PER34_ARATH
ID PER34_ARATH Reviewed; 353 AA.
AC Q9SMU8; Q42206; Q42584; Q9C5R4;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Peroxidase 34;
DE Short=Atperox P34;
DE EC=1.11.1.7;
DE AltName: Full=ATPCb;
DE Flags: Precursor;
GN Name=PER34; Synonyms=P34, PRXCB; OrderedLocusNames=At3g49120;
GN ORFNames=F2K15.3, T2J13.40;
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;
RX PubMed=8115548; DOI=10.1104/pp.104.1.285;
RA Intapruk C., Takano M., Shinmyo A.;
RT "Nucleotide sequence of a new cDNA for peroxidase from Arabidopsis
RT thaliana.";
RL Plant Physiol. 104:285-286(1994).
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-226.
RC TISSUE=Leaf;
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-154.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [8]
RP CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=9738941; DOI=10.1016/s0014-5793(98)00849-7;
RA Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.;
RT "Computational analyses and annotations of the Arabidopsis peroxidase gene
RT family.";
RL FEBS Lett. 433:98-102(1998).
RN [9]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9449849; DOI=10.1104/pp.116.1.409;
RA Richards K.D., Schott E.J., Sharma Y.K., Davis K.R., Gardner R.C.;
RT "Aluminum induces oxidative stress genes in Arabidopsis thaliana.";
RL Plant Physiol. 116:409-418(1998).
RN [10]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10712528; DOI=10.1104/pp.122.3.657;
RA Ezaki B., Gardner R.C., Ezaki Y., Matsumoto H.;
RT "Expression of aluminum-induced genes in transgenic Arabidopsis plants can
RT ameliorate aluminum stress and/or oxidative stress.";
RL Plant Physiol. 122:657-665(2000).
RN [11]
RP INDUCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11101835; DOI=10.1038/82521;
RA Maleck K., Levine A., Eulgem T., Morgan A., Schmid J., Lawton K.A.,
RA Dangl J.L., Dietrich R.A.;
RT "The transcriptome of Arabidopsis thaliana during systemic acquired
RT resistance.";
RL Nat. Genet. 26:403-410(2000).
RN [12]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=12164808; DOI=10.1046/j.1365-313x.2002.01359.x;
RA Seki M., Narusaka M., Ishida J., Nanjo T., Fujita M., Oono Y., Kamiya A.,
RA Nakajima M., Enju A., Sakurai T., Satou M., Akiyama K., Taji T.,
RA Yamaguchi-Shinozaki K., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Monitoring the expression profiles of 7000 Arabidopsis genes under
RT drought, cold and high-salinity stresses using a full-length cDNA
RT microarray.";
RL Plant J. 31:279-292(2002).
RN [13]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11748215; DOI=10.1074/jbc.m104863200;
RA Scheideler M., Schlaich N.L., Fellenberg K., Beissbarth T., Hauser N.C.,
RA Vingron M., Slusarenko A.J., Hoheisel J.D.;
RT "Monitoring the switch from housekeeping to pathogen defense metabolism in
RT Arabidopsis thaliana using cDNA arrays.";
RL J. Biol. Chem. 277:10555-10561(2002).
RN [14]
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RA Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X.;
RT "Toward elucidating the global gene expression patterns of developing
RT Arabidopsis: parallel analysis of 8300 genes by a high-density
RT oligonucleotide probe array.";
RL Plant Physiol. Biochem. 39:221-242(2001).
RN [15]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12034502; DOI=10.1016/s0378-1119(02)00465-1;
RA Tognolli M., Penel C., Greppin H., Simon P.;
RT "Analysis and expression of the class III peroxidase large gene family in
RT Arabidopsis thaliana.";
RL Gene 288:129-138(2002).
RN [16]
RP CHARACTERIZATION.
RX PubMed=14751301; DOI=10.1016/j.phytochem.2003.11.019;
RA Shah K., Penel C., Gagnon J., Dunand C.;
RT "Purification and identification of a Ca(2+)-pectate binding peroxidase
RT from Arabidopsis leaves.";
RL Phytochemistry 65:307-312(2004).
CC -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC biosynthesis and degradation of lignin, suberization, auxin catabolism,
CC response to environmental stresses such as wounding, pathogen attack
CC and oxidative stress. These functions might be dependent on each
CC isozyme/isoform in each plant tissue.
