrid; 62892; 13.
DR   DIP; DIP-19386N; -.
DR   IntAct; Q94523; 3.
DR   STRING; 7227.FBpp0085736; -.
DR   PaxDb; Q94523; -.
DR   PRIDE; Q94523; -.
DR   EnsemblMetazoa; FBtr0086552; FBpp0085736; FBgn0261439.
DR   EnsemblMetazoa; FBtr0086553; FBpp0085737; FBgn0261439.
DR   EnsemblMetazoa; FBtr0086554; FBpp0085738; FBgn0261439.
DR   GeneID; 37228; -.
DR   KEGG; dme:Dmel_CG17246; -.
DR   CTD; 6389; -.
DR   FlyBase; FBgn0261439; SdhA.
DR   eggNOG; KOG2403; Eukaryota.
DR   eggNOG; COG1053; LUCA.
DR   GeneTree; ENSGT00910000144277; -.
DR   InParanoid; Q94523; -.
DR   KO; K00234; -.
DR   OMA; GDSPWEH; -.
DR   OrthoDB; 606981at2759; -.
DR   PhylomeDB; Q94523; -.
DR   Reactome; R-DME-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER01006.
DR   ChiTaRS; SdhA; fly.
DR   GenomeRNAi; 37228; -.
DR   PRO; PR:Q94523; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0261439; Expressed in 47 organ(s), highest expression level in adult tagma (Drosophila).
DR   Genevisible; Q94523; DM.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:FlyBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
DR   GO; GO:0045282; C:plasma membrane succinate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:FlyBase.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0022900; P:electron transport chain; IMP:UniProtKB.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS:FlyBase.
DR   Gene3D; 3.50.50.60; -; 1.
DR   Gene3D; 3.90.700.10; -; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR003952; FRD_SDH_FAD_BS.
DR   InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   SUPFAM; SSF46977; SSF46977; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF56425; SSF56425; 1.
DR   TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR   TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Electron transport; FAD; Flavoprotein; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Transit peptide; Transport;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1     41       Mitochondrion. {ECO:0000255}.
FT   CHAIN        42    661       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                /FTId=PRO_0000010340.
FT   NP_BIND      65     70       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   NP_BIND      88    103       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   NP_BIND     454    455       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   ACT_SITE    337    337       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     272    272       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     293    293       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     305    305       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     404    404       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     438    438       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     449    449       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   MOD_RES      96     96       Tele-8alpha-FAD histidine.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   CONFLICT    207    207       S -> N (in Ref. 5; CAA70285).
FT                                {ECO:0000305}.
FT   CONFLICT    251    251       I -> L (in Ref. 5; CAA70285).
FT                                {ECO:0000305}.
FT   CONFLICT    503    503       Q -> L (in Ref. 5; CAA70285).
FT                                {ECO:0000305}.
FT   CONFLICT    520    520       H -> L (in Ref. 5; CAA70285).
FT                                {ECO:0000305}.
SQ   SEQUENCE   661 AA;  72343 MW;  301B578C7F765011 CRC64;
     MSGIMRVPSI LAKNAVASMQ RAAAVGVQRS YHITHGRQQA SAANPDKISK QYPVVDHAYD
     AIVVGAGGAG LRAAFGLVAE GFRTAVITKL FPTRSHTIAA QGGINAALGN MEEDDWKWHM
     YDTVKGSDWL GDQDAIHYMT REAPKAVIEL ENYGMPFSRT QDGKIYQRAF GGQSLKFGKG
     GQAHRCCAVA DRTGHSLLHT LYGQSLSYDC NYFVEYFALD LIFEDGECRG VLALNLEDGT
     LHRFRAKNTV IATGGYGRAF FSCTSAHTCT GDGTAMVARQ GLPSQDLEFV QFHPTGIYGA
     GCLITEGCRG EGGYLINGNG ERFMERYAPV AKDLASRDVV SRSMTIEIME GRGAGPEKDH
     VYLQLHHLPP KQLAERLPGI SETAMIFAGV DVTREPIPVL PTVHYNMGGV PTNYRGQVIT
     IDKDGKDVIV PGLYAAGEAA SSSVHGANRL GANSLLDLVV FGRACAKTIA ELNKPGAPAP
     TLKENAGEAS VANLDKLRHA NGQITTADLR LKMQKTMQHH AAVFRDGPIL QDGVNKMKEI
     YKQFKDIKVV DRSLIWNSDL VETLELQNLL ANAQMTIVSA EARKESRGAH AREDFKVRED
     EYDFSKPLDG QQKKPMDQHW RKHTLSWVCN DNGDITLDYR NVIDTTLDNE VSTVPPAIRS
     Y
//
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