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

 SDHA_PIG                Reviewed;         664 AA.
Q0QF01; A0SNV1;
02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
02-MAR-2010, sequence version 2.
10-OCT-2018, entry version 74.
RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
EC=1.3.5.1 {ECO:0000305|PubMed:15989954};
AltName: Full=Flavoprotein subunit of complex II;
Short=Fp;
Flags: Precursor;
Name=SDHA;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-47, SUBUNIT, AND
SUBCELLULAR LOCATION.
TISSUE=Heart;
PubMed=17480203; DOI=10.1111/j.1742-4658.2007.05698.x;
Huo X., Su D., Wang A., Zhai Y., Xu J., Li X., Bartlam M., Sun F.,
Rao Z.;
"Preliminary molecular characterization and crystallization of
mitochondrial respiratory complex II from porcine heart.";
FEBS J. 274:1524-1529(2007).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 59-599.
TISSUE=Liver;
PubMed=16751257; DOI=10.1093/molbev/msl027;
Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
"Housekeeping genes for phylogenetic analysis of eutherian
relationships.";
Mol. Biol. Evol. 23:1493-1503(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 165-663.
PubMed=17697375; DOI=10.1186/1471-2199-8-67;
Nygard A.B., Jorgensen C.B., Cirera S., Fredholm M.;
"Selection of reference genes for gene expression studies in pig
tissues using SYBR green qPCR.";
BMC Mol. Biol. 8:67-67(2007).
[4]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND
SUBSTRATE ANALOG 3-NITROPROPIONATE, FUNCTION, CATALYTIC ACTIVITY,
PATHWAY, COFACTOR, AND SUBUNIT.
PubMed=15989954; DOI=10.1016/j.cell.2005.05.025;
Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., Bartlam M., Rao Z.;
"Crystal structure of mitochondrial respiratory membrane protein
complex II.";
Cell 121:1043-1057(2005).
-!- 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) (Probable). Can act as a
tumor suppressor (By similarity). {ECO:0000250|UniProtKB:P31040,
ECO:0000305|PubMed:15989954}.
-!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
{ECO:0000305|PubMed:15989954}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:15989954};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
fumarate from succinate (eukaryal route): step 1/1.
{ECO:0000305|PubMed:15989954}.
-!- 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 (PubMed:15989954,
PubMed:17480203). Interacts with SDHAF2/SDH5; interaction is
required for FAD attachment (By similarity). Interacts with TRAP1
(By similarity). {ECO:0000250|UniProtKB:P31040,
ECO:0000269|PubMed:15989954, ECO:0000269|PubMed:17480203}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:17480203}; Peripheral membrane protein
{ECO:0000269|PubMed:17480203}; Matrix side
{ECO:0000269|PubMed:17480203}.
-!- PTM: Phosphorylation at Tyr-215 is important for efficient
electron transfer in complex II and the prevention of ROS
generation. {ECO:0000250|UniProtKB:P31040}.
-!- PTM: Acetylated. Deacetylated by SIRT3.
{ECO:0000250|UniProtKB:Q8K2B3}.
-!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
FRD/SDH subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABI29191.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; DQ402993; ABD77326.1; -; mRNA.
EMBL; DQ845177; ABI29191.1; ALT_INIT; mRNA.
UniGene; Ssc.24988; -.
PDB; 1ZOY; X-ray; 2.40 A; A=43-664.
PDB; 1ZP0; X-ray; 3.50 A; A=43-664.
PDB; 3ABV; X-ray; 3.24 A; A=43-664.
PDB; 3AE1; X-ray; 3.14 A; A=43-664.
PDB; 3AE2; X-ray; 3.10 A; A=43-664.
PDB; 3AE3; X-ray; 3.35 A; A=43-664.
PDB; 3AE4; X-ray; 2.91 A; A=43-664.
PDB; 3AE5; X-ray; 3.41 A; A=43-664.
PDB; 3AE6; X-ray; 3.40 A; A=43-664.
PDB; 3AE7; X-ray; 3.62 A; A=43-664.
PDB; 3AE8; X-ray; 3.40 A; A=43-664.
PDB; 3AE9; X-ray; 3.31 A; A=43-664.
PDB; 3AEA; X-ray; 3.39 A; A=43-664.
PDB; 3AEB; X-ray; 3.00 A; A=43-664.
PDB; 3AEC; X-ray; 3.61 A; A=43-664.
PDB; 3AED; X-ray; 3.52 A; A=43-664.
PDB; 3AEE; X-ray; 3.22 A; A=43-664.
PDB; 3AEF; X-ray; 2.80 A; A=43-664.
PDB; 3AEG; X-ray; 3.27 A; A=43-664.
PDB; 3SFD; X-ray; 2.61 A; A=43-664.
PDB; 3SFE; X-ray; 2.81 A; A=43-664.
PDB; 4YTP; X-ray; 3.10 A; A=1-664.