CC -!- FUNCTION: May be implicated in the systemic acquired resistance
CC response via the salicylic acid signal transduction pathway. Exhibits a
CC Ca(2+)-pectate binding affinity which could be interpreted in vivo as a
CC specificity to interact with the pectic structure of the cell wall.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00297};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole {ECO:0000305}.
CC Note=Carboxy-terminal extension appears to target the protein to
CC vacuoles.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in roots, but also
CC detected in flowers, leaves and stems.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during leaf development.
CC {ECO:0000269|Ref.14}.
CC -!- INDUCTION: Late-induced by Al treatment. Expression increased over 48
CC hours of Al treatment. Induced by oxidative stress. Up-regulated during
CC a continuous drought stress. Early induced by benzothiadiazol, a
CC chemical analog of salicylic acid. Enhanced expression following both
CC compatible or incompatible pathogen attacks.
CC {ECO:0000269|PubMed:10712528, ECO:0000269|PubMed:11101835,
CC ECO:0000269|PubMed:11748215, ECO:0000269|PubMed:12164808,
CC ECO:0000269|PubMed:9449849}.
CC -!- MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG40051.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X71794; CAA50677.1; -; mRNA.
DR EMBL; AL132956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL132967; CAB61998.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78501.1; -; Genomic_DNA.
DR EMBL; AF324700; AAG40051.2; ALT_FRAME; mRNA.
DR EMBL; AF326880; AAG41462.1; -; mRNA.
DR EMBL; AF339700; AAK00382.1; -; mRNA.
DR EMBL; AF419569; AAL31901.1; -; mRNA.
DR EMBL; AY079106; AAL84990.1; -; mRNA.
DR EMBL; AY087926; AAM65476.1; -; mRNA.
DR EMBL; AF083684; AAN60243.1; -; mRNA.
DR EMBL; Z29133; CAA82392.1; -; mRNA.
DR PIR; S37495; S37495.
DR PIR; T46118; T46118.
DR RefSeq; NP_190481.1; NM_114771.3.
DR AlphaFoldDB; Q9SMU8; -.
DR SMR; Q9SMU8; -.
DR BioGRID; 9391; 2.
DR STRING; 3702.AT3G49120.1; -.
DR PeroxiBase; 200; AtPrx34.
DR PaxDb; Q9SMU8; -.
DR PRIDE; Q9SMU8; -.
DR ProteomicsDB; 236453; -.
DR EnsemblPlants; AT3G49120.1; AT3G49120.1; AT3G49120.
DR GeneID; 824073; -.
DR Gramene; AT3G49120.1; AT3G49120.1; AT3G49120.
DR KEGG; ath:AT3G49120; -.
DR Araport; AT3G49120; -.
DR TAIR; locus:2101318; AT3G49120.
DR eggNOG; ENOG502QVXS; Eukaryota.
DR HOGENOM; CLU_010543_0_1_1; -.
DR InParanoid; Q9SMU8; -.
DR OMA; RAHCITF; -.
DR OrthoDB; 819626at2759; -.
DR PhylomeDB; Q9SMU8; -.
DR BioCyc; ARA:AT3G49120-MON; -.
DR PRO; PR:Q9SMU8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SMU8; baseline and differential.
DR Genevisible; Q9SMU8; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:TAIR.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR CDD; cd00693; secretory_peroxidase; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31388; PTHR31388; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Vacuole.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..353
FT /note="Peroxidase 34"
FT /id="PRO_0000023700"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 200
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 68
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 31
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 74..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 127..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 207..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 97
FT /note="A -> R (in Ref. 1; CAA50677)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="P -> S (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="L -> F (in Ref. 1; CAA50677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 38832 MW; 8CDB98A2EF3E130B CRC64;
MHFSSSSTSS TWTILITLGC LMLHASLSAA QLTPTFYDRS CPNVTNIVRE TIVNELRSDP
RIAASILRLH FHDCFVNGCD ASILLDNTTS FRTEKDAFGN ANSARGFPVI DRMKAAVERA
CPRTVSCADM LTIAAQQSVT LAGGPSWRVP LGRRDSLQAF LELANANLPA PFFTLPQLKA
SFRNVGLDRP SDLVALSGGH TFGKNQCQFI LDRLYNFSNT GLPDPTLNTT YLQTLRGLCP
LNGNRSALVD FDLRTPTVFD NKYYVNLKER KGLIQSDQEL FSSPNATDTI PLVRAYADGT
QTFFNAFVEA MNRMGNITPT TGTQGQIRLN CRVVNSNSLL HDVVDIVDFV SSM
