CYSKM_ARATH
ID CYSKM_ARATH Reviewed; 430 AA.
AC Q43725; Q8L4A2; Q9M1Z8; Q9M440;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cysteine synthase, mitochondrial;
DE EC=2.5.1.47;
DE AltName: Full=Beta-substituted Ala synthase 2;2;
DE Short=ARAth-Bsas2;2;
DE AltName: Full=CSase C;
DE Short=AtCS-C;
DE Short=CS-C;
DE AltName: Full=O-acetylserine (thiol)-lyase;
DE AltName: Full=O-acetylserine sulfhydrylase;
DE AltName: Full=OAS-TL C;
DE Flags: Precursor;
GN Name=OASC; Synonyms=ACS 1; OrderedLocusNames=At3g59760; ORFNames=F24G16.30;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Flower;
RX PubMed=10319184; DOI=10.1007/bf01321531;
RA Hesse H., Lipke J., Altmann T., Hofgen R.;
RT "Molecular cloning and expression analyses of mitochondrial and plastidic
RT isoforms of cysteine synthase (O-acetylserine(thiol)lyase) from Arabidopsis
RT thaliana.";
RL Amino Acids 16:113-131(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 43-430, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INTERACTION WITH SAT3.
RC STRAIN=cv. Columbia;
RX PubMed=10940562; DOI=10.1016/s0378-1119(00)00261-4;
RA Jost R., Berkowitz O., Wirtz M., Hopkins L., Hawkesford M.J., Hell R.;
RT "Genomic and functional characterization of the oas gene family encoding O-
RT acetylserine (thiol) lyases, enzymes catalyzing the final step in cysteine
RT biosynthesis in Arabidopsis thaliana.";
RL Gene 253:237-247(2000).
RN [6]
RP NOMENCLATURE.
RX PubMed=10889265; DOI=10.1104/pp.123.3.1163;
RA Hatzfeld Y., Maruyama A., Schmidt A., Noji M., Ishizawa K., Saito K.;
RT "beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like
RT protein in spinach and Arabidopsis.";
RL Plant Physiol. 123:1163-1171(2000).
RN [7]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15258168; DOI=10.1093/jxb/erh201;
RA Wirtz M., Droux M., Hell R.;
RT "O-acetylserine (thiol) lyase: an enigmatic enzyme of plant cysteine
RT biosynthesis revisited in Arabidopsis thaliana.";
RL J. Exp. Bot. 55:1785-1798(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [9]
RP REVIEW.
RX PubMed=16307301; DOI=10.1007/s11120-005-8810-9;
RA Wirtz M., Droux M.;
RT "Synthesis of the sulfur amino acids: cysteine and methionine.";
RL Photosyn. Res. 86:345-362(2005).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18223034; DOI=10.1105/tpc.107.056747;
RA Heeg C., Kruse C., Jost R., Gutensohn M., Ruppert T., Wirtz M., Hell R.;
RT "Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family
RT demonstrates compartment-specific differences in the regulation of cysteine
RT synthesis.";
RL Plant Cell 20:168-185(2008).
RN [11]
RP GENE FAMILY, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18024555; DOI=10.1104/pp.107.106831;
RA Watanabe M., Kusano M., Oikawa A., Fukushima A., Noji M., Saito K.;
RT "Physiological roles of the beta-substituted alanine synthase gene family
RT in Arabidopsis.";
RL Plant Physiol. 146:310-320(2008).
RN [12]
RP COMPONENT OF THE CYSTEINE SYNTHASE COMPLEX.
RX PubMed=18801369; DOI=10.1016/j.jmb.2008.08.075;
RA Feldman-Salit A., Wirtz M., Hell R., Wade R.C.;
RT "A mechanistic model of the cysteine synthase complex.";
RL J. Mol. Biol. 386:37-59(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20658158; DOI=10.1007/s00726-010-0694-0;
RA Wirtz M., Heeg C., Samami A.A., Ruppert T., Hell R.;
RT "Enzymes of cysteine synthesis show extensive and conserved modifications
RT patterns that include N(alpha)-terminal acetylation.";
RL Amino Acids 39:1077-1086(2010).