PDB; 4YXD; X-ray; 3.00 A; A=1-664.
PDBsum; 1ZOY; -.
PDBsum; 1ZP0; -.
PDBsum; 3ABV; -.
PDBsum; 3AE1; -.
PDBsum; 3AE2; -.
PDBsum; 3AE3; -.
PDBsum; 3AE4; -.
PDBsum; 3AE5; -.
PDBsum; 3AE6; -.
PDBsum; 3AE7; -.
PDBsum; 3AE8; -.
PDBsum; 3AE9; -.
PDBsum; 3AEA; -.
PDBsum; 3AEB; -.
PDBsum; 3AEC; -.
PDBsum; 3AED; -.
PDBsum; 3AEE; -.
PDBsum; 3AEF; -.
PDBsum; 3AEG; -.
PDBsum; 3SFD; -.
PDBsum; 3SFE; -.
PDBsum; 4YTP; -.
PDBsum; 4YXD; -.
ProteinModelPortal; Q0QF01; -.
SMR; Q0QF01; -.
PeptideAtlas; Q0QF01; -.
PRIDE; Q0QF01; -.
Ensembl; ENSSSCT00000031591; ENSSSCP00000026945; ENSSSCG00000020686.
GeneTree; ENSGT00910000144277; -.
HOVERGEN; HBG001461; -.
InParanoid; Q0QF01; -.
Reactome; R-SSC-71403; Citric acid cycle (TCA cycle).
UniPathway; UPA00223; UER01006.
EvolutionaryTrace; Q0QF01; -.
Proteomes; UP000008227; Chromosome 16.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA: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; ISS:UniProtKB.
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:0055114; P:oxidation-reduction process; IC:UniProtKB.
GO; GO:0022904; P:respiratory electron transport chain; IC:UniProtKB.
GO; GO:0006105; P:succinate metabolic process; IEA:Ensembl.
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;
3D-structure; 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 42 Mitochondrion.
{ECO:0000269|PubMed:17480203}.
CHAIN 43 664 Succinate dehydrogenase [ubiquinone]
flavoprotein subunit, mitochondrial.
/FTId=PRO_0000391718.
NP_BIND 68 73 FAD. {ECO:0000269|PubMed:15989954}.
NP_BIND 91 106 FAD. {ECO:0000269|PubMed:15989954}.
NP_BIND 456 457 FAD. {ECO:0000269|PubMed:15989954}.
ACT_SITE 340 340 Proton acceptor.
{ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 275 275 FAD. {ECO:0000269|PubMed:15989954}.
BINDING 296 296 Substrate. {ECO:0000269|PubMed:15989954}.
BINDING 308 308 Substrate. {ECO:0000269|PubMed:15989954}.
BINDING 407 407 Substrate. {ECO:0000269|PubMed:15989954}.
BINDING 440 440 FAD. {ECO:0000269|PubMed:15989954}.
BINDING 451 451 Substrate. {ECO:0000269|PubMed:15989954}.
MOD_RES 99 99 Tele-8alpha-FAD histidine.
{ECO:0000269|PubMed:15989954}.
MOD_RES 167 167 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 179 179 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P31040}.
MOD_RES 179 179 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 182 182 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 215 215 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P31040}.
MOD_RES 335 335 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P31040}.
MOD_RES 335 335 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 480 480 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 485 485 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 485 485 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 498 498 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 498 498 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 517 517 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 538 538 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 538 538 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 550 550 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 598 598 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 608 608 N6-acetyllysine.
{ECO:0000250|UniProtKB:P31040}.
MOD_RES 615 615 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 624 624 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 633 633 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 636 636 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
MOD_RES 647 647 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K2B3}.
CONFLICT 165 171 DGKIYQR -> LQESARG (in Ref. 3; ABI29191).
{ECO:0000305}.
CONFLICT 222 222 L -> S (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 235 235 I -> T (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 358 358 G -> N (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 453 453 G -> E (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 509 509 S -> W (in Ref. 2; ABD77326).
{ECO:0000305}.
CONFLICT 566 566 L -> P (in Ref. 2; ABD77326).
{ECO:0000305}.
STRAND 57 61 {ECO:0000244|PDB:1ZOY}.
STRAND 63 67 {ECO:0000244|PDB:1ZOY}.
HELIX 71 82 {ECO:0000244|PDB:1ZOY}.
STRAND 87 93 {ECO:0000244|PDB:1ZOY}.
HELIX 95 97 {ECO:0000244|PDB:1ZOY}.
HELIX 99 102 {ECO:0000244|PDB:1ZOY}.
STRAND 113 115 {ECO:0000244|PDB:1ZOY}.
HELIX 119 129 {ECO:0000244|PDB:1ZOY}.
TURN 130 132 {ECO:0000244|PDB:1ZOY}.
HELIX 136 156 {ECO:0000244|PDB:1ZOY}.
STRAND 166 168 {ECO:0000244|PDB:1ZOY}.
