CHIB_ARATH
ID CHIB_ARATH Reviewed; 335 AA.
AC P19171; Q9S7J5; Q9S838; Q9SXJ2; Q9SXJ3; Q9SXJ4;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Basic endochitinase B;
DE EC=3.2.1.14;
DE AltName: Full=Pathogenesis-related protein 3;
DE Short=AtChiB;
DE Short=PR-3;
DE Flags: Precursor;
GN Name=CHI-B; Synonyms=PR3; OrderedLocusNames=At3g12500;
GN ORFNames=MQC3.32, T2E22.18, T2E22_119;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=16667600; DOI=10.1104/pp.93.3.907;
RA Samac D.A., Hironaka C.M., Yallaly P.E., Shah D.M.;
RT "Isolation and characterization of the genes encoding basic and acidic
RT chitinase in Arabidopsis thaliana.";
RL Plant Physiol. 93:907-914(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=cv. Aa-0, cv. Al-0, cv. Bl-1, cv. Bla-10, cv. Bs-1, cv. Chi-0,
RC cv. Ci-0, cv. Es-0, cv. Gr-1, cv. Hiroshima, cv. Ita-0, cv. Kn-0, cv. Mt-0,
RC cv. Pog-0, cv. Shokei, and cv. Yo-0;
RX PubMed=10545472; DOI=10.1093/genetics/153.3.1445;
RA Kawabe A., Miyashita N.T.;
RT "DNA variation in the basic chitinase locus (ChiB) region of the wild plant
RT Arabidopsis thaliana.";
RL Genetics 153:1445-1453(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-335.
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 [7]
RP PROTEIN SEQUENCE OF 237-256, AND ANTIFUNGAL ACTIVITY.
RX PubMed=16668004; DOI=10.1104/pp.95.2.450;
RA Verburg J.G., Huynh Q.K.;
RT "Purification and characterization of an antifungal chitinase from
RT Arabidopsis thaliana.";
RL Plant Physiol. 95:450-455(1991).
RN [8]
RP INDUCTION.
RX PubMed=7610160; DOI=10.1104/pp.108.2.597;
RA Chen Q.G., Bleecker A.B.;
RT "Analysis of ethylene signal-transduction kinetics associated with
RT seedling-growth response and chitinase induction in wild-type and mutant
RT Arabidopsis.";
RL Plant Physiol. 108:597-607(1995).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=9844023; DOI=10.1073/pnas.95.25.15107;
RA Thomma B.P.H.J., Eggermont K., Penninckx I.A.M.A., Mauch-Mani B.,
RA Vogelsang R., Cammue B.P.A., Broekaert W.F.;
RT "Separate jasmonate-dependent and salicylate-dependent defense-response
RT pathways in Arabidopsis are essential for resistance to distinct microbial
RT pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15107-15111(1998).
RN [10]
RP INDUCTION.
RX PubMed=10608663; DOI=10.1023/a:1006319216982;
RA van Wees S.C., Luijendijk M., Smoorenburg I., van Loon L.C., Pieterse C.M.;
RT "Rhizobacteria-mediated induced systemic resistance (ISR) in Arabidopsis is
RT not associated with a direct effect on expression of known defense-related
RT genes but stimulates the expression of the jasmonate-inducible gene Atvsp
RT upon challenge.";
RL Plant Mol. Biol. 41:537-549(1999).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=23738689; DOI=10.1111/tpj.12257;
RA Shen J., Suen P.K., Wang X., Lin Y., Lo S.W., Rojo E., Jiang L.;
RT "An in vivo expression system for the identification of cargo proteins of
RT vacuolar sorting receptors in Arabidopsis culture cells.";
RL Plant J. 75:1003-1017(2013).
CC -!- FUNCTION: Defense against chitin-containing fungal pathogens. Seems
CC particularly implicated in resistance to jasmonate-inducing pathogens
CC such as A.brassicicola. In vitro antifungal activity against T.reesei,
CC but not against A.solani, F.oxysporum, S.sclerotiorum, G.graminis and
CC P.megasperma. {ECO:0000269|PubMed:9844023}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:23738689}.
CC -!- TISSUE SPECIFICITY: High constitutive level in roots with lower levels
CC in leaves and flowering shoots. {ECO:0000269|PubMed:16667600}.
CC -!- INDUCTION: Ethylene induces high levels of systemic expression of basic
CC chitinase with expression increasing with plant age. Locally and
CC systemically induced by jasmonic acid (JA) and pathogens such as
CC A.brassicicola and P.syringae, particularly in case of hypersensitive
CC responses (HR). Not induced by wounding. {ECO:0000269|PubMed:10608663,
CC ECO:0000269|PubMed:16667600, ECO:0000269|PubMed:7610160,
CC ECO:0000269|PubMed:9844023}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK96819.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB03157.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M38240; AAA32769.1; -; Genomic_DNA.
