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 03-AUG-2022, entry version 165.
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}.
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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.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 InParanoid; P31039; -.
DR OrthoDB; 606981at2759; -.
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: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; IEA:UniProtKB-UniPathway.
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; 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 PANTHER; PTHR11632; PTHR11632; 1.
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 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
