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Protein

Endochitinase A

Gene

CHN48

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: 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 A (EC:3.2.1.14)
Short name:
CHN-A
Gene namesi
Name:CHN48
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Subcellular locationi

Vacuole 1 Publication
Note: Vacuolar and protoplast.

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 – 2323Add
BLAST
Chaini24 – 322299Endochitinase APRO_0000005330Add
BLAST
Propeptidei323 – 3297Removed in mature formPRO_0000005331

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 41PROSITE-ProRule annotation
Disulfide bondi35 ↔ 47PROSITE-ProRule annotation
Disulfide bondi40 ↔ 54PROSITE-ProRule annotation
Disulfide bondi59 ↔ 63PROSITE-ProRule annotation
Modified residuei67 – 6714-hydroxyproline; partial1 Publication
Modified residuei69 – 6914-hydroxyproline1 Publication
Modified residuei71 – 7114-hydroxyproline1 Publication
Modified residuei72 – 7214-hydroxyproline1 Publication
Modified residuei74 – 7414-hydroxyproline1 Publication
Modified residuei75 – 7514-hydroxyproline; partial1 Publication
Disulfide bondi101 ↔ 163PROSITE-ProRule annotation
Disulfide bondi175 ↔ 183PROSITE-ProRule annotation
Disulfide bondi282 ↔ 314PROSITE-ProRule annotation

Post-translational modificationi

The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein.

Keywords - PTMi

Disulfide bond, Hydroxylation

Proteomic databases

ProMEXiP08252.

Expressioni

Developmental stagei

Expressed during flower formation.1 Publication

Inductioni

By ethylene.

Structurei

3D structure databases

ProteinModelPortaliP08252.
SMRiP08252. Positions 24-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 6542Chitin-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.

P08252-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLCKFTALS SLLFSLLLLS ASAEQCGSQA GGARCPSGLC CSKFGWCGNT
60 70 80 90 100
NDYCGPGNCQ SQCPGGPTPT PPTPPGGGDL GSIISSSMFD QMLKHRNDNA
110 120 130 140 150
CQGKGFYSYN AFINAARSFP GFGTSGDTTA RKREIAAFFA QTSHETTGGW
160 170 180 190 200
ATAPDGPYAW GYCWLREQGS PGDYCTPSGQ WPCAPGRKYF GRGPIQISHN
210 220 230 240 250
YNYGPCGRAI GVDLLNNPDL VATDPVISFK SALWFWMTPQ SPKPSCHDVI
260 270 280 290 300
IGRWQPSAGD RAANRLPGFG VITNIINGGL ECGRGTDSRV QDRIGFYRRY
310 320
CSILGVSPGD NLDCGNQRSF GNGLLVDTM
Length:329
Mass (Da):35,156
Last modified:August 1, 1990 - v2
Checksum:i3EC99D96E6C0114C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 786TPPGGG → HPTRC in AAB23374. (PubMed:2152343)Curated
Sequence conflicti263 – 2631A → S in AAB23374. (PubMed:2152343)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16938 Genomic DNA. Translation: CAA34812.1.
X16939 mRNA. Translation: CAA34813.1.
S44869 mRNA. Translation: AAB23374.1.
PIRiS08627.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16938 Genomic DNA. Translation: CAA34812.1.
X16939 mRNA. Translation: CAA34813.1.
S44869 mRNA. Translation: AAB23374.1.
PIRiS08627.

3D structure databases

ProteinModelPortaliP08252.
SMRiP08252. Positions 24-320.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Proteomic databases

ProMEXiP08252.

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. "Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain."
    Shinshi H., Neuhaus J.-M., Ryals J., Meins F. Jr.
    Plant Mol. Biol. 14:357-368(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: cv. Havana 425.
    Tissue: Leaf.
  2. "Chitinase, beta-1,3-glucanase, osmotin, and extensin are expressed in tobacco explants during flower formation."
    Neale A.D., Wahleithner J.A., Lund M., Bonnett H.T., Kelly A., Meeks-Wagner D.R., Peacock W.J., Dennis E.S.
    Plant Cell 2:673-684(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Strain: cv. Samsun.
    Tissue: Flower bud.
  3. "A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole."
    Neuhaus J.-M., Sticher L., Meins F. Jr., Boller T.
    Proc. Natl. Acad. Sci. U.S.A. 88:10362-10366(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing proteins."
    Sticher L., Hofsteenge J., Milani A., Neuhaus J.-M., Meins F. Jr.
    Science 257:655-657(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: HYDROXYLATION AT PRO-67; PRO-69; PRO-71; PRO-72; PRO-74 AND PRO-75, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCHI1_TOBAC
AccessioniPrimary (citable) accession number: P08252
Secondary accession number(s): Q41180
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1990
Last modified: January 7, 2015
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

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.