ID SDHA_PIG Reviewed; 664 AA. AC Q0QF01; A0SNV1; DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 02-MAR-2010, sequence version 2. DT 27-MAR-2024, entry version 97. DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial; DE EC=1.3.5.1 {ECO:0000305|PubMed:15989954}; DE AltName: Full=Flavoprotein subunit of complex II; DE Short=Fp; DE Flags: Precursor; GN Name=SDHA; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-47, SUBUNIT, AND RP SUBCELLULAR LOCATION. RC TISSUE=Heart; RX PubMed=17480203; DOI=10.1111/j.1742-4658.2007.05698.x; RA Huo X., Su D., Wang A., Zhai Y., Xu J., Li X., Bartlam M., Sun F., Rao Z.; RT "Preliminary molecular characterization and crystallization of RT mitochondrial respiratory complex II from porcine heart."; RL FEBS J. 274:1524-1529(2007). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-599. RC TISSUE=Liver; RX PubMed=16751257; DOI=10.1093/molbev/msl027; RA Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.; RT "Housekeeping genes for phylogenetic analysis of eutherian relationships."; RL Mol. Biol. Evol. 23:1493-1503(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 165-663. RX PubMed=17697375; DOI=10.1186/1471-2199-8-67; RA Nygard A.B., Jorgensen C.B., Cirera S., Fredholm M.; RT "Selection of reference genes for gene expression studies in pig tissues RT using SYBR green qPCR."; RL BMC Mol. Biol. 8:67-67(2007). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND SUBSTRATE RP ANALOG 3-NITROPROPIONATE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, RP AND SUBUNIT. RX PubMed=15989954; DOI=10.1016/j.cell.2005.05.025; RA Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., Bartlam M., Rao Z.; RT "Crystal structure of mitochondrial respiratory membrane protein complex RT II."; RL Cell 121:1043-1057(2005). 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) (Probable). Can act as a tumor suppressor (By CC similarity). {ECO:0000250|UniProtKB:P31040, CC ECO:0000305|PubMed:15989954}. 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:0000305|PubMed:15989954}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:15989954}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate CC from succinate (eukaryal route): step 1/1. CC {ECO:0000305|PubMed:15989954}. 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 (PubMed:15989954, PubMed:17480203). CC Interacts with SDHAF2/SDH5; interaction is required for FAD attachment CC (By similarity). Interacts with TRAP1 (By similarity). Interacts with CC LACC1 (By similarity). {ECO:0000250|UniProtKB:P31040, CC ECO:0000269|PubMed:15989954, ECO:0000269|PubMed:17480203}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:17480203}; Peripheral membrane protein CC {ECO:0000269|PubMed:17480203}; Matrix side CC {ECO:0000269|PubMed:17480203}. CC -!- PTM: Phosphorylation at Tyr-215 is important for efficient electron CC transfer in complex II and the prevention of ROS generation. CC {ECO:0000250|UniProtKB:P31040}. CC -!- PTM: Acetylated. Deacetylated by SIRT3. {ECO:0000250|UniProtKB:Q8K2B3}. CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC FRD/SDH subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ABI29191.1; Type=Erroneous initiation; Evidence={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; DQ402993; ABD77326.1; -; mRNA. DR EMBL; DQ845177; ABI29191.1; ALT_INIT; mRNA. DR PDB; 1ZOY; X-ray; 2.40 A; A=43-664. DR PDB; 1ZP0; X-ray; 3.50 A; A=43-664. DR PDB; 3ABV; X-ray; 3.24 A; A=43-664. DR PDB; 3AE1; X-ray; 3.14 A; A=43-664. DR PDB; 3AE2; X-ray; 3.10 A; A=43-664. DR PDB; 3AE3; X-ray; 3.35 A; A=43-664. DR PDB; 3AE4; X-ray; 2.91 A; A=43-664. DR PDB; 3AE5; X-ray; 3.41 A; A=43-664. DR PDB; 3AE6; X-ray; 3.40 A; A=43-664. DR PDB; 3AE7; X-ray; 3.62 A; A=43-664. DR PDB; 3AE8; X-ray; 3.40 A; A=43-664. DR PDB; 3AE9; X-ray; 3.31 A; A=43-664. DR PDB; 3AEA; X-ray; 3.39 A; A=43-664. DR PDB; 3AEB; X-ray; 3.00 A; A=43-664. DR PDB; 3AEC; X-ray; 3.61 A; A=43-664. DR PDB; 3AED; X-ray; 3.52 A; A=43-664. DR PDB; 3AEE; X-ray; 3.22 A; A=43-664. DR PDB; 3AEF; X-ray; 2.80 A; A=43-664. DR PDB; 3AEG; X-ray; 3.27 A; A=43-664. DR PDB; 3SFD; X-ray; 2.61 A; A=43-664. DR PDB; 3SFE; X-ray; 2.81 A; A=43-664. DR PDB; 4YTP; X-ray; 3.10 A; A=1-664. DR PDB; 4YXD; X-ray; 3.00 A; A=1-664. DR PDBsum; 1ZOY; -. DR PDBsum; 1ZP0; -. DR PDBsum; 3ABV; -. DR PDBsum; 3AE1; -. DR PDBsum; 3AE2; -. DR PDBsum; 3AE3; -. DR PDBsum; 3AE4; -. DR PDBsum; 3AE5; -. DR PDBsum; 3AE6; -. DR PDBsum; 3AE7; -. DR