ID   CHI3_CANAL              Reviewed;         567 AA.
AC   P40954; A0A1D8PU43; Q5ACQ6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   02-SEP-2026, entry version 140.
DE   RecName: Full=Chitinase 3;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHT3; OrderedLocusNames=CAALFM_CR10110WA; ORFNames=CaO19.7586;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061;
RX   PubMed=7708682; DOI=10.1073/pnas.92.7.2544;
RA   McCreath K.J., Specht C.A., Robbins P.W.;
RT   "Molecular cloning and characterization of chitinase genes from Candida
RT   albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:2544-2548(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [5]
RP   INDUCTION.
RX   PubMed=15255906; DOI=10.1111/j.1365-2958.2004.04185.x;
RA   Kelly M.T., MacCallum D.M., Clancy S.D., Odds F.C., Brown A.J., Butler G.;
RT   "The Candida albicans CaACE2 gene affects morphogenesis, adherence and
RT   virulence.";
RL   Mol. Microbiol. 53:969-983(2004).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=16214381; DOI=10.1016/j.fgb.2005.08.001;
RA   Dunkler A., Walther A., Specht C.A., Wendland J.;
RT   "Candida albicans CHT3 encodes the functional homolog of the Cts1 chitinase
RT   of Saccharomyces cerevisiae.";
RL   Fungal Genet. Biol. 42:935-947(2005).
RN   [7]
RP   INDUCTION.
RX   PubMed=20859005;
RA   Kaneko Y., Ohno H., Kohno S., Miyazaki Y.;
RT   "Micafungin alters the expression of genes related to cell wall integrity
RT   in Candida albicans biofilms.";
RL   Jpn. J. Infect. Dis. 63:355-357(2010).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=20641015; DOI=10.1002/yea.1775;
RA   Sorgo A.G., Heilmann C.J., Dekker H.L., Brul S., de Koster C.G., Klis F.M.;
RT   "Mass spectrometric analysis of the secretome of Candida albicans.";
RL   Yeast 27:661-672(2010).
CC   -!- FUNCTION: Chitinase involved in the remodeling of chitin in the fungal
CC       cell wall. Plays a role in cell separation.
CC       {ECO:0000269|PubMed:16214381}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC         (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC         Evidence={ECO:0000269|PubMed:16214381};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20641015}.
CC   -!- INDUCTION: Expression is positively regulated by ACE2. Transcription is
CC       greater during growth of the yeast form as compared to the mycelial
CC       form, and down-regulated by micafungin treatment.
CC       {ECO:0000269|PubMed:15255906, ECO:0000269|PubMed:20859005,
CC       ECO:0000269|PubMed:7708682}.
CC   -!- DISRUPTION PHENOTYPE: Leads to strong decrease of secreted chitinase
CC       activity, as well as to the clumping or clusterings of cells from early
CC       exponential phase. {ECO:0000269|PubMed:16214381}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class III subfamily. {ECO:0000305}.
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DR   EMBL; U15801; AAA68016.1; -; Genomic_DNA.
DR   EMBL; CP017630; AOW31663.1; -; Genomic_DNA.
DR   RefSeq; XP_719348.1; XM_714255.1.
DR   AlphaFoldDB; P40954; -.
DR   SMR; P40954; -.
DR   FunCoup; P40954; 175.
DR   STRING; 237561.P40954; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GlyCosmos; P40954; 1 site, No reported glycans.
DR   PaxDb; 237561-P40954; -.
DR   EnsemblFungi; CR_10110W_A-T; CR_10110W_A-T-p1; CR_10110W_A.
DR   GeneID; 3638967; -.
DR   KEGG; cal:CAALFM_CR10110WA; -.
DR   CGD; CAL0000194074; CHT3.
DR   VEuPathDB; FungiDB:CR_10110W_A; -.
DR   eggNOG; KOG4701; Eukaryota.
DR   HOGENOM; CLU_007818_7_0_1; -.
DR   InParanoid; P40954; -.
DR   OMA; GTTCFAY; -.
DR   OrthoDB; 6020543at2759; -.
DR   BRENDA; 3.2.1.14; 1096.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0009986; C:cell surface; IDA:CGD.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
DR   GO; GO:0004568; F:chitinase activity; IDA:CGD.
DR   GO; GO:0008843; F:endochitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0098743; P:cell aggregation; IMP:CGD.
DR   GO; GO:0000282; P:cellular bud site selection; IMP:CGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR   CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR   FunFam; 3.20.20.80:FF:000125; CTS1p Endochitinase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR045321; Cts1-like.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR   PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..567
FT                   /note="Chitinase 3"
FT                   /id="PRO_0000011926"
FT   DOMAIN          23..313
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          313..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..436
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..471
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        157
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   567 AA;  60061 MW;  DD843126F65E22C2 CRC64;
     MLYLLTIFSL LLPALAINAR SNSNVAVYWG QNSGGSQQRL SYYCDSDAVD IVILSFMHQF
     PSPIQLNFAN ACEGTYTANG ILQCQTIAED IKYCQNKGKT ILLSLGGAAG SYGFSDDATA
     KQFAHTLWDL FGNSKNLATN DRPFYDAVLD GFDFDIENNW STGYPALATE LRTLFQKDTS
     KNYYLGAAPQ CPYPDASVGP LLKQSEIDFV FIQFYNNYCN LGSSSFNWDT WLNYAETDSP
     NKNIKLFVGV PASSRAAGSG YNDPSAVSQY LTSDILNSKY FGGISMWDVS AGWSNTNSNG
     NFVENMKAIV KKASPGEETT SSSTTTTTTT TSTTISSSSS SSKTSKTSTT STTSSSISST
     TSSTTSSTSS SSTSSSTSST TSSSTTSSQI STTSTAPTSS TSLSSSTIST SASTSDTTSV
     TSSETTPVVT PSSLSSAITI PGDSTTTGIS KSSSTKPATS TTSALSSSTT TVATIPDDKE
     IINTPTDTET TSKPPAIITE SDATTITQNL TPSTTTKNVK TTSTNIVTEW VWAPTTLRTL
     TTTYQILTTR THIETVFAEP STVVIYN
//