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P19171 (CHIB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Basic endochitinase B

EC=3.2.1.14
Alternative name(s):
Pathogenesis-related protein 3
Short name=AtChiB
Short name=PR-3
Gene names
Name:CHI-B
Synonyms:PR3
Ordered Locus Names:At3g12500
ORF Names:MQC3.32, T2E22.18, T2E22_119
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Catalytic activity

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

Subcellular location

Vacuole Ref.11.

Tissue specificity

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

Induction

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. Ref.1 Ref.8 Ref.9 Ref.10

Sequence similarities

Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily.

Contains 1 chitin-binding type-1 domain.

Sequence caution

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333
Chain34 – 328295Basic endochitinase B
PRO_0000005287
Propeptide329 – 3357Removed in mature form Probable
PRO_0000005288

Regions

Domain34 – 7542Chitin-binding type-1
Motif329 – 3357Vacuolar targeting signal Potential

Amino acid modifications

Disulfide bond36 ↔ 51 By similarity
Disulfide bond45 ↔ 57 By similarity
Disulfide bond50 ↔ 64 By similarity
Disulfide bond69 ↔ 73 By similarity
Disulfide bond107 ↔ 169 By similarity
Disulfide bond181 ↔ 189 By similarity
Disulfide bond288 ↔ 320 By similarity

Natural variations

Natural variant171N → K in strain: cv. Bl-1, cv. Shokei and cv. Yo-0.
Natural variant1061A → T in strain: cv. Aa-0.
Natural variant1271G → S in strain: cv. Yo-0.
Natural variant2061N → D in strain: cv. Ci-0.

Sequences

Sequence LengthMass (Da)Tools
P19171 [UniParc].

Last modified August 30, 2005. Version 3.
Checksum: 0973CE89B30ABF61

FASTA33536,184
        10         20         30         40         50         60 
MPPQKENHRT LNKMKTNLFL FLIFSLLLSL SSAEQCGRQA GGALCPNGLC CSEFGWCGNT 

        70         80         90        100        110        120 
EPYCKQPGCQ SQCTPGGTPP GPTGDLSGII SSSQFDDMLK HRNDAACPAR GFYTYNAFIT 

       130        140        150        160        170        180 
AAKSFPGFGT TGDTATRKKE VAAFFGQTSH ETTGGWATAP DGPYSWGYCF KQEQNPASDY 

       190        200        210        220        230        240 
CEPSATWPCA SGKRYYGRGP MQLSWNYNYG LCGRAIGVDL LNNPDLVAND AVIAFKAAIW 

       250        260        270        280        290        300 
FWMTAQPPKP SCHAVIAGQW QPSDADRAAG RLPGYGVITN IINGGLECGR GQDGRVADRI 

       310        320        330 
GFYQRYCNIF GVNPGGNLDC YNQRSFVNGL LEAAI 

« Hide

References

« Hide 'large scale' references
[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(1990) [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(1999) [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(2000) [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. expand/collapse author list , 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(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-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. expand/collapse author list , 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(2003) [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(1991) [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(1995) [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(1998) [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(1999) [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(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB45511.
RefSeqNP_566426.2. NM_112085.3.
UniGeneAt.296.
At.75583.

3D structure databases

ProteinModelPortalP19171.
SMRP19171. Positions 34-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid5763. 1 interaction.

Protein family/group databases

CAZyCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Proteomic databases

PaxDbP19171.
PRIDEP19171.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G12500.1; AT3G12500.1; AT3G12500.
GeneID820429.
KEGGath:AT3G12500.

Organism-specific databases

TAIRAT3G12500.

Phylogenomic databases

eggNOGCOG3979.
HOGENOMHOG000231411.
InParanoidP19171.
KOK01183.
OMACHAVIAG.
PhylomeDBP19171.

Enzyme and pathway databases

BioCycARA:AT3G12500-MONOMER.

Gene expression databases

GenevestigatorP19171.

Family and domain databases

Gene3D3.30.60.10. 1 hit.
InterProIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFPIRSF001060. Endochitinase. 1 hit.
PRINTSPR00451. CHITINBINDNG.
ProDomPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEPS00026. 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]
ProtoNetSearch...

Entry information

Entry nameCHIB_ARATH
AccessionPrimary (citable) accession number: P19171
Secondary accession number(s): Q9S7J5 expand/collapse secondary AC list , Q9S838, Q9SXJ2, Q9SXJ3, Q9SXJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: August 30, 2005
Last modified: July 9, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names