ID   OSL3_ARATH              Reviewed;         244 AA.
AC   P50700; Q9T0D2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Osmotin-like protein OSM34;
DE   Flags: Precursor;
GN   Name=OSM34; OrderedLocusNames=At4g11650; ORFNames=T5C23.80;
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=Leaf;
RX   PubMed=9210588; DOI=10.1016/s0378-1119(97)00029-2;
RA   Capelli N., Diogon T., Greppin H., Simon P.;
RT   "Isolation and characterization of a cDNA clone encoding an osmotin-like
RT   protein from Arabidopsis thaliana.";
RL   Gene 191:51-56(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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).
CC   -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00699}.
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DR   EMBL; X89008; CAA61411.1; -; mRNA.
DR   EMBL; AL049500; CAB39936.1; -; Genomic_DNA.
DR   EMBL; AL161532; CAB78208.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83033.1; -; Genomic_DNA.
DR   PIR; T04212; T04212.
DR   RefSeq; NP_192902.1; NM_117234.3.
DR   AlphaFoldDB; P50700; -.
DR   SMR; P50700; -.
DR   BioGRID; 12068; 1.
DR   STRING; 3702.AT4G11650.1; -.
DR   iPTMnet; P50700; -.
DR   PaxDb; P50700; -.
DR   PRIDE; P50700; -.
DR   ProteomicsDB; 226036; -.
DR   EnsemblPlants; AT4G11650.1; AT4G11650.1; AT4G11650.
DR   GeneID; 826770; -.
DR   Gramene; AT4G11650.1; AT4G11650.1; AT4G11650.
DR   KEGG; ath:AT4G11650; -.
DR   Araport; AT4G11650; -.
DR   TAIR; locus:2139777; AT4G11650.
DR   eggNOG; ENOG502QV4N; Eukaryota.
DR   HOGENOM; CLU_043181_5_0_1; -.
DR   InParanoid; P50700; -.
DR   OMA; NCHRILC; -.
DR   OrthoDB; 1135904at2759; -.
DR   PhylomeDB; P50700; -.
DR   PRO; PR:P50700; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P50700; baseline and differential.
DR   Genevisible; P50700; AT.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR   Gene3D; 2.60.110.10; -; 1.
DR   InterPro; IPR037176; Osmotin/thaumatin-like_sf.
DR   InterPro; IPR001938; Thaumatin.
DR   InterPro; IPR017949; Thaumatin_CS.
DR   PANTHER; PTHR31048; PTHR31048; 1.
DR   Pfam; PF00314; Thaumatin; 1.
DR   PIRSF; PIRSF002703; Thaumatin; 1.
DR   PRINTS; PR00347; THAUMATIN.
DR   SMART; SM00205; THN; 1.
DR   SUPFAM; SSF49870; SSF49870; 1.
DR   PROSITE; PS00316; THAUMATIN_1; 1.
DR   PROSITE; PS51367; THAUMATIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..244
FT                   /note="Osmotin-like protein OSM34"
FT                   /id="PRO_0000034038"
FT   DISULFID        31..222
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        72..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        87..93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        138..212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        143..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        151..161
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        165..174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        175..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   CONFLICT        186
FT                   /note="E -> V (in Ref. 1; CAA61411)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   244 AA;  26633 MW;  9FBE9A45E9E195E0 CRC64;
     MANLLVSTFI FSALLLISTA TAATFEILNQ CSYTVWAAAS PGGGRRLDAG QSWRLDVAAG
     TKMARIWGRT NCNFDSSGRG RCQTGDCSGG LQCTGWGQPP NTLAEYALNQ FNNLDFYDIS
     LVDGFNIPME FSPTSSNCHR ILCTADINGQ CPNVLRAPGG CNNPCTVFQT NQYCCTNGQG
     SCSDTEYSRF FKQRCPDAYS YPQDDPTSTF TCTNTNYRVV FCPRSRLGAT GSHQLPIKMV
     TEEN