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Protein

Endochitinase EP3

Gene

EP3

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

Functioni

Probably involved in hypersensitive reaction upon Xanthomonas campestris infection.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 4.8.1 Publication

GO - Molecular functioni

  • chitinase activity Source: TAIR
  • chitin binding Source: UniProtKB-KW

GO - Biological processi

  • cell wall macromolecule catabolic process Source: InterPro
  • chitin catabolic process Source: UniProtKB-KW
  • defense response Source: UniProtKB-KW
  • polysaccharide catabolic process Source: UniProtKB-KW
  • response to bacterium Source: UniProtKB
  • response to wounding Source: UniProtKB
  • somatic embryogenesis Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Enzyme and pathway databases

BioCyciARA:AT3G54420-MONOMER.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Endochitinase EP31 Publication (EC:3.2.1.14)
Alternative name(s):
Chitinase class IV1 Publication
Short name:
AtchitIV1 Publication
Protein HOMOLOG OF CARROT EP3-3 CHITINASE1 Publication
Short name:
AtEP31 Publication
Gene namesi
Name:EP31 Publication
Synonyms:CHIV1 Publication
Ordered Locus Names:At3g54420Imported
ORF Names:T12E18.110Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G54420.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 273245Endochitinase EP3Sequence analysisPRO_0000433911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi31 ↔ 39PROSITE-ProRule annotation
Disulfide bondi33 ↔ 45PROSITE-ProRule annotation
Disulfide bondi38 ↔ 52PROSITE-ProRule annotation
Glycosylationi47 – 471N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi56 ↔ 61PROSITE-ProRule annotation
Glycosylationi157 – 1571N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi270 – 2701N-linked (GlcNAc...)PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9M2U5.
PRIDEiQ9M2U5.

Expressioni

Tissue specificityi

Expressed in cells surrounding embryos, stems, seedlings, pollen, roots, shoots, inflorescence, flowers, siliques and leaves (PubMed:11525512, PubMed:19420714). Present in seedpods and seed embryos, but not in roots, inflorescence stems, leaves and flowers (PubMed:9426222).3 Publications

Developmental stagei

Expressed during somatic embryogenesis in nursing cells surrounding the embryos but not in embryos. Accumulates in mature pollen and growing pollen tubes until they enter the receptive synergid, but not in endosperm and integuments. In adult plants, present in hydathodes, stipules, root epidermis and emerging root hairs.1 Publication

Inductioni

Accumulates rapidly and transiently in leaves after inoculation with Xanthomonas campestris (PubMed:9426222). Slightly repressed by wounding (PubMed:19420714).2 Publications

Gene expression databases

GenevisibleiQ9M2U5. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G54420.1.

Structurei

3D structure databases

ProteinModelPortaliQ9M2U5.
SMRiQ9M2U5. Positions 75-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 6335Chitin-binding type-1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 273204CatalyticBy similarityAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4742. Eukaryota.
COG3979. LUCA.
HOGENOMiHOG000231411.
InParanoidiQ9M2U5.
KOiK01183.
OMAiGNTSDYC.
PhylomeDBiQ9M2U5.

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. 2 hits.
[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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9M2U5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTPTISKSI SLVTILLVLQ AFSNTTKAQN CGCSSELCCS QFGFCGNTSD
60 70 80 90 100
YCGVGCQQGP CFAPPPANGV SVAEIVTQEF FNGIISQAAS SCAGNRFYSR
110 120 130 140 150
GAFLEALDSY SRFGRVGSTD DSRREIAAFF AHVTHETGHF CYIEEIDGAS
160 170 180 190 200
KDYCDENATQ YPCNPNKGYY GRGPIQLSWN FNYGPAGTAI GFDGLNAPET
210 220 230 240 250
VATDPVISFK TALWYWTNRV QPVISQGFGA TIRAINGALE CDGANTATVQ
260 270
ARVRYYTDYC RQLGVDPGNN LTC
Length:273
Mass (Da):29,436
Last modified:October 1, 2000 - v1
Checksum:i1DB0A002F4EF44EC
GO

