CDC25_ARATH
ID CDC25_ARATH Reviewed; 146 AA.
AC Q8GY31; Q8LC90; Q9LZE1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Dual specificity phosphatase Cdc25 {ECO:0000303|PubMed:15329414};
DE EC=3.1.3.48 {ECO:0000269|PubMed:15329414};
DE AltName: Full=Arath;CDC25 {ECO:0000303|PubMed:15329414};
DE AltName: Full=Arsenate reductase {ECO:0000303|PubMed:16507083};
DE Short=AtASR {ECO:0000303|PubMed:16507083};
DE AltName: Full=Arsenate reductase 2 {ECO:0000303|PubMed:16567632};
DE EC=1.20.4.1 {ECO:0000269|PubMed:16766666};
DE AltName: Full=Sulfurtransferase 5 {ECO:0000303|PubMed:17408957};
DE Short=AtStr5 {ECO:0000303|PubMed:17408957};
GN Name=CDC25 {ECO:0000303|PubMed:15329414};
GN Synonyms=ACR2 {ECO:0000303|PubMed:16567632},
GN ASR {ECO:0000303|PubMed:16507083}, STR5 {ECO:0000303|PubMed:17408957};
GN OrderedLocusNames=At5g03455 {ECO:0000312|Araport:AT5G03455};
GN ORFNames=F12E4_220 {ECO:0000312|EMBL:CAB83305.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15720653; DOI=10.1111/j.1469-8137.2004.01288.x;
RA Sorrell D.A., Chrimes D., Dickinson J.R., Rogers H.J., Francis D.;
RT "The Arabidopsis CDC25 induces a short cell length when overexpressed in
RT fission yeast: evidence for cell cycle function.";
RL New Phytol. 165:425-428(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16507083; DOI=10.1111/j.1365-313x.2005.02651.x;
RA Bleeker P.M., Hakvoort H.W., Bliek M., Souer E., Schat H.;
RT "Enhanced arsenate reduction by a CDC25-like tyrosine phosphatase explains
RT increased phytochelatin accumulation in arsenate-tolerant Holcus lanatus.";
RL Plant J. 45:917-929(2006).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16766666; DOI=10.1104/pp.106.084079;
RA Ellis D.R., Gumaelius L., Indriolo E., Pickering I.J., Banks J.A.,
RA Salt D.E.;
RT "A novel arsenate reductase from the arsenic hyperaccumulating fern Pteris
RT vittata.";
RL Plant Physiol. 141:1544-1554(2006).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16567632; DOI=10.1073/pnas.0509770102;
RA Dhankher O.P., Rosen B.P., McKinney E.C., Meagher R.B.;
RT "Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced for
RT arsenate reductase (ACR2).";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5413-5418(2006).
RN [10]
RP GENE FAMILY.
RX PubMed=17408957; DOI=10.1016/j.plaphy.2007.02.005;
RA Bartels A., Mock H.P., Papenbrock J.;
RT "Differential expression of Arabidopsis sulfurtransferases under various
RT growth conditions.";
RL Plant Physiol. Biochem. 45:178-187(2007).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=20647223; DOI=10.1093/aob/mcq142;
RA Spadafora N.D., Doonan J.H., Herbert R.J., Bitonti M.B., Wallace E.,
RA Rogers H.J., Francis D.;
RT "Arabidopsis T-DNA insertional lines for CDC25 are hypersensitive to
RT hydroxyurea but not to zeocin or salt stress.";
RL Ann. Bot. 107:1183-1192(2011).
RN [12]
RP 3D-STRUCTURE MODELING, AND FUNCTION.
RX PubMed=22562211; DOI=10.1007/s00894-012-1419-y;
RA Nahar N., Rahman A., Mos M., Warzecha T., Algerin M., Ghosh S.,
RA Johnson-Brousseau S., Mandal A.;
RT "In silico and in vivo studies of an Arabidopsis thaliana gene, ACR2,
RT putatively involved in arsenic accumulation in plants.";
RL J. Mol. Model. 18:4249-4262(2012).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=22879969; DOI=10.1371/journal.pone.0042408;
RA Liu W., Schat H., Bliek M., Chen Y., McGrath S.P., George G., Salt D.E.,
RA Zhao F.J.;
RT "Knocking out ACR2 does not affect arsenic redox status in Arabidopsis
RT thaliana: implications for as detoxification and accumulation in plants.";
RL PLoS ONE 7:E42408-E42408(2012).
RN [14]
RP DISRUPTION PHENOTYPE.
