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Protein

Basic endochitinase B

Gene

CHI-B

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Defense against chitin containing fungal pathogens. Seems particularly implicated in resistance to jasmonate-inducing pathogens such as A.brassicicola. In vitro antifungal activity against T.reesei, but not against A.solani, F.oxysporum, S.sclerotiorum, G.graminis and P.megasperma.1 Publication

Catalytic activityi

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

GO - Molecular functioni

  1. chitinase activity Source: UniProtKB-EC
  2. chitin binding Source: UniProtKB-KW

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. chitin catabolic process Source: UniProtKB-KW
  3. defense response to fungus Source: UniProtKB-KW
  4. killing of cells of other organism Source: UniProtKB-KW
  5. plant-type hypersensitive response Source: UniProtKB-KW
  6. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Fungicide, Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Hypersensitive response, Plant defense, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Enzyme and pathway databases

BioCyciARA:AT3G12500-MONOMER.

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Names & Taxonomyi

Protein namesi
Recommended name:
Basic endochitinase B (EC:3.2.1.14)
Alternative name(s):
Pathogenesis-related protein 3
Short name:
AtChiB
Short name:
PR-3
Gene namesi
Name:CHI-B
Synonyms:PR3
Ordered Locus Names:At3g12500
ORF Names:MQC3.32, T2E22.18, T2E22_119
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G12500.

Subcellular locationi

Vacuole 1 Publication

GO - Cellular componenti

  1. vacuole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Add
BLAST
Chaini34 – 328295Basic endochitinase BPRO_0000005287Add
BLAST
Propeptidei329 – 3357Removed in mature formCuratedPRO_0000005288

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 51PROSITE-ProRule annotation
Disulfide bondi45 ↔ 57PROSITE-ProRule annotation
Disulfide bondi50 ↔ 64PROSITE-ProRule annotation
Disulfide bondi69 ↔ 73PROSITE-ProRule annotation
Disulfide bondi107 ↔ 169PROSITE-ProRule annotation
Disulfide bondi181 ↔ 189PROSITE-ProRule annotation
Disulfide bondi288 ↔ 320PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP19171.
PRIDEiP19171.

Expressioni

Tissue specificityi

High constitutive level in roots with lower levels in leaves and flowering shoots.1 Publication

Inductioni

Ethylene induces high levels of systemic expression of basic chitinase with expression increasing with plant age. Locally and systemically induced by jasmonic acid (JA) and pathogens such as A.brassicicola and P.syringae, particularly in case of hypersensitive responses (HR). Not induced by wounding.4 Publications

Gene expression databases

GenevestigatoriP19171.

Interactioni

Protein-protein interaction databases

BioGridi5763. 1 interaction.

Structurei

3D structure databases

SMRiP19171. Positions 34-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 7542Chitin-binding type-1PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi329 – 3357Vacuolar targeting signalSequence Analysis

Sequence similaritiesi

Contains 1 chitin-binding type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3979.
HOGENOMiHOG000231411.
InParanoidiP19171.
KOiK01183.
OMAiCHAVIAG.
PhylomeDBiP19171.

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19171-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPQKENHRT LNKMKTNLFL FLIFSLLLSL SSAEQCGRQA GGALCPNGLC
60 70 80 90 100
CSEFGWCGNT EPYCKQPGCQ SQCTPGGTPP GPTGDLSGII SSSQFDDMLK
110 120 130 140 150
HRNDAACPAR GFYTYNAFIT AAKSFPGFGT TGDTATRKKE VAAFFGQTSH
160 170 180 190 200
ETTGGWATAP DGPYSWGYCF KQEQNPASDY CEPSATWPCA SGKRYYGRGP
210 220 230 240 250
MQLSWNYNYG LCGRAIGVDL LNNPDLVAND AVIAFKAAIW FWMTAQPPKP
260 270 280 290 300
SCHAVIAGQW QPSDADRAAG RLPGYGVITN IINGGLECGR GQDGRVADRI
310 320 330
GFYQRYCNIF GVNPGGNLDC YNQRSFVNGL LEAAI
Length:335
Mass (Da):36,184
Last modified:August 30, 2005 - v3
Checksum:i0973CE89B30ABF61
GO

Sequence cautioni

The sequence AAK96819.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB03157.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171N → K in strain: cv. Bl-1, cv. Shokei and cv. Yo-0.
Natural varianti106 – 1061A → T in strain: cv. Aa-0.
Natural varianti127 – 1271G → S in strain: cv. Yo-0.
Natural varianti206 – 2061N → D in strain: cv. Ci-0.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38240 Genomic DNA. Translation: AAA32769.1.
AB023448 Genomic DNA. Translation: BAA82810.1.
AB023449 Genomic DNA. Translation: BAA82811.1.
AB023450 Genomic DNA. Translation: BAA82812.1.
AB023451 Genomic DNA. Translation: BAA82813.1.
AB023452 Genomic DNA. Translation: BAA82814.1.
AB023453 Genomic DNA. Translation: BAA82815.1.
AB023454 Genomic DNA. Translation: BAA82816.1.
AB023455 Genomic DNA. Translation: BAA82817.1.
AB023456 Genomic DNA. Translation: BAA82818.1.
AB023457 Genomic DNA. Translation: BAA82819.1.
AB023458 Genomic DNA. Translation: BAA82820.1.
AB023459 Genomic DNA. Translation: BAA82821.1.
AB023460 Genomic DNA. Translation: BAA82822.1.
AB023461 Genomic DNA. Translation: BAA82823.1.
AB023462 Genomic DNA. Translation: BAA82824.1.
AB023463 Genomic DNA. Translation: BAA82825.1.
AP002047 Genomic DNA. Translation: BAB03157.1. Different initiation.
AC069474 Genomic DNA. Translation: AAG51023.1.
CP002686 Genomic DNA. Translation: AEE75203.1.
AY054628 mRNA. Translation: AAK96819.1. Different initiation.
AY081519 mRNA. Translation: AAM10081.1.
PIRiB45511.
RefSeqiNP_566426.2. NM_112085.3.
UniGeneiAt.296.
At.75583.

