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 24-JAN-2024, entry version 171. 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; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Heart; RX PubMed=1375942; DOI=10.1016/s0021-9258(19)49946-8; RA Birch-MacHin M.A., Farnsworth L., Ackrell B.A.C., Cochran B., Jackson S., RA 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 succinate RT 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 (SDH) CC that is involved in complex II of the mitochondrial electron transport CC chain and is responsible for transferring electrons from succinate to CC ubiquinone (coenzyme Q) (Probable). Can act as a tumor suppressor (By CC similarity). {ECO:0000250|UniProtKB:P31040, CC ECO:0000305|PubMed:8417779}. 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: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; fumarate CC 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 cytochrome CC b560 composed of SDHC and SDHD (By similarity). Interacts with CC SDHAF2/SDH5; interaction is required for FAD attachment (By CC similarity). Interacts with TRAP1 (By similarity). Interacts with LACC1 CC (By similarity). {ECO:0000250|UniProtKB:P31040, 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 -!- PTM: Phosphorylation at Tyr-216 is important for efficient electron CC transfer in complex II and the prevention of ROS generation. CC {ECO:0000250|UniProtKB:P31040}. CC -!- PTM: Acetylated. Deacetylated by SIRT3. {ECO:0000250|UniProtKB:Q8K2B3}. CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC FRD/SDH subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; P31039; -. DR SMR; P31039; -. DR CORUM; P31039; -. DR IntAct; P31039; 2. DR STRING; 9913.ENSBTAP00000056370; -. DR PaxDb; 9913-ENSBTAP00000054495; -. DR PeptideAtlas; P31039; -. DR GeneID; 281480; -. DR KEGG; bta:281480; -. DR CTD; 6389; -. DR eggNOG; KOG2403; Eukaryota. DR InParanoid; P31039; -. DR OrthoDB; 551958at2759; -. 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; IBA:GO_Central. DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC. DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB. DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1. DR Gene3D; 4.10.80.40; succinate dehydrogenase protein domain; 1. DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 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; IPR030664; SdhA/FrdA/AprA. 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 NCBIfam; TIGR01816; sdhA_forward; 1. DR NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1. DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1. DR PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 1. DR Pfam; PF00890; FAD_binding_2; 1. DR Pfam; PF02910; Succ_DH_flav_C; 1. DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1. DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1. DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1. PE 1: Evidence at protein level; KW Acetylation; Direct protein sequencing; Electron transport; FAD; KW Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide; KW Transport; Tricarboxylic acid cycle; Tumor suppressor. FT TRANSIT 1..43 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT CHAIN 44..665 FT /note="Succinate dehydrogenase [ubiquinone] flavoprotein FT subunit, mitochondrial" FT /id="PRO_0000010334" FT ACT_SITE 341 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9YHT1" FT BINDING 69..74 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 92..107 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 276 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 297 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 309 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 408 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 441 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 452 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 457..458 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT MOD_RES 100 FT /note="Tele-8alpha-FAD histidine" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT MOD_RES 168 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 180 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 180 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 183 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 216 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 336 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 336 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 481 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 486 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 486 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 499 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 499 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 518 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 539 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 539 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 551 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 599 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 609 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 616 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 625 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 634 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 637 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT CONFLICT 242..253 FT /note="DGSIHRIRARNT -> ERVHPPHQGQEH (in Ref. 3; AAD38150)" FT /evidence="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 //