DR EMBL; AB023448; BAA82810.1; -; Genomic_DNA.
DR EMBL; AB023449; BAA82811.1; -; Genomic_DNA.
DR EMBL; AB023450; BAA82812.1; -; Genomic_DNA.
DR EMBL; AB023451; BAA82813.1; -; Genomic_DNA.
DR EMBL; AB023452; BAA82814.1; -; Genomic_DNA.
DR EMBL; AB023453; BAA82815.1; -; Genomic_DNA.
DR EMBL; AB023454; BAA82816.1; -; Genomic_DNA.
DR EMBL; AB023455; BAA82817.1; -; Genomic_DNA.
DR EMBL; AB023456; BAA82818.1; -; Genomic_DNA.
DR EMBL; AB023457; BAA82819.1; -; Genomic_DNA.
DR EMBL; AB023458; BAA82820.1; -; Genomic_DNA.
DR EMBL; AB023459; BAA82821.1; -; Genomic_DNA.
DR EMBL; AB023460; BAA82822.1; -; Genomic_DNA.
DR EMBL; AB023461; BAA82823.1; -; Genomic_DNA.
DR EMBL; AB023462; BAA82824.1; -; Genomic_DNA.
DR EMBL; AB023463; BAA82825.1; -; Genomic_DNA.
DR EMBL; AP002047; BAB03157.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC069474; AAG51023.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75203.1; -; Genomic_DNA.
DR EMBL; AY054628; AAK96819.1; ALT_INIT; mRNA.
DR EMBL; AY081519; AAM10081.1; -; mRNA.
DR PIR; B45511; B45511.
DR RefSeq; NP_566426.2; NM_112085.4.
DR AlphaFoldDB; P19171; -.
DR SMR; P19171; -.
DR BioGRID; 5763; 2.
DR STRING; 3702.AT3G12500.1; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; P19171; -.
DR PRIDE; P19171; -.
DR ProteomicsDB; 240890; -.
DR EnsemblPlants; AT3G12500.1; AT3G12500.1; AT3G12500.
DR GeneID; 820429; -.
DR Gramene; AT3G12500.1; AT3G12500.1; AT3G12500.
DR KEGG; ath:AT3G12500; -.
DR Araport; AT3G12500; -.
DR TAIR; locus:2092502; AT3G12500.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_0_1; -.
DR InParanoid; P19171; -.
DR OMA; CEPSATW; -.
DR OrthoDB; 1132954at2759; -.
DR PhylomeDB; P19171; -.
DR BioCyc; ARA:AT3G12500-MON; -.
DR PRO; PR:P19171; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P19171; baseline and differential.
DR Genevisible; P19171; AT.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.10; -; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF57016; SSF57016; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS00773; CHITINASE_19_1; 1.
DR PROSITE; PS00774; CHITINASE_19_2; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Direct protein sequencing; Disulfide bond; Fungicide; Glycosidase;
KW Hydrolase; Hypersensitive response; Plant defense;
KW Polysaccharide degradation; Reference proteome; Signal; Vacuole.
FT SIGNAL 1..33
FT CHAIN 34..328
FT /note="Basic endochitinase B"
FT /id="PRO_0000005287"
FT PROPEP 329..335
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000005288"
FT DOMAIN 34..75
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT MOTIF 329..335
FT /note="Vacuolar targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 36..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 45..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 50..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 69..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 107..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 181..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 288..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT VARIANT 17
FT /note="N -> K (in strain: cv. Bl-1, cv. Shokei and cv. Yo-
FT 0)"
FT VARIANT 106
FT /note="A -> T (in strain: cv. Aa-0)"
FT VARIANT 127
FT /note="G -> S (in strain: cv. Yo-0)"
FT VARIANT 206
FT /note="N -> D (in strain: cv. Ci-0)"
SQ SEQUENCE 335 AA; 36184 MW; 0973CE89B30ABF61 CRC64;
MPPQKENHRT LNKMKTNLFL FLIFSLLLSL SSAEQCGRQA GGALCPNGLC CSEFGWCGNT
EPYCKQPGCQ SQCTPGGTPP GPTGDLSGII SSSQFDDMLK HRNDAACPAR GFYTYNAFIT
AAKSFPGFGT TGDTATRKKE VAAFFGQTSH ETTGGWATAP DGPYSWGYCF KQEQNPASDY
CEPSATWPCA SGKRYYGRGP MQLSWNYNYG LCGRAIGVDL LNNPDLVAND AVIAFKAAIW
FWMTAQPPKP SCHAVIAGQW QPSDADRAAG RLPGYGVITN IINGGLECGR GQDGRVADRI
GFYQRYCNIF GVNPGGNLDC YNQRSFVNGL LEAAI