Genome annotation databases

EnsemblPlantsiAT3G12500.1; AT3G12500.1; AT3G12500.
GeneIDi820429.
KEGGiath:AT3G12500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38240 Genomic DNA. Translation: AAA32769.1.
AB023448 Genomic DNA. Translation: BAA82810.1.
AB023449 Genomic DNA. Translation: BAA82811.1.
AB023450 Genomic DNA. Translation: BAA82812.1.
AB023451 Genomic DNA. Translation: BAA82813.1.
AB023452 Genomic DNA. Translation: BAA82814.1.
AB023453 Genomic DNA. Translation: BAA82815.1.
AB023454 Genomic DNA. Translation: BAA82816.1.
AB023455 Genomic DNA. Translation: BAA82817.1.
AB023456 Genomic DNA. Translation: BAA82818.1.
AB023457 Genomic DNA. Translation: BAA82819.1.
AB023458 Genomic DNA. Translation: BAA82820.1.
AB023459 Genomic DNA. Translation: BAA82821.1.
AB023460 Genomic DNA. Translation: BAA82822.1.
AB023461 Genomic DNA. Translation: BAA82823.1.
AB023462 Genomic DNA. Translation: BAA82824.1.
AB023463 Genomic DNA. Translation: BAA82825.1.
AP002047 Genomic DNA. Translation: BAB03157.1. Different initiation.
AC069474 Genomic DNA. Translation: AAG51023.1.
CP002686 Genomic DNA. Translation: AEE75203.1.
AY054628 mRNA. Translation: AAK96819.1. Different initiation.
AY081519 mRNA. Translation: AAM10081.1.
PIRiB45511.
RefSeqiNP_566426.2. NM_112085.3.
UniGeneiAt.296.
At.75583.

3D structure databases

SMRiP19171. Positions 34-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi5763. 1 interaction.

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Proteomic databases

PaxDbiP19171.
PRIDEiP19171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G12500.1; AT3G12500.1; AT3G12500.
GeneIDi820429.
KEGGiath:AT3G12500.

Organism-specific databases

TAIRiAT3G12500.

Phylogenomic databases

eggNOGiCOG3979.
HOGENOMiHOG000231411.
InParanoidiP19171.
KOiK01183.
OMAiCHAVIAG.
PhylomeDBiP19171.

Enzyme and pathway databases

BioCyciARA:AT3G12500-MONOMER.

Gene expression databases

GenevestigatoriP19171.

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the genes encoding basic and acidic chitinase in Arabidopsis thaliana."
    Samac D.A., Hironaka C.M., Yallaly P.E., Shah D.M.
    Plant Physiol. 93:907-914(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
  2. "DNA variation in the basic chitinase locus (ChiB) region of the wild plant Arabidopsis thaliana."
    Kawabe A., Miyashita N.T.
    Genetics 153:1445-1453(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS.
    Strain: cv. Aa-0, cv. Al-0, cv. Bl-1, cv. Bla-10, cv. Bs-1, cv. Chi-0, cv. Ci-0, cv. Es-0, cv. Gr-1, cv. Hiroshima, cv. Ita-0, cv. Kn-0, cv. Mt-0, cv. Pog-0, cv. Shokei and cv. Yo-0.
  3. "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
    Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
    DNA Res. 7:217-221(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-335.
    Strain: cv. Columbia.
  7. "Purification and characterization of an antifungal chitinase from Arabidopsis thaliana."
    Verburg J.G., Huynh Q.K.
    Plant Physiol. 95:450-455(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 237-256, ANTIFUNGAL ACTIVITY.
  8. "Analysis of ethylene signal-transduction kinetics associated with seedling-growth response and chitinase induction in wild-type and mutant Arabidopsis."
    Chen Q.G., Bleecker A.B.
    Plant Physiol. 108:597-607(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Separate jasmonate-dependent and salicylate-dependent defense-response pathways in Arabidopsis are essential for resistance to distinct microbial pathogens."
    Thomma B.P.H.J., Eggermont K., Penninckx I.A.M.A., Mauch-Mani B., Vogelsang R., Cammue B.P.A., Broekaert W.F.
    Proc. Natl. Acad. Sci. U.S.A. 95:15107-15111(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  10. "Rhizobacteria-mediated induced systemic resistance (ISR) in Arabidopsis is not associated with a direct effect on expression of known defense-related genes but stimulates the expression of the jasmonate-inducible gene Atvsp upon challenge."
    van Wees S.C., Luijendijk M., Smoorenburg I., van Loon L.C., Pieterse C.M.
    Plant Mol. Biol. 41:537-549(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "An in vivo expression system for the identification of cargo proteins of vacuolar sorting receptors in Arabidopsis culture cells."
    Shen J., Suen P.K., Wang X., Lin Y., Lo S.W., Rojo E., Jiang L.
    Plant J. 75:1003-1017(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCHIB_ARATH
AccessioniPrimary (citable) accession number: P19171
Secondary accession number(s): Q9S7J5
, Q9S838, Q9SXJ2, Q9SXJ3, Q9SXJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: August 30, 2005
Last modified: April 1, 2015
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.