Sequence cautioni

The sequence CAA81243.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391H → RN in CAA74930 (PubMed:9426222).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14590 Genomic DNA. Translation: CAA74930.1.
AL132971 Genomic DNA. Translation: CAB81807.1.
CP002686 Genomic DNA. Translation: AEE79228.1.
BT010422 mRNA. Translation: AAQ62423.1.
AK176488 mRNA. Translation: BAD44251.1.
Z26409 mRNA. Translation: CAA81243.1. Different initiation.
PIRiT47601.
RefSeqiNP_191010.1. NM_115302.2.
UniGeneiAt.35109.

Genome annotation databases

EnsemblPlantsiAT3G54420.1; AT3G54420.1; AT3G54420.
GeneIDi824608.
GrameneiAT3G54420.1; AT3G54420.1; AT3G54420.
KEGGiath:AT3G54420.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14590 Genomic DNA. Translation: CAA74930.1.
AL132971 Genomic DNA. Translation: CAB81807.1.
CP002686 Genomic DNA. Translation: AEE79228.1.
BT010422 mRNA. Translation: AAQ62423.1.
AK176488 mRNA. Translation: BAD44251.1.
Z26409 mRNA. Translation: CAA81243.1. Different initiation.
PIRiT47601.
RefSeqiNP_191010.1. NM_115302.2.
UniGeneiAt.35109.

3D structure databases

ProteinModelPortaliQ9M2U5.
SMRiQ9M2U5. Positions 75-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G54420.1.

Protein family/group databases

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

Proteomic databases

PaxDbiQ9M2U5.
PRIDEiQ9M2U5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G54420.1; AT3G54420.1; AT3G54420.
GeneIDi824608.
GrameneiAT3G54420.1; AT3G54420.1; AT3G54420.
KEGGiath:AT3G54420.

Organism-specific databases

TAIRiAT3G54420.

Phylogenomic databases

eggNOGiKOG4742. Eukaryota.
COG3979. LUCA.
HOGENOMiHOG000231411.
InParanoidiQ9M2U5.
KOiK01183.
OMAiGNTSDYC.
PhylomeDBiQ9M2U5.

Enzyme and pathway databases

BioCyciARA:AT3G54420-MONOMER.

Miscellaneous databases

PROiQ9M2U5.

Gene expression databases

GenevisibleiQ9M2U5. AT.

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. 2 hits.
[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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Arabidopsis thaliana class IV chitinase is early induced during the interaction with Xanthomonas campestris."
    Gerhardt L.B.A., Sachetto-Martins G., Contarini M.G., Sandroni M., Ferreira R.P., de Lima V.M., Cordeiro M.C., de Oliveira D.E., Margis-Pinheiro M.
    FEBS Lett. 419:69-75(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION BY XANTHOMONAS CAMPESTRIS.
    Strain: cv. Columbia.
  2. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "The Arabidopsis thaliana transcribed genome: the GDR cDNA program."
    Philipps G., Gigot C.
    Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-72.
  7. "Expression pattern of the Arabidopsis thaliana AtEP3/AtchitIV endochitinase gene."
    Passarinho P.A., Van Hengel A.J., Fransz P.F., de Vries S.C.
    Planta 212:556-567(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY.
    Strain: cv. Columbia and cv. Landsberg erecta.
  8. "Chitinase gene expression in response to environmental stresses in Arabidopsis thaliana: chitinase inhibitor allosamidin enhances stress tolerance."
    Takenaka Y., Nakano S., Tamoi M., Sakuda S., Fukamizo T.
    Biosci. Biotechnol. Biochem. 73:1066-1071(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION BY WOUNDING.
    Strain: cv. Columbia.

Entry informationi

Entry nameiCHI5_ARATH
AccessioniPrimary (citable) accession number: Q9M2U5
Secondary accession number(s): O23248, Q42085
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2015
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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 one 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.