SDHA_PIG
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 03-AUG-2022, entry version 89.
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};
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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 PRIDE; Q0QF01; -.
DR Ensembl; ENSSSCT00000031591; ENSSSCP00000026945; ENSSSCG00000020686.
DR Ensembl; ENSSSCT00015035859; ENSSSCP00015014270; ENSSSCG00015026639.
DR Ensembl; ENSSSCT00025042442; ENSSSCP00025018064; ENSSSCG00025031010.
DR Ensembl; ENSSSCT00030061501; ENSSSCP00030028123; ENSSSCG00030043981.
DR Ensembl; ENSSSCT00035020617; ENSSSCP00035007412; ENSSSCG00035016133.
DR Ensembl; ENSSSCT00040063165; ENSSSCP00040026647; ENSSSCG00040044535.
DR Ensembl; ENSSSCT00045051093; ENSSSCP00045035533; ENSSSCG00045028783.
DR Ensembl; ENSSSCT00050066913; ENSSSCP00050028731; ENSSSCG00050049167.
DR Ensembl; ENSSSCT00055029043; ENSSSCP00055023128; ENSSSCG00055014552.
DR Ensembl; ENSSSCT00060007021; ENSSSCP00060002482; ENSSSCG00060005542.
DR GeneTree; ENSGT00910000144277; -.
DR InParanoid; Q0QF01; -.
DR OMA; DPIPIQP; -.
DR UniPathway; UPA00223; UER01006.
DR EvolutionaryTrace; Q0QF01; -.
DR Proteomes; UP000008227; Chromosome 16.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000020686; Expressed in psoas major muscle and 43 other 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:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
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; 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; -; 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 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
