ID   CHI1_CANAL              Reviewed;         462 AA.
AC   Q5AAH2; A0A1D8PRM1;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Chitinase 1;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHT1; OrderedLocusNames=CAALFM_CR00180CA; ORFNames=CaO19.7517;
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 [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   [2]
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   [3]
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   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12456000; DOI=10.1128/ec.1.4.514-525.2002;
RA   Monteoliva L., Matas M.L., Gil C., Nombela C., Pla J.;
RT   "Large-scale identification of putative exported proteins in Candida
RT   albicans by genetic selection.";
RL   Eukaryot. Cell 1:514-525(2002).
RN   [5]
RP   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   [6]
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   [7]
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   -!- 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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12456000,
CC       ECO:0000269|PubMed:20641015}.
CC   -!- INDUCTION: Transcription is greater during growth of the yeast form as
CC       compared to the mycelial form and up-regulated by micafungin treatment.
CC       {ECO:0000269|PubMed:20859005}.
CC   -!- DISRUPTION PHENOTYPE: Leads to increased hyphal growth on solid media.
CC       {ECO:0000269|PubMed:16214381}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class V subfamily. {ECO:0000305}.
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DR   EMBL; CP017630; AOW30789.1; -; Genomic_DNA.
DR   RefSeq; XP_718674.1; XM_713581.1.
DR   AlphaFoldDB; Q5AAH2; -.
DR   SMR; Q5AAH2; -.
DR   STRING; 237561.Q5AAH2; -.
DR   GeneID; 3639704; -.
DR   KEGG; cal:CAALFM_CR00180CA; -.
DR   CGD; CAL0000179750; CHT1.
DR   VEuPathDB; FungiDB:CR_00180C_A; -.
DR   HOGENOM; CLU_007818_7_2_1; -.
DR   InParanoid; Q5AAH2; -.
DR   OMA; TETCNTG; -.
DR   OrthoDB; 923272at2759; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
DR   GO; GO:0009277; C:fungal-type cell wall; IEA:EnsemblFungi.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; ISS:CGD.
DR   GO; GO:0008843; F:endochitinase activity; IEA:EnsemblFungi.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000920; P:septum digestion after cytokinesis; IEA:EnsemblFungi.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..462
FT                   /note="Chitinase 1"
FT                   /id="PRO_0000429924"
FT   DOMAIN          18..291
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   462 AA;  48890 MW;  7689BEB6BAE000A0 CRC64;
     MILNLIILLA ISIVASASNI AAYWGQNAGG DQQTLGDYCS SSPASIIILS FLDGFPNLSL
     NFANQCSGTF SSGLAHCSQI GSDIKSCQQQ GKTILLSLGG ATGNYGFSSD SEAVQFAGTL
     WNKFGGGKDS ERPFDDAIVD GFDFDIENKD QTGYAALATQ LRKYFSTGTK SYYLSAAPQC
     PYPDESVGDL MSQVDLDFAF IQFYNNYCSL NQQFNWNSWS NYARGKSIKL YLGLPGSSSS
     AGSGFVGLST VQRVVASIKG DSSFGGISIW DISSAENGGY LNQLHQALSG SGSPAAPSNS
     YQPNTPLTRT YGGSTATASA YISVGFTAGA THGSTTTNDL LAWIDSLFGS SQSSVQQYAT
     PVQSVTATPQ PVAATTTSAP KPTASAFNWF GWFDGTTTST TLQTVYSTVP ADQTVYVTLT
     TTVGSQMLQS LFDKRDVIAE AKSTNLQICW LLFIPLLALI CS