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Database: UniProt/SWISS-PROT
Entry: SDHA_DANRE
LinkDB: SDHA_DANRE
Original site: SDHA_DANRE 
ID   SDHA_DANRE              Reviewed;         661 AA.
AC   Q7ZVF3; Q1LV99;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   16-JAN-2019, entry version 126.
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   Flags: Precursor;
GN   Name=sdha; ORFNames=si:dkeyp-84f11.2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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).
CC       {ECO:0000250|UniProtKB:P31040}.
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   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
DR   EMBL; BX890617; CAK11468.1; -; Genomic_DNA.
DR   EMBL; BC045885; AAH45885.1; -; mRNA.
DR   RefSeq; NP_957204.1; NM_200910.1.
DR   UniGene; Dr.105233; -.
DR   ProteinModelPortal; Q7ZVF3; -.
DR   SMR; Q7ZVF3; -.
DR   STRING; 7955.ENSDARP00000018027; -.
DR   PaxDb; Q7ZVF3; -.
DR   PRIDE; Q7ZVF3; -.
DR   Ensembl; ENSDART00000015559; ENSDARP00000018027; ENSDARG00000016721.
DR   GeneID; 393884; -.
DR   KEGG; dre:393884; -.
DR   CTD; 6389; -.
DR   ZFIN; ZDB-GENE-040426-874; sdha.
DR   eggNOG; KOG2403; Eukaryota.
DR   eggNOG; COG1053; LUCA.
DR   GeneTree; ENSGT00910000144277; -.
DR   HOGENOM; HOG000160475; -.
DR   HOVERGEN; HBG001461; -.
DR   InParanoid; Q7ZVF3; -.
DR   KO; K00234; -.
DR   OrthoDB; 606981at2759; -.
DR   TreeFam; TF300763; -.
DR   Reactome; R-DRE-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER01006.
DR   PRO; PR:Q7ZVF3; -.
DR   Proteomes; UP000000437; Chromosome 19.
DR   Bgee; ENSDARG00000016721; Expressed in 37 organ(s), highest expression level in heart.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
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:UniProtKB.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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     39       Mitochondrion.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   CHAIN        41    661       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                /FTId=PRO_0000344985.
FT   NP_BIND      65     70       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   NP_BIND      88    103       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   NP_BIND     453    454       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     437    437       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     448    448       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   MOD_RES      96     96       Tele-8alpha-FAD histidine.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   CONFLICT     18     18       C -> S (in Ref. 2; AAH45885).
FT                                {ECO:0000305}.
FT   CONFLICT    545    545       D -> N (in Ref. 2; AAH45885).
FT                                {ECO:0000305}.
SQ   SEQUENCE   661 AA;  72078 MW;  636BF993BE55D19B CRC64;
     MAAVCAASRV LGTKILSCKS LPAVCQANRQ LHFSIYGKRG DAKISDGVSN QYPVVDHEFD
     AVVVGAGGAG LRAAFGLSEA GFNTACVTKL FPTRSHTVAA QGGINAALGN MEQDDWRWHF
     YDTVKGSDWL GDQDAIHYMT EQAPAAVVEL ENFGMPFSRT DDGKIYQRAF GGQSLKFGKG
     GQAHRCCCVA DRTGHSLLHT LYGRSLRYDT SYFVEYFALD LLMEDGECKG VIALCMEDGS
     IHRFRAKNTV IATGGYGRTF FSCTSAHTST GDGNAMVTRA GLPCQDLEFV QFHPTGIYGA
     GCLITEGCRG EGGILINSEG ERFMERYAPN AKDLASRDVV SRSMTIEIRE GRGVGPDKDH
     VHLQLHHLPP QQLAARLPGI SETAMIFAGV DVTKEPIPVL PTVHYNMGGI PTNYKGQVIT
     YKDGQDHVVP GLYACGEAGC ASVHGANRLG ANSLLDLVVF GRACALTIAE IDTPGEKLSP
     LKPNAGEASV ANLDKMRYAN GSTRTSEIRL NMQKTMQSHA AVFRTGDVLK EGCVKMESVY
     KSMDDIKTFD RGIVWNTDLV ETLELQNLML NAVQTIVSAE ARKESRGAHA REDFKDRVDE
     YDYSKPLQGQ VKKPFEQHWR KHTLSYVDPE TGKVTLEYRP VIDSSLDAED CAAIPPAIRS
     Y
//
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