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Database: UniProt/SWISS-PROT
Entry: SDHA_RAT
LinkDB: SDHA_RAT
Original site: 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   20-JUN-2018, entry version 139.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RP   IDENTIFICATION 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
CC       (SDH) that is involved in complex II of the mitochondrial electron
CC       transport chain and is responsible for transferring electrons from
CC       succinate to ubiquinone (coenzyme Q). Can act as a tumor
CC       suppressor. {ECO:0000250|UniProtKB:P31040}.
CC   -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
CC       {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;
CC       fumarate 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
CC       cytochrome b560 composed of SDHC and SDHD (By similarity).
CC       Interacts with SDHAF2/SDH5; interaction is required for FAD
CC       attachment (By similarity). Interacts with TRAP1 (By similarity).
CC       {ECO:0000250|UniProtKB:P31040, 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.
CC       {ECO:0000250|UniProtKB:Q8K2B3}.
CC   -!- PTM: Phosphorylation at Tyr-207 is important for efficient
CC       electron transfer in complex II and the prevention of ROS
CC       generation. {ECO:0000250|UniProtKB:P31040}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
DR   EMBL; AB072907; BAB69818.1; -; mRNA.
DR   RefSeq; NP_569112.1; NM_130428.1.
DR   UniGene; Rn.228607; -.
DR   ProteinModelPortal; Q920L2; -.
DR   SMR; Q920L2; -.
DR   BioGrid; 250905; 1.
DR   ComplexPortal; CPX-564; Mitochondrial respiratory chain complex II.
DR   CORUM; Q920L2; -.
DR   IntAct; Q920L2; 1.
DR   STRING; 10116.ENSRNOP00000018336; -.
DR   CarbonylDB; Q920L2; -.
DR   iPTMnet; Q920L2; -.
DR   PhosphoSitePlus; Q920L2; -.
DR   World-2DPAGE; 0004:Q920L2; -.
DR   PaxDb; Q920L2; -.
DR   PRIDE; Q920L2; -.
DR   Ensembl; ENSRNOT00000018336; ENSRNOP00000018336; ENSRNOG00000013331.
DR   GeneID; 157074; -.
DR   KEGG; rno:157074; -.
DR   UCSC; RGD:621557; rat.
DR   CTD; 6389; -.
DR   RGD; 621557; Sdha.
DR   eggNOG; KOG2403; Eukaryota.
DR   eggNOG; COG1053; LUCA.
DR   GeneTree; ENSGT00910000144277; -.
DR   HOGENOM; HOG000160475; -.
DR   HOVERGEN; HBG001461; -.
DR   InParanoid; Q920L2; -.
DR   KO; K00234; -.
DR   OMA; GDSPWEH; -.
DR   OrthoDB; EOG091G041Z; -.
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; -.
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:0043209; C:myelin sheath; IEA:Ensembl.
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; IEA:InterPro.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IMP:RGD.
DR   GO; GO:0009061; P:anaerobic respiration; 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; IEA:Ensembl.
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; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 2.
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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   SUPFAM; SSF46977; SSF46977; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
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; Complete proteome; Direct protein sequencing;
KW   Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Transit peptide; Transport;
KW   Tricarboxylic acid cycle; Tumor suppressor.
FT   TRANSIT       1     34       Mitochondrion.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   CHAIN        35    656       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                /FTId=PRO_0000010338.
FT   NP_BIND      60     65       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   NP_BIND      83     98       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   NP_BIND     448    449       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   ACT_SITE    332    332       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     267    267       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     288    288       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     300    300       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     399    399       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     432    432       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     443    443       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   MOD_RES      91     91       Tele-8alpha-FAD histidine.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   MOD_RES     171    171       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     171    171       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     174    174       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     207    207       Phosphotyrosine; by SRC.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     242    242       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     242    242       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     327    327       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     327    327       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     415    415       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     472    472       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     477    477       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     477    477       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     490    490       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     490    490       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     509    509       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     530    530       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     530    530       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     542    542       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     590    590       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     600    600       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     607    607       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     616    616       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     625    625       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     628    628       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     639    639       N6-acetyllysine.
FT                                {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
//
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