HEVL_ARATH
ID HEVL_ARATH Reviewed; 212 AA.
AC P43082;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Hevein-like preproprotein;
DE Contains:
DE RecName: Full=CB-HEL;
DE Contains:
DE RecName: Full=CD-HEL;
DE EC=3.1.-.-;
DE AltName: Full=RNase;
DE Flags: Precursor;
GN Name=HEL; OrderedLocusNames=At3g04720; ORFNames=F7O18.21;
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], AND INDUCTION.
RX PubMed=8118053; DOI=10.1094/mpmi-6-680;
RA Potter S., Uknes S., Lawton K., Winter A.M., Chandler D., Dimaio J.,
RA Novitzky R., Ward E., Ryals J.;
RT "Regulation of a hevein-like gene in Arabidopsis.";
RL Mol. Plant Microbe Interact. 6:680-685(1993).
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 INDUCTION.
RX PubMed=21193575; DOI=10.1093/jxb/erq396;
RA Proietti S., Bertini L., Van der Ent S., Leon-Reyes A., Pieterse C.M.,
RA Tucci M., Caporale C., Caruso C.;
RT "Cross activity of orthologous WRKY transcription factors in wheat and
RT Arabidopsis.";
RL J. Exp. Bot. 62:1975-1990(2011).
RN [7]
RP FUNCTION, 3D-STRUCTURE MODELING, PROTEOLYTIC PROCESSING, INTERACTION,
RP SUBCELLULAR LOCATION, DOMAIN, AND DISULFIDE BOND.
RX PubMed=22868784; DOI=10.1515/hsz-2012-0225;
RA Bertini L., Proietti S., Aleandri M.P., Mondello F., Sandini S.,
RA Caporale C.;
RT "Modular structure of HEL protein from Arabidopsis reveals new potential
RT functions for PR-4 proteins.";
RL Biol. Chem. 393:1533-1546(2012).
CC -!- FUNCTION: Fungal growth inhibitors. Neither CB-HEL nor CD-HEL have
CC chitinase activity, but both have antimicrobial activities. CD-HEL has
CC RNase, but no DNase activity. {ECO:0000269|PubMed:22868784}.
CC -!- SUBUNIT: CB-HEL interacts strongly with a fungal fruiting body lectin.
CC {ECO:0000269|PubMed:22868784}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:22868784}.
CC Note=associated with the tonoplast.
CC -!- INDUCTION: Up-regulated by ethylene, methyl jasmonate, wounding and
CC virus infection. Weakly induced by salicylic acid and 2,6-
CC dichlorisonicotinic acid. {ECO:0000269|PubMed:21193575,
CC ECO:0000269|PubMed:8118053}.
CC -!- DOMAIN: The C-terminal vacuolar sorting signal (VSS) (194-212) is
CC required for vacuolar localization. {ECO:0000269|PubMed:22868784}.
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DR EMBL; U01880; AAA20642.1; -; mRNA.
DR EMBL; AC011437; AAF04912.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74125.1; -; Genomic_DNA.
DR EMBL; AF370536; AAK48963.1; -; mRNA.
DR EMBL; BT000046; AAN15365.1; -; mRNA.
DR EMBL; AY088644; AAM66966.1; -; mRNA.
DR RefSeq; NP_187123.1; NM_111344.6.
DR AlphaFoldDB; P43082; -.
DR SMR; P43082; -.
DR BioGRID; 4967; 1.
DR IntAct; P43082; 1.
DR STRING; 3702.AT3G04720.1; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR PaxDb; P43082; -.
DR PRIDE; P43082; -.
DR ProteomicsDB; 230128; -.
DR EnsemblPlants; AT3G04720.1; AT3G04720.1; AT3G04720.
DR GeneID; 819632; -.
DR Gramene; AT3G04720.1; AT3G04720.1; AT3G04720.
DR KEGG; ath:AT3G04720; -.
DR Araport; AT3G04720; -.
DR TAIR; locus:2084918; AT3G04720.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_1328439_0_0_1; -.
DR InParanoid; P43082; -.
DR OMA; ADKPYAW; -.
DR OrthoDB; 1332779at2759; -.
DR PhylomeDB; P43082; -.
DR PRO; PR:P43082; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P43082; baseline and differential.
DR Genevisible; P43082; AT.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; ISS:TAIR.
DR GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR GO; GO:0080027; P:response to herbivore; IEP:TAIR.
DR GO; GO:0009615; P:response to virus; IEP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IEP:TAIR.
DR Gene3D; 2.40.40.10; -; 1.
DR Gene3D; 3.30.60.10; -; 1.
DR InterPro; IPR018226; Barwin_CS.
DR InterPro; IPR001153; Barwin_dom.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR044301; PR4.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR46351; PTHR46351; 1.
DR Pfam; PF00967; Barwin; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR PRINTS; PR00602; BARWIN.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF50685; SSF50685; 1.
DR SUPFAM; SSF57016; SSF57016; 1.
DR PROSITE; PS00771; BARWIN_1; 1.
DR PROSITE; PS00772; BARWIN_2; 1.
DR PROSITE; PS51174; BARWIN_3; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Chitin-binding; Disulfide bond; Fungicide; Hydrolase;
KW Nuclease; Pathogenesis-related protein; Plant defense; Reference proteome;
KW Signal; Vacuole.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..212
FT /note="Hevein-like preproprotein"
FT /id="PRO_0000005284"
FT CHAIN 22..?
FT /note="CB-HEL"
FT /id="PRO_0000421568"
FT CHAIN ?..212
FT /note="CD-HEL"
FT /id="PRO_0000421569"
FT DOMAIN 22..64
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 72..193
FT /note="Barwin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00527"
FT DISULFID 24..39
FT /evidence="ECO:0000305|PubMed:22868784"
FT DISULFID 33..45
FT /evidence="ECO:0000305|PubMed:22868784"
FT DISULFID 38..52
FT /evidence="ECO:0000305|PubMed:22868784"
FT DISULFID 58..62
FT /evidence="ECO:0000305|PubMed:22868784"
FT DISULFID 100..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 121..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 135..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 212 AA; 22937 MW; 1EDAD140A21AA692 CRC64;
MKIRLSITII LLSYTVATVA GQQCGRQGGG RTCPGNICCS QYGYCGTTAD YCSPTNNCQS
NCWGSGPSGP GESASNVRAT YHFYNPAQNN WDLRAVSAYC STWDADKPYA WRSKYGWTAF
CGPAGPRGQA SCGKCLRVKN TRTNAAVTVR IVDQCSNGGL DLDVAMFNQI DTDGFGYQQG
HLIVDYQFVD CGNELIGQPD SRNMLVSAID RV