RN [14]
RP COMPONENT OF THE CYSTEINE SYNTHASE COMPLEX.
RX PubMed=20720017; DOI=10.1074/jbc.m110.157446;
RA Wirtz M., Birke H., Heeg C., Mueller C., Hosp F., Throm C., Koenig S.,
RA Feldman-Salit A., Rippe K., Petersen G., Wade R.C., Rybin V., Scheffzek K.,
RA Hell R.;
RT "Structure and function of the hetero-oligomeric cysteine synthase complex
RT in plants.";
RL J. Biol. Chem. 285:32810-32817(2010).
RN [15]
RP INTERACTION WITH SAT3, AND COMPONENT OF THE CYSTEINE SYNTHASE COMPLEX.
RX PubMed=22730323; DOI=10.1074/jbc.m112.372656;
RA Wirtz M., Beard K.F., Lee C.P., Boltz A., Schwarzlaender M., Fuchs C.,
RA Meyer A.J., Heeg C., Sweetlove L.J., Ratcliffe R.G., Hell R.;
RT "Mitochondrial cysteine synthase complex regulates O-acetylserine
RT biosynthesis in plants.";
RL J. Biol. Chem. 287:27941-27947(2012).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22511607; DOI=10.1093/mp/sss043;
RA Alvarez C., Garcia I., Romero L.C., Gotor C.;
RT "Mitochondrial sulfide detoxification requires a functional isoform O-
RT acetylserine(thiol)lyase C in Arabidopsis thaliana.";
RL Mol. Plant 5:1217-1226(2012).
RN [17]
RP INTERACTION WITH SAT3.
RX PubMed=23602110; DOI=10.1016/j.plantsci.2013.02.016;
RA Wawrzynska A., Kurzyk A., Mierzwinska M., Plochocka D., Wieczorek G.,
RA Sirko A.;
RT "Direct targeting of Arabidopsis cysteine synthase complexes with synthetic
RT polypeptides to selectively deregulate cysteine synthesis.";
RL Plant Sci. 207:148-157(2013).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-87.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Acts as a cysteine synthase. Plays a role in the sulfide
CC detoxification in mitochondria. {ECO:0000269|PubMed:18024555,
CC ECO:0000269|PubMed:18223034, ECO:0000269|PubMed:22511607}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC Evidence={ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.98 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
CC KM=0.43 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
CC KM=4.7 uM for H(2)S for the cysteine synthase activity
CC {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
CC Vmax=159 umol/min/mg enzyme for L-cysteine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
CC Vmax=534 umol/min/mg enzyme for L-cysteine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
CC Vmax=0.33 umol/min/mg enzyme for H(2)S for the L-3-cyanoalanine
CC synthase activity {ECO:0000269|PubMed:10940562,
CC ECO:0000269|PubMed:15258168};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with SAT3. Component of
CC the cysteine synthase complex (CSC) composed of two OAS-TL dimers and
CC one SAT hexamer. {ECO:0000250, ECO:0000269|PubMed:10940562,
CC ECO:0000269|PubMed:22730323, ECO:0000269|PubMed:23602110}.
CC -!- INTERACTION:
CC Q43725; Q43725: OASC; NbExp=3; IntAct=EBI-1633616, EBI-1633616;
CC Q43725; Q39218: SAT3; NbExp=6; IntAct=EBI-1633616, EBI-1633440;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022,
CC ECO:0000305|PubMed:25732537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q43725-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype but displays lower levels of
CC thiols in roots (PubMed:18024555). Growth retardation
CC (PubMed:18223034). Defects in root hair formation (PubMed:22511607).
CC {ECO:0000269|PubMed:18024555, ECO:0000269|PubMed:18223034,
CC ECO:0000269|PubMed:22511607}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA57498.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB75795.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X81973; CAA57498.1; ALT_FRAME; mRNA.
DR EMBL; AL138647; CAB75795.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79963.1; -; Genomic_DNA.
DR EMBL; AY099721; AAM20572.1; -; mRNA.
DR EMBL; AY128885; AAM91285.1; -; mRNA.
