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Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (Fp)

 SDHA_RAT                Reviewed;         656 AA.
Q920L2;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
23-MAY-2018, entry version 138.
RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
AltName: Full=Flavoprotein subunit of complex II;
Short=Fp;
Flags: Precursor;
Name=Sdha;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Tomitsuka E., Kita K.;
"Complex II from rat mitochondria.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 39-67; 225-238; 354-371 AND 444-457, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
-!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase
(SDH) that is involved in complex II of the mitochondrial electron
transport chain and is responsible for transferring electrons from
succinate to ubiquinone (coenzyme Q). Can act as a tumor
suppressor. {ECO:0000250|UniProtKB:P31040}.
-!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
{ECO:0000250|UniProtKB:P31040}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:Q0QF01};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
fumarate from succinate (eukaryal route): step 1/1.
{ECO:0000250|UniProtKB:P31040}.
-!- SUBUNIT: Component of complex II composed of four subunits: the
flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a
cytochrome b560 composed of SDHC and SDHD (By similarity).
Interacts with SDHAF2/SDH5; interaction is required for FAD
attachment (By similarity). Interacts with TRAP1 (By similarity).
{ECO:0000250|UniProtKB:P31040, ECO:0000250|UniProtKB:Q0QF01}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q0QF01}; Matrix side
{ECO:0000250|UniProtKB:Q0QF01}.
-!- PTM: Acetylated. Deacetylated by SIRT3.
{ECO:0000250|UniProtKB:Q8K2B3}.
-!- PTM: Phosphorylation at Tyr-207 is important for efficient
electron transfer in complex II and the prevention of ROS
generation. {ECO:0000250|UniProtKB:P31040}.
-!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
FRD/SDH subfamily. {ECO:0000305}.
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EMBL; AB072907; BAB69818.1; -; mRNA.
RefSeq; NP_569112.1; NM_130428.1.
UniGene; Rn.228607; -.
ProteinModelPortal; Q920L2; -.
SMR; Q920L2; -.
BioGrid; 250905; 1.
CORUM; Q920L2; -.
IntAct; Q920L2; 1.
STRING; 10116.ENSRNOP00000018336; -.
CarbonylDB; Q920L2; -.
iPTMnet; Q920L2; -.
PhosphoSitePlus; Q920L2; -.
World-2DPAGE; 0004:Q920L2; -.
PaxDb; Q920L2; -.
PRIDE; Q920L2; -.
Ensembl; ENSRNOT00000018336; ENSRNOP00000018336; ENSRNOG00000013331.
GeneID; 157074; -.
KEGG; rno:157074; -.
UCSC; RGD:621557; rat.
CTD; 6389; -.
RGD; 621557; Sdha.
eggNOG; KOG2403; Eukaryota.
eggNOG; COG1053; LUCA.
GeneTree; ENSGT00910000144277; -.
HOGENOM; HOG000160475; -.
HOVERGEN; HBG001461; -.
InParanoid; Q920L2; -.
KO; K00234; -.
OMA; GDSPWEH; -.
OrthoDB; EOG091G041Z; -.
PhylomeDB; Q920L2; -.
BRENDA; 1.3.5.1; 5301.
Reactome; R-RNO-71403; Citric acid cycle (TCA cycle).
SABIO-RK; Q920L2; -.
UniPathway; UPA00223; UER01006.
PRO; PR:Q920L2; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000013331; -.
Genevisible; Q920L2; RN.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:Ensembl.
GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IMP:RGD.
GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
GO; GO:0007399; P:nervous system development; IEA:Ensembl.
GO; GO:0022904; P:respiratory electron transport chain; IMP:RGD.
GO; GO:0006105; P:succinate metabolic process; IMP:RGD.
GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
Gene3D; 3.50.50.60; -; 2.
Gene3D; 3.90.700.10; -; 1.
InterPro; IPR003953; FAD-binding_2.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR003952; FRD_SDH_FAD_BS.
InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
InterPro; IPR011281; Succ_DH_flav_su_fwd.
InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
Pfam; PF00890; FAD_binding_2; 1.
Pfam; PF02910; Succ_DH_flav_C; 1.
SUPFAM; SSF46977; SSF46977; 1.
SUPFAM; SSF51905; SSF51905; 2.
SUPFAM; SSF56425; SSF56425; 1.
TIGRFAMs; TIGR01816; sdhA_forward; 1.
TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing;
Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
Reference proteome; Transit peptide; Transport;
Tricarboxylic acid cycle; Tumor suppressor.
TRANSIT 1 34 Mitochondrion.
{ECO:0000250|UniProtKB:Q0QF01}.
CHAIN 35 656 Succinate dehydrogenase [ubiquinone]
flavoprotein subunit, mitochondrial.
/FTId=PRO_0000010338.
NP_BIND 60 65 FAD. {ECO:0000250|UniProtKB:Q0QF01}.
NP_BIND 83 98 FAD. {ECO:0000250|UniProtKB:Q0QF01}.
NP_BIND 448 449 FAD. {ECO:0000250|UniProtKB:Q0QF01}.
ACT_SITE 332 332 Proton acceptor.
{ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 267 267 FAD. {ECO:0000250|UniProtKB:Q0QF01}.
BINDING 288 288 Substrate.
{ECO:0000250|UniProtKB:Q0QF01}.
BINDING 300 300 Substrate.
{ECO:0000250|UniProtKB:Q0QF01}.
BINDING 399 399 Substrate.
{ECO:0000250|UniProtKB:Q0QF01}.
BINDING 432 432 FAD. {ECO:0000250|UniProtKB:Q0QF01}.
BINDING 443 443 Substrate.
{ECO:0000250|UniProtKB:Q0QF01}.
MOD_RES 91 91 Tele-8alpha-FAD histidine.
{ECO:0000250|UniProtKB:Q0QF01}.
MOD_RES 171 171 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P31040}.
MOD_RES 171 171 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 174 174 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 207 207 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P31040}.
MOD_RES 242 242 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 242 242 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 327 327 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P31040}.
MOD_RES 327 327 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 415 415 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 472 472 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 477 477 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 477 477 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 490 490 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 490 490 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 509 509 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 530 530 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 530 530 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 542 542 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 590 590 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 600 600 N6-acetyllysine.
{ECO:0000250|UniProtKB:P31040}.
MOD_RES 607 607 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 616 616 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 625 625 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 628 628 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 639 639 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
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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