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Protein

Endochitinase

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (EC:3.2.1.14)
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115 Componenti: Unplaced

Subcellular locationi

Vacuole By similarity
Note: Vacuolar and protoplast.By similarity

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 – 2626Add
BLAST
Chaini27 – 321295EndochitinasePRO_0000005327Add
BLAST
Propeptidei322 – 3287Removed in mature formCuratedPRO_0000005328

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 44PROSITE-ProRule annotation
Disulfide bondi38 ↔ 50PROSITE-ProRule annotation
Disulfide bondi43 ↔ 57PROSITE-ProRule annotation
Disulfide bondi62 ↔ 66PROSITE-ProRule annotation
Disulfide bondi100 ↔ 162PROSITE-ProRule annotation
Disulfide bondi174 ↔ 182PROSITE-ProRule annotation
Disulfide bondi281 ↔ 313PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By ethylene.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P3Zmodel-A1-328[»]
ProteinModelPortaliP05315.
SMRiP05315. Positions 27-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 6842Chitin-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.
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.

P05315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRHKEVNFV AYLLFSLLVL VSAALAQNCG SQGGGKACAS GQCCSKFGWC
60 70 80 90 100
GNTNDYCGSG NCQSQCPGGG PGPGPGGDLG SAISNSMFDQ MLKHRNENSC
110 120 130 140 150
QGKNFYSYNA FINAARSFPG FGTSGDINAR KREIAAFFAQ TSHETTGGWA
160 170 180 190 200
SAPDGPYAWG YCFLRERGNP GDYCPPSSQW PCAPGRKYFG RGPIQISHNY
210 220 230 240 250
NYGPCGRAIG VDLLNNPDLV ATDPVISFKT ALWFWMTPQS PKPSCHDVII
260 270 280 290 300
GRWNPSSADR AANRLPGFGV ITNIINGGLE CGRGTDNRVQ DRIGFYRRYC
310 320
SILGVTPGDN LDCVNQRWFG NALLVDTL
Length:328
Mass (Da):35,407
Last modified:November 1, 1988 - v1
Checksum:i669B82159BC176EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07130 mRNA. Translation: CAA30142.1.
X15494 Genomic DNA. Translation: CAA33517.1.
PIRiS05426.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07130 mRNA. Translation: CAA30142.1.
X15494 Genomic DNA. Translation: CAA33517.1.
PIRiS05426.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P3Zmodel-A1-328[»]
ProteinModelPortaliP05315.
SMRiP05315. Positions 27-320.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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

  1. "Primary structure of an endochitinase mRNA from Solanum tuberosum."
    Gaynor J.J.
    Nucleic Acids Res. 16:5210-5210(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Russet Burbank-0.
    Tissue: Leaf.
  2. "Sequence analysis of a genomic clone encoding an endochitinase from Solanum tuberosum."
    Gaynor J.J., Unkenholz K.M.
    Nucleic Acids Res. 17:5855-5855(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Russet Burbank-0.
  3. "Endochitinase [precursor] function as a defense against chitin containing fungal pathogens."
    Rao G.S.
    Submitted (APR-2003) to the PDB data bank
    Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiCHIT_SOLTU
AccessioniPrimary (citable) accession number: P05315
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: January 7, 2015
This is version 109 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.