PDBsum; 3AE8; -. DR PDBsum; 3AE9; -. DR PDBsum; 3AEA; -. DR PDBsum; 3AEB; -. DR PDBsum; 3AEC; -. DR PDBsum; 3AED; -. DR PDBsum; 3AEE; -. DR PDBsum; 3AEF; -. DR PDBsum; 3AEG; -. DR PDBsum; 3SFD; -. DR PDBsum; 3SFE; -. DR PDBsum; 4YTP; -. DR PDBsum; 4YXD; -. DR AlphaFoldDB; Q0QF01; -. DR SMR; Q0QF01; -. DR STRING; 9823.ENSSSCP00000026945; -. DR PeptideAtlas; Q0QF01; -. DR Ensembl; ENSSSCT00000031591.3; ENSSSCP00000026945.2; ENSSSCG00000020686.4. DR Ensembl; ENSSSCT00015035859.1; ENSSSCP00015014270.1; ENSSSCG00015026639.1. DR Ensembl; ENSSSCT00025042442.1; ENSSSCP00025018064.1; ENSSSCG00025031010.1. DR Ensembl; ENSSSCT00030061501.1; ENSSSCP00030028123.1; ENSSSCG00030043981.1. DR Ensembl; ENSSSCT00035020617.1; ENSSSCP00035007412.1; ENSSSCG00035016133.1. DR Ensembl; ENSSSCT00040063165.1; ENSSSCP00040026647.1; ENSSSCG00040044535.1. DR Ensembl; ENSSSCT00045051093.1; ENSSSCP00045035533.1; ENSSSCG00045028783.1. DR Ensembl; ENSSSCT00050066913.1; ENSSSCP00050028731.1; ENSSSCG00050049167.1. DR Ensembl; ENSSSCT00055029043.1; ENSSSCP00055023128.1; ENSSSCG00055014552.1. DR Ensembl; ENSSSCT00060007021.1; ENSSSCP00060002482.1; ENSSSCG00060005542.1. DR VGNC; VGNC:110673; SDHA. DR GeneTree; ENSGT00910000144277; -. DR InParanoid; Q0QF01; -. DR OMA; FHPTGIW; -. DR Reactome; R-SSC-71403; Citric acid cycle (TCA cycle). DR UniPathway; UPA00223; UER01006. DR EvolutionaryTrace; Q0QF01; -. DR Proteomes; UP000008227; Chromosome 16. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Bgee; ENSSSCG00000020686; Expressed in psoas major muscle and 43 other cell types or tissues. DR ExpressionAtlas; Q0QF01; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:UniProtKB. 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:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC. DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB. 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; IC:UniProtKB. DR GO; GO:0006105; P:succinate metabolic process; IEA:Ensembl. DR GO; GO:0006099; P:tricarboxylic acid cycle; IC:UniProtKB. 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. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Electron transport; KW FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide; KW Transport; Tricarboxylic acid cycle; Tumor suppressor. FT TRANSIT 1..42 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:17480203" FT CHAIN 43..664 FT /note="Succinate dehydrogenase [ubiquinone] flavoprotein FT subunit, mitochondrial" FT /id="PRO_0000391718" FT ACT_SITE 340 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9YHT1" FT BINDING 68..73 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15989954" FT BINDING 91..106 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15989954" FT BINDING 275 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15989954" FT BINDING 296 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15989954" FT BINDING 308 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15989954" FT BINDING 407 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15989954" FT BINDING 440 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15989954" FT BINDING 451 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15989954" FT BINDING 456..457 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15989954" FT MOD_RES 99 FT /note="Tele-8alpha-FAD histidine" FT /evidence="ECO:0000269|PubMed:15989954" FT MOD_RES 167 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 179 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 179 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 182 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 215 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 335 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 335 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 480 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 485 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 485 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 498 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 498 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 517 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 538 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 538 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 550 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 598 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 608 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P31040" FT