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Database: UniProt/SWISS-PROT
Entry: SDHA_BOVIN
LinkDB: SDHA_BOVIN
Original site: SDHA_BOVIN 
ID   SDHA_BOVIN              Reviewed;         665 AA.
AC   P31039; Q9TUY8;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 3.
DT   28-MAR-2018, entry version 150.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE            EC=1.3.5.1 {ECO:0000305|PubMed:8417779};
DE   AltName: Full=Flavoprotein subunit of complex II;
DE            Short=Fp;
DE   Flags: Precursor;
GN   Name=SDHA; Synonyms=SDH2, SDHFP1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Heart;
RX   PubMed=1375942;
RA   Birch-MacHin M.A., Farnsworth L., Ackrell B.A.C., Cochran B.,
RA   Jackson S., Bindoff L.A., Aitken A., Diamond A.G., Turnbull D.M.;
RT   "The sequence of the flavoprotein subunit of bovine heart succinate
RT   dehydrogenase.";
RL   J. Biol. Chem. 267:11553-11558(1992).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=8142412; DOI=10.1016/0005-2728(94)90203-8;
RA   Morris A.A.M., Farnsworth L., Ackrell B.A.C., Turnbull D.M.,
RA   Birch-MacHin M.A.;
RT   "The cDNA sequence of the flavoprotein subunit of human heart
RT   succinate dehydrogenase.";
RL   Biochim. Biophys. Acta 1185:125-128(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-253.
RC   STRAIN=Hereford X Nelore;
RX   PubMed=10612251;
RA   Sonstegard T.S., Kappes S.M.;
RT   "Mapping of the SDHA locus to bovine chromosome 20.";
RL   Anim. Genet. 30:473-473(1999).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=8417779; DOI=10.1016/0005-2728(93)90067-P;
RA   Grivennikova V.G., Gavrikova E.V., Timoshin A.A., Vinogradov A.D.;
RT   "Fumarate reductase activity of bovine heart succinate-ubiquinone
RT   reductase. New assay system and overall properties of the reaction.";
RL   Biochim. Biophys. Acta 1140:282-292(1993).
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) (Probable). Can act as a
CC       tumor suppressor (By similarity). {ECO:0000250|UniProtKB:P31040,
CC       ECO:0000305|PubMed:8417779}.
CC   -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
CC       {ECO:0000305|PubMed:8417779}.
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:0000305|PubMed:8417779}.
CC   -!- SUBUNIT: Component of complex II composed of four subunits: the
CC       flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a
CC       cytochrome b560 composed of SDHC and SDHD (By similarity).
CC       Interacts with SDHAF2/SDH5; interaction is required for FAD
CC       attachment (By similarity). Interacts with TRAP1 (By similarity).
CC       {ECO:0000250|UniProtKB:P31040, 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   -!- PTM: Phosphorylation at Tyr-216 is important for efficient
CC       electron transfer in complex II and the prevention of ROS
CC       generation. {ECO:0000250|UniProtKB:P31040}.
CC   -!- PTM: Acetylated. Deacetylated by SIRT3.
CC       {ECO:0000250|UniProtKB:Q8K2B3}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
DR   EMBL; M60879; AAA30758.1; ALT_SEQ; mRNA.
DR   EMBL; AF139922; AAD38150.1; -; Genomic_DNA.
DR   PIR; A42792; A42792.
DR   RefSeq; NP_776603.1; NM_174178.2.
DR   UniGene; Bt.24449; -.
DR   ProteinModelPortal; P31039; -.
DR   SMR; P31039; -.
DR   CORUM; P31039; -.
DR   IntAct; P31039; 2.
DR   STRING; 9913.ENSBTAP00000054495; -.
DR   PaxDb; P31039; -.
DR   PeptideAtlas; P31039; -.
DR   PRIDE; P31039; -.
DR   GeneID; 281480; -.
DR   KEGG; bta:281480; -.
DR   CTD; 6389; -.
DR   eggNOG; KOG2403; Eukaryota.
DR   eggNOG; COG1053; LUCA.
DR   HOVERGEN; HBG001461; -.
DR   InParanoid; P31039; -.
DR   KO; K00234; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR   GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0055114; P:oxidation-reduction process; ISS:AgBase.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 2.
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; 2.
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   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Direct protein sequencing;
KW   Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Transit peptide; Transport;
KW   Tricarboxylic acid cycle; Tumor suppressor.
FT   TRANSIT       1     43       Mitochondrion.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   CHAIN        44    665       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                /FTId=PRO_0000010334.
FT   NP_BIND      69     74       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   NP_BIND      92    107       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   NP_BIND     457    458       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   ACT_SITE    341    341       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     276    276       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     297    297       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     309    309       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     408    408       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     441    441       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     452    452       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   MOD_RES     100    100       Tele-8alpha-FAD histidine.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   MOD_RES     168    168       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     180    180       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     180    180       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     183    183       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     216    216       Phosphotyrosine; by SRC.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     336    336       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     336    336       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     481    481       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     486    486       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     486    486       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     499    499       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     499    499       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     518    518       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     539    539       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     539    539       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     551    551       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     599    599       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     609    609       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     616    616       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     625    625       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     634    634       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     637    637       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   CONFLICT    242    253       DGSIHRIRARNT -> ERVHPPHQGQEH (in Ref. 3;
FT                                AAD38150). {ECO:0000305}.
SQ   SEQUENCE   665 AA;  72944 MW;  FE51160F248D51BC CRC64;
     MSGVAAVSRL WRARRLALTC TKWSAAWQTG TRSFHFTVDG NKRSSAKVSD AISAQYPVVD
     HEFDAVVVGA GGAGLRAAFG LSEAGFNTAC VTKLFPTRSH TVAAQGGINA ALGNMEEDNW
     RWHFYDTVKG SDWLGDQDAI HYMTEQAPAS VVELENYGMP FSRTEDGKIY QRAFGGQSLK
     FGKGGQAHRC CCVADRTGHS LLHTLYGRSL RYDTSYFVEY FALDLLMESG ECRGVIALCI
     EDGSIHRIRA RNTVIATGGY GRTYFSCTSA HTSTGDGTAM VTRAGLPCQD LEFVQFHPTG
     IYGAGCLITE GCRGEGGILI NSQGERFMER YAPVAKDLAS RDVVSRSMTL EIREGRGCGP
     EKDHVYLQLH HLPPAQLAMR LPGISETAMI FAGVDVTKEP IPVLPTVHYN MGGIPTNYKG
     QVLRHVNGQD QGVPGLYACG EAACASVHGA NRLGANSLLD LVVFGRACAL SIAESCRPGD
     KVPSIKPNAG EESVMNLDKL RFANGSIRTS ELRLNMQKSM QSHAAVFRVG SVLQEGCEKI
     SSLYGDLRHL KTFDRGMVWN TDLVETLELQ NLMLCALQTI YGAEARKESR GGPRREDFKE
     RVDEYDYSKP IQGQQKKPFE QHWRKHTLSY VDIKTGKVTL EYRPVIDRTL NETDCATVPP
     AIGSY
//
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