RX PubMed=25099865; DOI=10.1038/ncomms5617;
RA Sanchez-Bermejo E., Castrillo G., del Llano B., Navarro C.,
RA Zarco-Fernandez S., Martinez-Herrera D.J., Leo-del Puerto Y., Munoz R.,
RA Camara C., Paz-Ares J., Alonso-Blanco C., Leyva A.;
RT "Natural variation in arsenate tolerance identifies an arsenate reductase
RT in Arabidopsis thaliana.";
RL Nat. Commun. 5:4617-4617(2014).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25464340; DOI=10.1371/journal.pbio.1002009;
RA Chao D.Y., Chen Y., Chen J., Shi S., Chen Z., Wang C., Danku J.M.,
RA Zhao F.J., Salt D.E.;
RT "Genome-wide association mapping identifies a new arsenate reductase enzyme
RT critical for limiting arsenic accumulation in plants.";
RL PLoS Biol. 12:E1002009-E1002009(2014).
RN [16]
RP STRUCTURE BY NMR OF 15-146 OF CYS-145 IN COMPLEX WITH ZINC,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-145.
RX PubMed=15336525; DOI=10.1016/j.bbrc.2004.07.182;
RA Landrieu I., Hassan S., Sauty M., Dewitte F., Wieruszeski J.-M., Inze D.,
RA de Veylder L., Lippens G.;
RT "Characterization of the Arabidopsis thaliana Arath;CDC25 dual-specificity
RT tyrosine phosphatase.";
RL Biochem. Biophys. Res. Commun. 322:734-739(2004).
RN [17]
RP STRUCTURE BY NMR OF 15-146 OF CYS-86 MUTANT IN COMPLEX WITH ZINC, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF CYS-86.
RX PubMed=15329414; DOI=10.1073/pnas.0405248101;
RA Landrieu I., da Costa M., de Veylder L., Dewitte F., Vandepoele K.,
RA Hassan S., Wieruszeski J.-M., Corellou F., Faure J.-D., Van Montagu M.,
RA Inze D., Lippens G.;
RT "A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13380-13385(2004).
RN [18]
RP ERRATUM OF PUBMED:15329414.
RX DOI=10.1073/pnas.0407263101;
RA Landrieu I., da Costa M., de Veylder L., Dewitte F., Vandepoele K.,
RA Hassan S., Wieruszeski J.M., Corellou F., Faure J.D., Van Montagu M.,
RA Inze D., Lippens G.;
RL Proc. Natl. Acad. Sci. U.S.A. 101:16391-16391(2004).
CC -!- FUNCTION: Tyrosine protein phosphatase that dephosphorylates CDK
CC complex and activate its kinase activity in vitro.
CC {ECO:0000269|PubMed:15329414, ECO:0000269|PubMed:16766666}.
CC -!- FUNCTION: Arsenate reductase that plays a major role in the reduction
CC of arsenate to arsenite and arsenic retention in roots
CC (PubMed:16567632). Has an in vitro and in vivo arsenate reductase
CC activity (PubMed:16507083, PubMed:16766666, PubMed:22562211). Plays no
CC role in arsenic metabolism (PubMed:22879969, PubMed:25464340).
CC {ECO:0000269|PubMed:16507083, ECO:0000269|PubMed:16567632,
CC ECO:0000269|PubMed:16766666, ECO:0000269|PubMed:22879969,
CC ECO:0000269|PubMed:25464340}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:15329414};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[glutaredoxin]-dithiol + arsenate + glutathione + H(+) =
CC arsenite + glutathionyl-S-S-[glutaredoxin] + H2O;
CC Xref=Rhea:RHEA:22016, Rhea:RHEA-COMP:10729, Rhea:RHEA-COMP:17668,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29242,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:48597, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:146199; EC=1.20.4.1;
CC Evidence={ECO:0000269|PubMed:16766666};
CC -!- ACTIVITY REGULATION: Inhibited by NSC95397.
CC {ECO:0000269|PubMed:15329414}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 mM for para-nitrophenyl phosphate {ECO:0000269|PubMed:15329414,
CC ECO:0000269|PubMed:15336525};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and at lower levels in shoots
CC (at protein level). Expressed in leaves, stems and flowers.
