CHI3_CANAL
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 25-MAY-2022, entry version 126.
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; Saccharomycetes;
OC Saccharomycetales; 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 STRING; 237561.P40954; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CLAE; CHI18C_CANAL; -.
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; 923272at2759; -.
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:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IDA:CGD.
DR GO; GO:0000282; P:cellular bud site selection; IMP:CGD.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; SSF51445; 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 315..471
FT /note="Polar residues"
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