STRAND 170 178 {ECO:0000244|PDB:1ZOY}.
TURN 179 182 {ECO:0000244|PDB:1ZOY}.
STRAND 185 190 {ECO:0000244|PDB:1ZOY}.
HELIX 196 208 {ECO:0000244|PDB:1ZOY}.
TURN 209 212 {ECO:0000244|PDB:4YXD}.
STRAND 214 217 {ECO:0000244|PDB:1ZOY}.
STRAND 219 227 {ECO:0000244|PDB:1ZOY}.
STRAND 230 238 {ECO:0000244|PDB:1ZOY}.
TURN 239 241 {ECO:0000244|PDB:1ZOY}.
STRAND 244 248 {ECO:0000244|PDB:1ZOY}.
STRAND 250 254 {ECO:0000244|PDB:1ZOY}.
HELIX 260 262 {ECO:0000244|PDB:1ZOY}.
STRAND 263 268 {ECO:0000244|PDB:1ZOY}.
HELIX 275 282 {ECO:0000244|PDB:1ZOY}.
TURN 289 291 {ECO:0000244|PDB:4YXD}.
STRAND 293 297 {ECO:0000244|PDB:1ZOY}.
TURN 301 303 {ECO:0000244|PDB:1ZOY}.
HELIX 310 314 {ECO:0000244|PDB:1ZOY}.
STRAND 317 319 {ECO:0000244|PDB:1ZOY}.
STRAND 323 325 {ECO:0000244|PDB:3AE2}.
TURN 327 329 {ECO:0000244|PDB:3SFD}.
TURN 332 336 {ECO:0000244|PDB:1ZOY}.
HELIX 340 353 {ECO:0000244|PDB:1ZOY}.
STRAND 357 361 {ECO:0000244|PDB:3SFD}.
STRAND 365 367 {ECO:0000244|PDB:1ZOY}.
STRAND 369 371 {ECO:0000244|PDB:3AE1}.
HELIX 375 378 {ECO:0000244|PDB:1ZOY}.
HELIX 381 391 {ECO:0000244|PDB:1ZOY}.
TURN 395 397 {ECO:0000244|PDB:1ZOY}.
STRAND 400 402 {ECO:0000244|PDB:4YXD}.
STRAND 405 409 {ECO:0000244|PDB:1ZOY}.
STRAND 412 415 {ECO:0000244|PDB:1ZOY}.
STRAND 419 425 {ECO:0000244|PDB:1ZOY}.
STRAND 428 437 {ECO:0000244|PDB:1ZOY}.
HELIX 439 441 {ECO:0000244|PDB:3AEF}.
STRAND 442 444 {ECO:0000244|PDB:3SFD}.
HELIX 456 474 {ECO:0000244|PDB:1ZOY}.
TURN 486 489 {ECO:0000244|PDB:1ZOY}.
HELIX 490 500 {ECO:0000244|PDB:1ZOY}.
STRAND 505 507 {ECO:0000244|PDB:1ZOY}.
HELIX 508 522 {ECO:0000244|PDB:1ZOY}.
STRAND 523 527 {ECO:0000244|PDB:1ZOY}.
HELIX 529 545 {ECO:0000244|PDB:1ZOY}.
STRAND 548 550 {ECO:0000244|PDB:1ZOY}.
HELIX 560 584 {ECO:0000244|PDB:1ZOY}.
STRAND 587 589 {ECO:0000244|PDB:3AE6}.
STRAND 594 596 {ECO:0000244|PDB:1ZOY}.
STRAND 606 608 {ECO:0000244|PDB:1ZOY}.
STRAND 610 613 {ECO:0000244|PDB:1ZOY}.
HELIX 618 620 {ECO:0000244|PDB:1ZOY}.
STRAND 624 630 {ECO:0000244|PDB:1ZOY}.
TURN 632 634 {ECO:0000244|PDB:1ZOY}.
STRAND 637 642 {ECO:0000244|PDB:1ZOY}.
TURN 651 653 {ECO:0000244|PDB:1ZOY}.
SEQUENCE 664 AA; 72832 MW; 0120E14F7F6F60EE CRC64;
MSGVRAVSRL LRARRLALTW AQPAASPIGA RSFHFTVDGN KRSSAKVSDA ISTQYPVVDH
EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT VAAQGGINAA LGNMEEDNWR
WHFYDTVKGS DWLGDQDAIH YMTEQAPASV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF
GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE
DGSIHRIRAR NTVVATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI
YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE
KDHVYLQLHH LPPEQLAVRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ
VLRHVNGQDQ VVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IAESCRPGDK
VPSIKPNAGE ESVMNLDKLR FANGTIRTSE LRLSMQKSMQ SHAAVFRVGS VLQEGCEKIL
RLYGDLQHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDFKER
VDEYDYSKPI QGQQKKPFQE HWRKHTLSYV DVKTGKVSLE YRPVIDKTLN EADCATVPPA
IRSY


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