DR EMBL; AJ271727; CAB71290.1; -; mRNA.
DR PIR; T47800; T47800.
DR PIR; T52650; T52650.
DR RefSeq; NP_191535.2; NM_115838.6. [Q43725-1]
DR PDB; 4AEC; X-ray; 2.40 A; A/B=1-430.
DR PDBsum; 4AEC; -.
DR AlphaFoldDB; Q43725; -.
DR SMR; Q43725; -.
DR BioGRID; 10459; 6.
DR DIP; DIP-40500N; -.
DR IntAct; Q43725; 3.
DR STRING; 3702.AT3G59760.1; -.
DR SwissPalm; Q43725; -.
DR PaxDb; Q43725; -.
DR PRIDE; Q43725; -.
DR ProteomicsDB; 222774; -. [Q43725-1]
DR EnsemblPlants; AT3G59760.3; AT3G59760.3; AT3G59760. [Q43725-1]
DR GeneID; 825145; -.
DR Gramene; AT3G59760.3; AT3G59760.3; AT3G59760. [Q43725-1]
DR KEGG; ath:AT3G59760; -.
DR Araport; AT3G59760; -.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_1_1_1; -.
DR InParanoid; Q43725; -.
DR OMA; RTPVFKF; -.
DR PhylomeDB; Q43725; -.
DR BioCyc; MetaCyc:AT3G59760-MON; -.
DR BRENDA; 2.5.1.47; 399.
DR UniPathway; UPA00136; UER00200.
DR PRO; PR:Q43725; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q43725; baseline and differential.
DR Genevisible; Q43725; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IBA:GO_Central.
DR GO; GO:0009860; P:pollen tube growth; IBA:GO_Central.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR005856; Cys_synth.
DR InterPro; IPR005859; CysK.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01139; cysK; 1.
DR TIGRFAMs; TIGR01136; cysKM; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amino-acid biosynthesis;
KW Cysteine biosynthesis; Mitochondrion; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..87
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 88..430
FT /note="Cysteine synthase, mitochondrial"
FT /id="PRO_0000006353"
FT BINDING 185
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 289..293
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 154
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 49
FT /note="Missing (in Ref. 1; CAA57498 and 5; CAB71290)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="A -> G (in Ref. 1; CAA57498)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="Missing (in Ref. 1; CAA57498)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="E -> R (in Ref. 1; CAA57498)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..357
FT /note="SE -> ISKL (in Ref. 1; CAA57498)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="Missing (in Ref. 1; CAA57498)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="Missing (in Ref. 1; CAA57498)"
FT /evidence="ECO:0000305"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:4AEC"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4AEC"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:4AEC"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:4AEC"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:4AEC"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:4AEC"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:4AEC"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:4AEC"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 269..276
FT /evidence="ECO:0007829|PDB:4AEC"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:4AEC"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 292..304
FT /evidence="ECO:0007829|PDB:4AEC"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4AEC"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:4AEC"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 356..370
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:4AEC"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:4AEC"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:4AEC"
SQ SEQUENCE 430 AA; 45815 MW; 9DDEB1B8E314E143 CRC64;
MVAMIMASRF NREAKLASQI LSTLLGNRSC YTSMAATSSS ALLLNPLTSS SSSSTLRRFR
CSPEISSLSF SSASDFSLAM KRQSRSFADG SERDPSVVCE AVKRETGPDG LNIADNVSQL
IGKTPMVYLN SIAKGCVANI AAKLEIMEPC CSVKDRIGYS MVTDAEQKGF ISPGKSVLVE
PTSGNTGIGL AFIAASRGYR LILTMPASMS MERRVLLKAF GAELVLTDPA KGMTGAVQKA
EEILKNTPDA YMLQQFDNPA NPKIHYETTG PEIWDDTKGK VDIFVAGIGT GGTITGVGRF
IKEKNPKTQV IGVEPTESDI LSGGKPGPHK IQGIGAGFIP KNLDQKIMDE VIAISSEEAI
ETAKQLALKE GLMVGISSGA AAAAAIKVAK RPENAGKLIA VVFPSFGERY LSTPLFQSIR
EEVEKMQPEV
