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P21226

- CHI2_PEA

UniProt

P21226 - CHI2_PEA

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Protein

Endochitinase A2

Gene

CHI2

Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Defense against chitin containing fungal pathogens.

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 Source: UniProtKB-KW
  4. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Endochitinase A2 (EC:3.2.1.14)
Gene namesi
Name:CHI2
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 309289Endochitinase A2PRO_0000005308Add
BLAST
Propeptidei310 – 32415Removed in mature formBy similarityPRO_0000005309Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 ↔ 38PROSITE-ProRule annotation
Disulfide bondi32 ↔ 44PROSITE-ProRule annotation
Disulfide bondi37 ↔ 51PROSITE-ProRule annotation
Disulfide bondi55 ↔ 59PROSITE-ProRule annotation
Disulfide bondi151 ↔ 170PROSITE-ProRule annotation
Disulfide bondi269 ↔ 301PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By infection with the fungal pathogen Ascochyta pisi.

Structurei

3D structure databases

ProteinModelPortaliP21226.
SMRiP21226. Positions 21-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 6141Chitin-binding type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

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.
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.

P21226-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKLRIPILL VLFIVSCCSA EQCGTQAGGA LCPGGLCCSK FGWCGSTSEY
60 70 80 90 100
CGDGCQSQCS GSSGGGTLSS LISGDTFNNM LKHRNDNACQ GKPFYTYDAF
110 120 130 140 150
LSAAKAFPNF ANKGDTATKK REIAAFLGQT SHETTGGWPT APDGPYAWGY
160 170 180 190 200
CFLREQNPST YCQASSEFPC ASGKQYYGRG PIQISWNYNY GQCGRAIGVD
210 220 230 240 250
LLNNPDLVAT DPVISFKTAL WFWMTPQSPK PSCHDVITGG WTPSSADRAA
260 270 280 290 300
GRLPGYGTVT NIINGGLECG RGQDSRVQDR IGFYKRYCDI FGIGYGDNLD
310 320
CYSQRPFGSS LPLSSILLDT VAAA
Length:324
Mass (Da):34,678
Last modified:October 1, 1996 - v2
Checksum:i540F0DA5EC1DC2FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37876 Genomic DNA. Translation: AAA75196.1.
PIRiS56694.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37876 Genomic DNA. Translation: AAA75196.1 .
PIRi S56694.

3D structure databases

ProteinModelPortali P21226.
SMRi P21226. Positions 21-307.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.30.60.10. 1 hit.
InterProi IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view ]
PIRSFi PIRSF001060. Endochitinase. 1 hit.
PRINTSi PR00451. CHITINBINDNG.
SMARTi SM00270. ChtBD1. 1 hit.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEi PS00026. 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 ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and characterization of a pea chitinase gene expressed in response to wounding, fungal infection and the elicitor chitosan."
    Chang M.M., Horovitz D., Culley D., Hadwiger L.A.
    Plant Mol. Biol. 28:105-111(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Alcan.
  2. "Induction, purification and characterization of chitinase isolated from pea leaves inoculated with Ascochyta pisi."
    Vad K., Mikkelsen J.D., Collinge D.B.
    Planta 184:24-29(1991)
    Cited for: PROTEIN SEQUENCE OF 21-36.
    Strain: cv. Birte.
    Tissue: Leaf.

Entry informationi

Entry nameiCHI2_PEA
AccessioniPrimary (citable) accession number: P21226
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 1, 1996
Last modified: October 1, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3