CC {ECO:0000269|PubMed:15720653, ECO:0000269|PubMed:16567632,
CC ECO:0000269|PubMed:22879969}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but plants show reduced root size when grown in presence of
CC hydroxyurea (PubMed:20647223). No visible phenotype, but decreased
CC accumulation of total arsenic in shoots (PubMed:16507083). No effect on
CC arsenate sensitivity (PubMed:25099865). No effect on the accumulation
CC of arsenate in roots, efflux of arsenite or uptake of arsenate, or the
CC total arsenic accumulation in shoots (PubMed:22879969,
CC PubMed:25464340). {ECO:0000269|PubMed:16507083,
CC ECO:0000269|PubMed:20647223, ECO:0000269|PubMed:22879969,
CC ECO:0000269|PubMed:25099865, ECO:0000269|PubMed:25464340}.
CC -!- MISCELLANEOUS: Binds 1 zinc ion which is not required for enzyme
CC activity (PubMed:15329414). Plants silencing ACR2 show increased
CC sensitivity to arsenate but not arsenite (PubMed:16567632).
CC {ECO:0000305|PubMed:15329414, ECO:0000305|PubMed:16567632}.
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63780.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB83305.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162751; CAB83305.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90607.1; -; Genomic_DNA.
DR EMBL; AK117898; BAC42537.1; -; mRNA.
DR EMBL; BT003658; AAO39886.1; -; mRNA.
DR EMBL; AY086729; AAM63780.1; ALT_INIT; mRNA.
DR PIR; T48370; T48370.
DR RefSeq; NP_568119.1; NM_120425.3.
DR PDB; 1T3K; NMR; -; A=15-146.
DR PDBsum; 1T3K; -.
DR AlphaFoldDB; Q8GY31; -.
DR SMR; Q8GY31; -.
DR BioGRID; 17108; 3.
DR IntAct; Q8GY31; 3.
DR STRING; 3702.AT5G03455.1; -.
DR PaxDb; Q8GY31; -.
DR PRIDE; Q8GY31; -.
DR ProteomicsDB; 223970; -.
DR EnsemblPlants; AT5G03455.1; AT5G03455.1; AT5G03455.
DR GeneID; 831832; -.
DR Gramene; AT5G03455.1; AT5G03455.1; AT5G03455.
DR KEGG; ath:AT5G03455; -.
DR Araport; AT5G03455; -.
DR TAIR; locus:505006579; AT5G03455.
DR eggNOG; KOG3772; Eukaryota.
DR HOGENOM; CLU_107716_2_0_1; -.
DR InParanoid; Q8GY31; -.
DR OMA; PVCRCTN; -.
DR OrthoDB; 1513881at2759; -.
DR PhylomeDB; Q8GY31; -.
DR BioCyc; ARA:AT5G03455-MON; -.
DR SABIO-RK; Q8GY31; -.
DR EvolutionaryTrace; Q8GY31; -.
DR PRO; PR:Q8GY31; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GY31; baseline and differential.
DR Genevisible; Q8GY31; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:TAIR.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0046685; P:response to arsenic-containing substance; IMP:TAIR.
DR DisProt; DP00916; -.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Hydrolase; Metal-binding; Mitosis;
KW Nucleus; Oxidoreductase; Protein phosphatase; Reference proteome; Zinc.
FT CHAIN 1..146
FT /note="Dual specificity phosphatase Cdc25"
FT /id="PRO_0000198663"
FT DOMAIN 34..135
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 86
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 45..48
FT /ligand="substrate"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15329414,
FT ECO:0000269|PubMed:15336525"
FT BINDING 68..71
FT /ligand="substrate"
FT BINDING 90..92
FT /ligand="substrate"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15329414,
FT ECO:0000269|PubMed:15336525"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15329414,
FT ECO:0000269|PubMed:15336525"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15329414,
FT ECO:0000269|PubMed:15336525"
FT MUTAGEN 86
FT /note="C->S: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:15329414"
FT MUTAGEN 145
FT /note="C->S: No major structural changes."
FT /evidence="ECO:0000269|PubMed:15336525"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1T3K"
FT TURN 26..31
FT /evidence="ECO:0007829|PDB:1T3K"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1T3K"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1T3K"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1T3K"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1T3K"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:1T3K"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1T3K"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1T3K"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:1T3K"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1T3K"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:1T3K"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:1T3K"
SQ SEQUENCE 146 AA; 16450 MW; EA2DD0E79784D538 CRC64;
MGRSIFSFFT KKKKMAMARS ISYITSTQLL PLHRRPNIAI IDVRDEERNY DGHIAGSLHY
ASGSFDDKIS HLVQNVKDKD TLVFHCALSQ VRGPTCARRL VNYLDEKKED TGIKNIMILE
RGFNGWEASG KPVCRCAEVP CKGDCA
