ID SDHA_RAT Reviewed; 656 AA. AC Q920L2; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 164. 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; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Tomitsuka E., Kita K.; RT "Complex II from rat mitochondria."; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 39-67; 225-238; 354-371 AND 444-457, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord; RA Lubec G., Afjehi-Sadat L.; RL Submitted (NOV-2006) to UniProtKB. 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-207 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: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; AB072907; BAB69818.1; -; mRNA. DR RefSeq; NP_569112.1; NM_130428.1. DR AlphaFoldDB; Q920L2; -. DR SMR; Q920L2; -. DR BioGRID; 250905; 4. DR ComplexPortal; CPX-564; Mitochondrial respiratory chain complex II. DR CORUM; Q920L2; -. DR IntAct; Q920L2; 2. DR MINT; Q920L2; -. DR STRING; 10116.ENSRNOP00000018336; -. DR ChEMBL; CHEMBL4523415; -. DR CarbonylDB; Q920L2; -. DR GlyGen; Q920L2; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; Q920L2; -. DR PhosphoSitePlus; Q920L2; -. DR SwissPalm; Q920L2; -. DR jPOST; Q920L2; -. DR PaxDb; 10116-ENSRNOP00000018336; -. DR GeneID; 157074; -. DR KEGG; rno:157074; -. DR UCSC; RGD:621557; rat. DR AGR; RGD:621557; -. DR CTD; 6389; -. DR RGD; 621557; Sdha. DR VEuPathDB; HostDB:ENSRNOG00000013331; -. DR eggNOG; KOG2403; Eukaryota. DR HOGENOM; CLU_014312_6_1_1; -. DR InParanoid; Q920L2; -. DR OrthoDB; 551958at2759; -. DR PhylomeDB; Q920L2; -. DR BRENDA; 1.3.5.1; 5301. DR Reactome; R-RNO-71403; Citric acid cycle (TCA cycle). DR SABIO-RK; Q920L2; -. DR UniPathway; UPA00223; UER01006. DR PRO; PR:Q920L2; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000013331; Expressed in heart and 19 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD. DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISO:RGD. DR GO; GO:0045257; C:succinate dehydrogenase complex (ubiquinone); ISO:RGD. 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; IMP:RGD. DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central. DR GO; GO:0007399; P:nervous system development; ISO:RGD. DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal. DR GO; GO:0022904; P:respiratory electron transport chain; IMP:RGD. DR GO; GO:0006105; P:succinate metabolic process; IMP:RGD. DR GO; GO:0006099; P:tricarboxylic acid cycle; NAS:ComplexPortal. 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. DR World-2DPAGE; 0004:Q920L2; -. DR Genevisible; Q920L2; RN. 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..34 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT CHAIN 35..656 FT /note="Succinate dehydrogenase [ubiquinone] flavoprotein FT subunit, mitochondrial" FT /id="PRO_0000010338" FT ACT_SITE 332 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9YHT1" FT BINDING 60..65 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 83..98 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 267 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 288 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 300 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 399 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 432 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 443 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT BINDING 448..449 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT MOD_RES 91 FT /note="Tele-8alpha-FAD histidine" FT /evidence="ECO:0000250|UniProtKB:Q0QF01" FT MOD_RES 171 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 171 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 174 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 207 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 242 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 242 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 327 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 327 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 415 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 472 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 477 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 477 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 490 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 490 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 509 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 530 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 530 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 542 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 590 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 600 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 607 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 616 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 625 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 628 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 639 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" SQ SEQUENCE 656 AA; 71615 MW; 9E820F7FF7EC3B36 CRC64; MAGVGAVSRL LRGRRLALAG ATRGFHFSVG ESKKASAKVS DAISTQYPVV DHEFDAVVVG AGGAGLRAAF GLSEAGFNTA CLTKLFPTRS HTVAAQGGIN AALGNMEEDN WRWHFYDTVK GSDWLGDQDA IHYMTEQAPA SVVELENYGM PFSRTEDGRI YQRAFGGQSL KFGKGGQAHR CCCVADRTGH SLLHTLYGRS LRYDTSYFVE YFALDLLMEN GECRGVIALC IEDGSIHRIR AKNTIIATGG YGRTYFSCTS AHTSTGDGTA MVTRAGLPCQ DLEFVQFHPT GIYGAGCLIT EGCRGEGGIL INSQGERFME RYAPVAKDLA SRDVVSRSMT LEIREGRGCG PEKDHVYLQL HHLPPEQLAT RLPGISETAM IFAGVDVTKE PIPVLPTVHY NMGGIPTNYK GQVLKHVNGQ DQIVPGLYAC GEAACASVHG ANRLGANSLL DLVVFGRACA LSIAESCRPG DKVPPIKANA GEESVMNLDK LRFADGSVRT SELRLSMQKS MQSHAAVFRV GSVLQEGCEK VSQLYGDLQH LKTFDRGMVW NTDLVETLEL QNLMLCALQT IYGAEARKES RGAHAREDYK VRIDEYDYSK PIEGQQKKPF AEHWRKHTLS YVDTKTGKVT LDYRPVIDKT LNEADCATVP PAIRSY //