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Protein

Chitinase 3

Gene

CHT3

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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei157Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

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

GO - Biological processi

  • cellular bud site selection Source: CGD
  • chitin catabolic process Source: UniProtKB-KW
  • 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.
mycoCLAPiCHI18C_CANAL.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitinase 3 (EC:3.2.1.14)
Gene namesi
Name:CHT3
Ordered Locus Names:CAALFM_CR10110WA
ORF Names:CaO19.7586
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Chromosome R

Organism-specific databases

CGDiCAL0000194074. CHT3.
EuPathDBiFungiDB:CR_10110W_A.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Leads to strong decrease of secreted chitinase activity, as well as to the clumping or clusterings of cells from early exponential phase.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_000001192617 – 567Chitinase 3Add BLAST551

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi159N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP40954.

Expressioni

Inductioni

Expression is positively regulated by ACE2. Transcription is greater during growth of the yeast form as compared to the mycelial form, and down-regulated by micafungin treatment.3 Publications

Structurei

3D structure databases

ProteinModelPortaliP40954.
SMRiP40954.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi319 – 555Ser/Thr-richAdd BLAST237

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP40954.
KOiK01183.
OrthoDBiEOG092C49QH.

Family and domain databases

InterProiView protein in InterPro
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
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.

P40954-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYLLTIFSL LLPALAINAR SNSNVAVYWG QNSGGSQQRL SYYCDSDAVD
60 70 80 90 100
IVILSFMHQF PSPIQLNFAN ACEGTYTANG ILQCQTIAED IKYCQNKGKT
110 120 130 140 150
ILLSLGGAAG SYGFSDDATA KQFAHTLWDL FGNSKNLATN DRPFYDAVLD
160 170 180 190 200
GFDFDIENNW STGYPALATE LRTLFQKDTS KNYYLGAAPQ CPYPDASVGP
210 220 230 240 250
LLKQSEIDFV FIQFYNNYCN LGSSSFNWDT WLNYAETDSP NKNIKLFVGV
260 270 280 290 300
PASSRAAGSG YNDPSAVSQY LTSDILNSKY FGGISMWDVS AGWSNTNSNG
310 320 330 340 350
NFVENMKAIV KKASPGEETT SSSTTTTTTT TSTTISSSSS SSKTSKTSTT
360 370 380 390 400
STTSSSISST TSSTTSSTSS SSTSSSTSST TSSSTTSSQI STTSTAPTSS
410 420 430 440 450
TSLSSSTIST SASTSDTTSV TSSETTPVVT PSSLSSAITI PGDSTTTGIS
460 470 480 490 500
KSSSTKPATS TTSALSSSTT TVATIPDDKE IINTPTDTET TSKPPAIITE
510 520 530 540 550
SDATTITQNL TPSTTTKNVK TTSTNIVTEW VWAPTTLRTL TTTYQILTTR
560
THIETVFAEP STVVIYN
Length:567
Mass (Da):60,061
Last modified:November 1, 1995 - v2
Checksum:iDD843126F65E22C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15801 Genomic DNA. Translation: AAA68016.1.
CP017630 Genomic DNA. Translation: AOW31663.1.
RefSeqiXP_719348.1. XM_714255.1.

Genome annotation databases

EnsemblFungiiAOW31663; AOW31663; CAALFM_CR10110WA.
GeneIDi3638967.
KEGGical:CAALFM_CR10110WA.

Similar proteinsi

Entry informationi

Entry nameiCHI3_CANAL
AccessioniPrimary (citable) accession number: P40954
Secondary accession number(s): A0A1D8PU43, Q5ACQ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: November 22, 2017
This is version 107 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