SDHA_RAT
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 03-AUG-2022, entry version 158.
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}.
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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 iPTMnet; Q920L2; -.
DR PhosphoSitePlus; Q920L2; -.
DR World-2DPAGE; 0004:Q920L2; -.
DR jPOST; Q920L2; -.
DR PaxDb; Q920L2; -.
DR PRIDE; Q920L2; -.
DR GeneID; 157074; -.
DR KEGG; rno:157074; -.
DR UCSC; RGD:621557; rat.
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 OMA; DPIPIQP; -.
DR OrthoDB; 606981at2759; -.
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 tissues.
DR Genevisible; Q920L2; RN.
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:0005730; C:nucleolus; IEA:Ensembl.
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; IMP:RGD.
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:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC: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; IC:ComplexPortal.
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..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
