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Protein

Chitinase 2

Gene

CHT2

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Chitinase involved in the remodeling of chitin in the fungal cell wall. Plays a role in cell separation.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei153Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

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

GO - Biological processi

  • cellular response to starvation Source: CGD
  • chitin catabolic process Source: UniProtKB-KW
  • filamentous growth Source: CGD
  • filamentous growth of a population of unicellular organisms Source: CGD
  • filamentous growth of a population of unicellular organisms in response to starvation Source: CGD
  • polysaccharide catabolic process Source: UniProtKB-KW

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Chitin degradation, Polysaccharide degradation
LigandChitin-binding

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.
mycoCLAPiCHI18B_CANAL.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitinase 2 (EC:3.2.1.14)
Gene namesi
Name:CHT2
Ordered Locus Names:CAALFM_C504130CA
ORF Names:CaO19.11376, CaO19.3895
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Chromosome 5

Organism-specific databases

CGDiCAL0000190954. CHT2.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • cell surface Source: CGD
  • extracellular region Source: CGD
  • fungal-type cell wall Source: CGD
  • yeast-form cell wall Source: CGD

Keywords - Cellular componenti

Cell wall, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Leads to the clumping or clusterings of cells from early exponential phase, and to increased hyphal growth on solid media.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001192520 – 560Chitinase 2Add BLAST541
PropeptideiPRO_0000429923561 – 583Removed in mature formSequence analysisAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi370N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi546N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi549N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi560GPI-anchor amidated glycineSequence analysis1

Post-translational modificationi

The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.1 Publication
Proteolytic cleavage by SAP9 and SAP10 leads to the cell wall release of CHT2 and increased chitinase activity, suggesting a direct influence of SAP9 and SAP10 on CHT2 function.1 Publication

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PRIDEiP40953.

Expressioni

Inductioni

Expression is positivelay regulated by BCR1 and FKH2. Transcription is greater during growth of the yeast form as compared to the mycelial form, and down-regulated by micafungin treatment.4 Publications

Structurei

3D structure databases

ProteinModelPortaliP40953.
SMRiP40953.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi315 – 556Ser/Thr-richAdd BLAST242

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP40953.
KOiK01183.
OrthoDBiEOG092C49QH.

Family and domain databases

InterProiView protein in InterPro
IPR025928. Flocculin_t3_rpt.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
PF13928. Flocculin_t3. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiView protein in PROSITE
PS01095. CHITINASE_18. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P40953-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSFKSLLAA AVVASSALAS ASNQVALYWG QNGAGGQERL AQYCQEADVD
60 70 80 90 100
IILLSFLNLF PDPLNVNFAN QCGNTFESGL LHCSQIGADI KTCQSLGKTV
110 120 130 140 150
LLSLGGGVGD YGFSDVASAT KFADTLWNKF GAGEDPERPF DDAVVDGFDF
160 170 180 190 200
DIEHGGATGY PELATALRGK FAKDTSKNYF LSAAPQCPYP DASLGDLLSK
210 220 230 240 250
VPLDFAFIQF YNNYCSINGQ FNYDTWSKFA DSAPNKNIKL FVGVPATSNI
260 270 280 290 300
AGYVDTSKLS SAIEEIKCDS HFAGVSLWDA SGAWLNTDEK GENFVVQVKN
310 320 330 340 350
VLNQNACVAP SSSATTQSTT TTSSAVTQST TTTSAAITQS ATTTSAAVAT
360 370 380 390 400
KSNQIVTSSS SSSSSIFYGN STTESSTGIA TGTVLPTGSN ENAATTGSGS
410 420 430 440 450
NTKLAISTVT DVQKTVITIT SCSEHKCVAT PVTTGVVVVT DIDTVYTTYC
460 470 480 490 500
PLTNSQVYVS VKTVVCTEET CVPSPTSTSQ KPKASTTIKG VEKGQTTSYP
510 520 530 540 550
VVGTTEGVKK IVTTSAQTVG SSTKYVTIEL TSTITPVTYP TSVASNGTNT
560 570 580
TVPVFTFEGG AAVANSLNSV WFTVPFLLAA FAF
Length:583
Mass (Da):60,815
Last modified:March 15, 2017 - v2
Checksum:iE0D1E48662CF37AF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti47A → T in AAA68015 (PubMed:7708682).Curated1
Sequence conflicti52I → V in AAA68015 (PubMed:7708682).Curated1
Sequence conflicti349A → T in AAA68015 (PubMed:7708682).Curated1
Sequence conflicti460 – 462SVK → PVQ in AAA68015 (PubMed:7708682).Curated3
Sequence conflicti479S → A in AAA68015 (PubMed:7708682).Curated1
Sequence conflicti573T → P in AAA68015 (PubMed:7708682).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15800 Genomic DNA. Translation: AAA68015.1.
CP017627 Genomic DNA. Translation: AOW29822.1.
RefSeqiXP_721807.2. XM_716714.2.

Genome annotation databases

GeneIDi3636523.
KEGGical:CAALFM_C504130CA.

Similar proteinsi

Entry informationi

Entry nameiCHI2_CANAL
AccessioniPrimary (citable) accession number: P40953
Secondary accession number(s): A0A1D8PNW0, Q5AKC5, Q5AKT9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: March 15, 2017
Last modified: August 30, 2017
This is version 113 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: 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