MOD_RES 615 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 624 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 633 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 636 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT MOD_RES 647 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K2B3" FT CONFLICT 165..171 FT /note="DGKIYQR -> LQESARG (in Ref. 3; ABI29191)" FT /evidence="ECO:0000305" FT CONFLICT 222 FT /note="L -> S (in Ref. 1; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 235 FT /note="I -> T (in Ref. 1; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 358 FT /note="G -> N (in Ref. 1; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 453 FT /note="G -> E (in Ref. 1; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 509 FT /note="S -> W (in Ref. 2; ABD77326)" FT /evidence="ECO:0000305" FT CONFLICT 566 FT /note="L -> P (in Ref. 2; ABD77326)" FT /evidence="ECO:0000305" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 63..67 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 71..82 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 87..93 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 99..102 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 119..129 FT /evidence="ECO:0007829|PDB:1ZOY" FT TURN 130..132 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 136..156 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 170..178 FT /evidence="ECO:0007829|PDB:1ZOY" FT TURN 179..182 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 185..190 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 196..208 FT /evidence="ECO:0007829|PDB:1ZOY" FT TURN 209..212 FT /evidence="ECO:0007829|PDB:4YXD" FT STRAND 214..217 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 219..227 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 230..238 FT /evidence="ECO:0007829|PDB:1ZOY" FT TURN 239..241 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 250..254 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 260..262 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 275..282 FT /evidence="ECO:0007829|PDB:1ZOY" FT TURN 289..291 FT /evidence="ECO:0007829|PDB:4YXD" FT STRAND 293..297 FT /evidence="ECO:0007829|PDB:1ZOY" FT TURN 301..303 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 310..314 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 317..319 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:3AE2" FT TURN 327..329 FT /evidence="ECO:0007829|PDB:3SFD" FT TURN 332..336 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 340..353 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 357..361 FT /evidence="ECO:0007829|PDB:3SFD" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:3AE1" FT HELIX 375..378 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 381..391 FT /evidence="ECO:0007829|PDB:1ZOY" FT TURN 395..397 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 400..402 FT /evidence="ECO:0007829|PDB:4YXD" FT STRAND 405..409 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 412..415 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 419..425 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 428..437 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 439..441 FT /evidence="ECO:0007829|PDB:3AEF" FT STRAND 442..444 FT /evidence="ECO:0007829|PDB:3SFD" FT HELIX 456..474 FT /evidence="ECO:0007829|PDB:1ZOY" FT TURN 486..489 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 490..500 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 505..507 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 508..522 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 523..527 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 529..545 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 548..550 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 560..584 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 587..589 FT /evidence="ECO:0007829|PDB:3AE6" FT STRAND 594..596 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 606..608 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 610..613 FT /evidence="ECO:0007829|PDB:1ZOY" FT HELIX 618..620 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 624..630 FT /evidence="ECO:0007829|PDB:1ZOY" FT TURN 632..634 FT /evidence="ECO:0007829|PDB:1ZOY" FT STRAND 637..642 FT /evidence="ECO:0007829|PDB:1ZOY" FT TURN 651..653 FT /evidence="ECO:0007829|PDB:1ZOY" SQ 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 //