ID   SDHA_MESAU              Reviewed;         551 AA.
AC   Q0QF17;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial {ECO:0000250|UniProtKB:P31040};
DE            EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE   AltName: Full=Flavoprotein subunit of complex II {ECO:0000250|UniProtKB:P31040};
DE            Short=Fp {ECO:0000250|UniProtKB:P31040};
DE   Flags: Fragment;
GN   Name=SDHA {ECO:0000312|EMBL:ABD77310.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1] {ECO:0000312|EMBL:ABD77310.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver {ECO:0000312|EMBL:ABD77310.1};
RX   PubMed=16751257; DOI=10.1093/molbev/msl027;
RA   Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT   "Housekeeping genes for phylogenetic analysis of eutherian relationships.";
RL   Mol. Biol. Evol. 23:1493-1503(2006).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
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). Can act as a tumor suppressor.
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; fumarate
CC       from succinate (eukaryal route): step 1/1.
CC       {ECO:0000250|UniProtKB:P31040}.
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: Acetylated. Deacetylated by SIRT3. {ECO:0000250|UniProtKB:Q8K2B3}.
CC   -!- PTM: Phosphorylation at Tyr-157 is important for efficient electron
CC       transfer in complex II and the prevention of ROS generation.
CC       {ECO:0000250|UniProtKB:P31040}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000255}.
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DR   EMBL; DQ402977; ABD77310.1; -; mRNA.
DR   STRING; 10036.ENSMAUP00000023754; -.
DR   eggNOG; KOG2403; Eukaryota.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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:0022900; P:electron transport chain; IEA:InterPro.
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; 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; Electron transport; FAD; Flavoprotein; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Transport; Tricarboxylic acid cycle;
KW   Tumor suppressor.
FT   CHAIN           <1..>551
FT                   /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT                   subunit, mitochondrial"
FT                   /id="PRO_0000394746"
FT   ACT_SITE        282
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         33..48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         217
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         382
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         393
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         398..399
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   MOD_RES         41
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   MOD_RES         109
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         121
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P31040"
FT   MOD_RES         121
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         124
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         157
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250|UniProtKB:P31040"
FT   MOD_RES         192
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         192
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         277
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P31040"
FT   MOD_RES         277
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         365
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         422
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         427
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         427
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         440
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         440
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         459
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         480
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         480
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         489
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         489
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         492
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         540
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ABD77310.1"
FT   NON_TER         551
FT                   /evidence="ECO:0000312|EMBL:ABD77310.1"
SQ   SEQUENCE   551 AA;  60045 MW;  13CB219D31B9B678 CRC64;
     DHEFDAVVVG AGGAGLRAAF GLSEAGFNTA CGTKLFPTRS HTVAAQGGIN AALGNMEEDN
     WRWHFYDTVK GSDWLGDQDA IHYMTEQAPA SVVELENYGM PFSTTEDGKI YQRAFGGQSL
     KFGKGGQAHR SCCVADRTGH SLLHTLYGRS LRYDTSYFVE NFALDLLMEN GECRGVIALC
     IEDGSIHRIR AKNTVIATGG YGRTYFSCTS AHTSTGDGTA MVTRAGLPCQ DLEFIQFHPT
     GIYGAGCLIT EGCRGEGGIL INSQGERFME RYAPVAKDLA SRDVVSRSMT LEIREGRSWG
     PEKDHVYLQL HHLPPEQLAT RLPGISETAM IFAGVDVTKE PIPVLPTVHY NMGGIPTNYK
     GQVLKHVNGQ DQVVPGLYAC GEAACASVHG AIRLGANSLL DLVVFGRACA LSIAESCSPG
     DKVPPIKANA GEESVMNLDK LRFADGSIRT SELRLSMQKS MQSHAAVFRV GSVLQEGCEK
     ISQLYGELKH LKTFDRGMVW NTDLVETLEL QNLMLCALQT IYGAEARKES RGAHAREDYK
     VRVDEYDYYX A
//