ID   CHI2_YEAST              Reviewed;         511 AA.
AC   Q06350; D6VT02;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Sporulation-specific chitinase 2;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CTS2; OrderedLocusNames=YDR371W; ORFNames=D9481.7;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
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:0000305}.
CC   -!- MISCELLANEOUS: Present with 3050 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class III subfamily. {ECO:0000305}.
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DR   EMBL; U28373; AAB64807.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12212.1; -; Genomic_DNA.
DR   PIR; S61166; S61166.
DR   RefSeq; NP_010659.1; NM_001180679.1.
DR   AlphaFoldDB; Q06350; -.
DR   SMR; Q06350; -.
DR   BioGRID; 32430; 73.
DR   DIP; DIP-5251N; -.
DR   IntAct; Q06350; 3.
DR   STRING; 4932.YDR371W; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GlyCosmos; Q06350; 4 sites, No reported glycans.
DR   GlyGen; Q06350; 4 sites.
DR   MaxQB; Q06350; -.
DR   PaxDb; 4932-YDR371W; -.
DR   PeptideAtlas; Q06350; -.
DR   EnsemblFungi; YDR371W_mRNA; YDR371W; YDR371W.
DR   GeneID; 851977; -.
DR   KEGG; sce:YDR371W; -.
DR   AGR; SGD:S000002779; -.
DR   SGD; S000002779; CTS2.
DR   VEuPathDB; FungiDB:YDR371W; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   GeneTree; ENSGT00940000175593; -.
DR   HOGENOM; CLU_002833_1_2_1; -.
DR   InParanoid; Q06350; -.
DR   OMA; SYPESKY; -.
DR   OrthoDB; 3203764at2759; -.
DR   BioCyc; YEAST:G3O-29921-MONOMER; -.
DR   Reactome; R-SCE-189085; Digestion of dietary carbohydrate.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 851977; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q06350; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q06350; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR   GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR   GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IGI:SGD.
DR   CDD; cd06548; GH18_chitinase; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal; Sporulation.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..511
FT                   /note="Sporulation-specific chitinase 2"
FT                   /id="PRO_0000011937"
FT   DOMAIN          73..472
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        223
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        456
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        472
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   511 AA;  59118 MW;  238FF79963BF0D63 CRC64;
     MVGHSAQHRS KSSLVSHLLI LLIFITIIIE MCLYNKIFKN QRSDDIRDNF NNGGHRVPSN
     VQNHGTHIRD EAFISGVYYS NWSPYKPRFH FPHDINLKQV SHIYYAFFKI NSRTGGIENT
     DSWSDLEMNL YKSLAIKNSE LIKESSNNSV QNILPLGCIG ELFYLKNTCS DKKFKVIMSI
     GGWSDSENFK IIIKDDKLLQ NFVDSSVETM FRLGFDGIDL DWEFPGNNES EPRGYLKLVR
     MLRLKLNSLE SQIFGKRTED HFQLSIAAPA FKDKLFYLPI TEIDQYVDYW NMMTYDYYGS
     WSETTGYHSN LFSETELNGN FAMHYMIDRF GVNSRKLVLG MAAYGRSFHI KDNKFEPFNQ
     NTVLINKIFK GVGKPTKEID KADGKEGIWP YKNLPKIGTI EQYDPKYVSA YCFDEKNSIF
     ISYDNTKSVK TKAEYVTHNN LGGGFWWESC GEAYANESRS LINAFNEGLH FNVSSKPSIF
     QDVRVKKYYL NKYGDGGFLS PYLKHLDSRK Q
//