CHI2_CANAL
ID CHI2_CANAL Reviewed; 583 AA.
AC P40953; A0A1D8PNW0; Q5AKC5; Q5AKT9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Chitinase 2;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=CHT2; OrderedLocusNames=CAALFM_C504130CA;
GN ORFNames=CaO19.11376, CaO19.3895;
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], INDUCTION, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
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=12455696; DOI=10.1128/ec.1.5.787-798.2002;
RA Bensen E.S., Filler S.G., Berman J.;
RT "A forkhead transcription factor is important for true hyphal as well as
RT yeast morphogenesis in Candida albicans.";
RL Eukaryot. Cell 1:787-798(2002).
RN [6]
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 [7]
RP INDUCTION.
RX PubMed=16839200; DOI=10.1371/journal.ppat.0020063;
RA Nobile C.J., Andes D.R., Nett J.E., Smith F.J., Yue F., Phan Q.T.,
RA Edwards J.E., Filler S.G., Mitchell A.P.;
RT "Critical role of Bcr1-dependent adhesins in C. albicans biofilm formation
RT in vitro and in vivo.";
RL PLoS Pathog. 2:E63-E63(2006).
RN [8]
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 [9]
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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND PROTEOLYTIC
RP CLEAVAGE BYSAP9 AND SAP10.
RX PubMed=21097664; DOI=10.1128/ec.00210-10;
RA Schild L., Heyken A., de Groot P.W., Hiller E., Mock M., de Koster C.,
RA Horn U., Rupp S., Hube B.;
RT "Proteolytic cleavage of covalently linked cell wall proteins by Candida
RT albicans Sap9 and Sap10.";
RL Eukaryot. Cell 10:98-109(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21622905; DOI=10.1128/ec.05011-11;
RA Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S., de Koster C.G.,
RA de Koning L.J., Klis F.M.;
RT "Effects of fluconazole on the secretome, the wall proteome, and wall
RT integrity of the clinical fungus Candida albicans.";
RL Eukaryot. Cell 10:1071-1081(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=20864472; DOI=10.1099/mic.0.044206-0;
RA Sosinska G.J., de Koning L.J., de Groot P.W., Manders E.M., Dekker H.L.,
RA Hellingwerf K.J., de Koster C.G., Klis F.M.;
RT "Mass spectrometric quantification of the adaptations in the wall proteome
RT of Candida albicans in response to ambient pH.";
RL Microbiology 157:136-146(2011).
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:7708682}.
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, cell wall. Membrane; Lipid-anchor, GPI-
CC anchor.
CC -!- INDUCTION: Expression is positively regulated by BCR1 and FKH2.
CC Transcription is greater during growth of the yeast form as compared to
CC the mycelial form, and down-regulated by micafungin treatment.
CC {ECO:0000269|PubMed:12455696, ECO:0000269|PubMed:16839200,
CC ECO:0000269|PubMed:20859005, ECO:0000269|PubMed:7708682}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC {ECO:0000269|PubMed:21097664}.
CC -!- PTM: Proteolytic cleavage by SAP9 and SAP10 leads to the cell wall
CC release of CHT2 and increased chitinase activity, suggesting a direct
CC influence of SAP9 and SAP10 on CHT2 function.
CC {ECO:0000269|PubMed:21097664}.
CC -!- DISRUPTION PHENOTYPE: Leads to the clumping or clusterings of cells
CC from early exponential phase, and to increased hyphal growth on solid
CC media. {ECO:0000269|PubMed:16214381, ECO:0000269|PubMed:7708682}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U15800; AAA68015.1; -; Genomic_DNA.
DR EMBL; CP017627; AOW29822.1; -; Genomic_DNA.
DR RefSeq; XP_721807.2; XM_716714.2.
DR AlphaFoldDB; P40953; -.
DR SMR; P40953; -.
DR STRING; 237561.P40953; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CLAE; CHI18B_CANAL; -.
DR GeneID; 3636523; -.
DR KEGG; cal:CAALFM_C504130CA; -.
DR CGD; CAL0000190954; CHT2.
DR VEuPathDB; FungiDB:C5_04130C_A; -.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_007818_7_2_1; -.
DR InParanoid; P40953; -.
DR OrthoDB; 923272at2759; -.
DR PRO; PR:P40953; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; ISS:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
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:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
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; IPR025928; Flocculin_t3_rpt.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13928; Flocculin_t3; 1.
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; Cell wall; Chitin degradation; Chitin-binding;
KW Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..560
FT /note="Chitinase 2"
FT /id="PRO_0000011925"
FT PROPEP 561..583
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429923"
FT DOMAIN 23..305
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT LIPID 560
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 47
FT /note="A -> T (in Ref. 1; AAA68015)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="I -> V (in Ref. 1; AAA68015)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="A -> T (in Ref. 1; AAA68015)"
FT /evidence="ECO:0000305"
FT CONFLICT 460..462
FT /note="SVK -> PVQ (in Ref. 1; AAA68015)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="S -> A (in Ref. 1; AAA68015)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="T -> P (in Ref. 1; AAA68015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 60815 MW; E0D1E48662CF37AF CRC64;
MLSFKSLLAA AVVASSALAS ASNQVALYWG QNGAGGQERL AQYCQEADVD IILLSFLNLF
PDPLNVNFAN QCGNTFESGL LHCSQIGADI KTCQSLGKTV LLSLGGGVGD YGFSDVASAT
KFADTLWNKF GAGEDPERPF DDAVVDGFDF DIEHGGATGY PELATALRGK FAKDTSKNYF
LSAAPQCPYP DASLGDLLSK VPLDFAFIQF YNNYCSINGQ FNYDTWSKFA DSAPNKNIKL
FVGVPATSNI AGYVDTSKLS SAIEEIKCDS HFAGVSLWDA SGAWLNTDEK GENFVVQVKN
VLNQNACVAP SSSATTQSTT TTSSAVTQST TTTSAAITQS ATTTSAAVAT KSNQIVTSSS
SSSSSIFYGN STTESSTGIA TGTVLPTGSN ENAATTGSGS NTKLAISTVT DVQKTVITIT
SCSEHKCVAT PVTTGVVVVT DIDTVYTTYC PLTNSQVYVS VKTVVCTEET CVPSPTSTSQ
KPKASTTIKG VEKGQTTSYP VVGTTEGVKK IVTTSAQTVG SSTKYVTIEL TSTITPVTYP
TSVASNGTNT TVPVFTFEGG AAVANSLNSV WFTVPFLLAA FAF
