CHIT_YEAST
ID CHIT_YEAST Reviewed; 562 AA.
AC P29029; D6VYT1; P29028;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Endochitinase;
DE EC=3.2.1.14;
DE AltName: Full=Soluble cell wall protein 2;
DE Flags: Precursor;
GN Name=CTS1; Synonyms=SCW2; OrderedLocusNames=YLR286C; ORFNames=L8003.13;
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-38.
RC STRAIN=DBY918, and DBY939;
RX PubMed=1918080; DOI=10.1016/s0021-9258(18)55057-2;
RA Kuranda M.J., Robbins P.W.;
RT "Chitinase is required for cell separation during growth of Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 266:19758-19767(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 21-32, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 96099 / S288c / SEY6210;
RX PubMed=9748433; DOI=10.1128/jb.180.19.5030-5037.1998;
RA Cappellaro C., Mrsa V., Tanner W.;
RT "New potential cell wall glucanases of Saccharomyces cerevisiae and their
RT involvement in mating.";
RL J. Bacteriol. 180:5030-5037(1998).
RN [6]
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 -!- FUNCTION: Chitinase is required for cell separation during growth of
CC S.cerevisiae.
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:9748433}. Secreted,
CC cell wall {ECO:0000269|PubMed:9748433}. Note=Most of the enzyme is
CC secreted, but a significant amount of chitinase is also found
CC associated with the cell wall through binding of C-terminal domain to
CC chitin.
CC -!- PTM: Extensively glycosylated with a series of short O-linked mannose
CC oligosaccharides ranging in size from Man(2) to Man(5).
CC -!- MISCELLANEOUS: Present with 6350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
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DR EMBL; M74070; AAA34539.1; -; Genomic_DNA.
DR EMBL; M74069; AAA34538.1; -; Genomic_DNA.
DR EMBL; U17243; AAB67331.1; -; Genomic_DNA.
DR EMBL; AY693040; AAT93059.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09597.1; -; Genomic_DNA.
DR PIR; A41035; A41035.
DR PIR; B41035; B41035.
DR PIR; S50371; S50371.
DR RefSeq; NP_013388.1; NM_001182173.1.
DR PDB; 2UY2; X-ray; 1.60 A; A=22-315.
DR PDB; 2UY3; X-ray; 1.90 A; A=22-315.
DR PDB; 2UY4; X-ray; 1.75 A; A=22-315.
DR PDB; 2UY5; X-ray; 1.60 A; A=22-315.
DR PDB; 4TXE; X-ray; 1.80 A; A=22-315.
DR PDBsum; 2UY2; -.
DR PDBsum; 2UY3; -.
DR PDBsum; 2UY4; -.
DR PDBsum; 2UY5; -.
DR PDBsum; 4TXE; -.
DR AlphaFoldDB; P29029; -.
DR SMR; P29029; -.
DR BioGRID; 31551; 86.
DR STRING; 4932.YLR286C; -.
DR BindingDB; P29029; -.
DR ChEMBL; CHEMBL1293195; -.
DR DrugCentral; P29029; -.
DR CAZy; CBM19; Carbohydrate-Binding Module Family 19.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; P29029; -.
DR MaxQB; P29029; -.
DR PaxDb; P29029; -.
DR PRIDE; P29029; -.
DR EnsemblFungi; YLR286C_mRNA; YLR286C; YLR286C.
DR GeneID; 850992; -.
DR KEGG; sce:YLR286C; -.
DR SGD; S000004276; CTS1.
DR VEuPathDB; FungiDB:YLR286C; -.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_007818_7_0_1; -.
DR InParanoid; P29029; -.
DR OMA; SSWSTMN; -.
DR BioCyc; YEAST:YLR286C-MON; -.
DR BRENDA; 3.2.1.14; 984.
DR EvolutionaryTrace; P29029; -.
DR PRO; PR:P29029; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P29029; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; HDA:SGD.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR GO; GO:0008843; F:endochitinase activity; IDA:SGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006032; P:chitin catabolic process; IC:SGD.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:SGD.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR InterPro; IPR005089; CBM_fam19.
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; PF03427; CBM_19; 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 3D-structure; Carbohydrate metabolism; Cell wall;
KW Cell wall biogenesis/degradation; Chitin degradation; Chitin-binding;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1918080,
FT ECO:0000269|PubMed:9748433"
FT CHAIN 21..562
FT /note="Endochitinase"
FT /id="PRO_0000011936"
FT DOMAIN 27..311
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 329..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..562
FT /note="Chitin-binding, high affinity"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 16
FT /note="L -> P (in strain: DBY939)"
FT VARIANT 23
FT /note="R -> S (in strain: DBY939 and SEY6210)"
FT VARIANT 321
FT /note="T -> S (in strain: DBY939)"
FT VARIANT 336..340
FT /note="Missing (in strain: DBY939)"
FT VARIANT 399
FT /note="S -> A (in strain: DBY939)"
FT VARIANT 433..434
FT /note="PI -> SL (in strain: DBY939)"
FT VARIANT 461
FT /note="T -> K (in strain: DBY939)"
FT VARIANT 477..481
FT /note="Missing (in strain: DBY939)"
FT CONFLICT 168
FT /note="A -> R (in Ref. 1; AAA34539/AAA34538)"
FT /evidence="ECO:0000305"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:2UY2"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 54..64
FT /evidence="ECO:0007829|PDB:2UY2"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2UY2"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2UY2"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:2UY4"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:2UY2"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:2UY2"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:2UY2"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:2UY2"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:2UY5"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 243..251
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:2UY2"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:2UY2"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:2UY2"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:4TXE"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:2UY2"
SQ SEQUENCE 562 AA; 59015 MW; 0ABCEFBF448E1E19 CRC64;
MSLLYIILLF TQFLLLPTDA FDRSANTNIA VYWGQNSAGT QESLATYCES SDADIFLLSF
LNQFPTLGLN FANACSDTFS DGLLHCTQIA EDIETCQSLG KKVLLSLGGA SGSYLFSDDS
QAETFAQTLW DTFGEGTGAS ERPFDSAVVD GFDFDIENNN EVGYSALATK LRTLFAEGTK
QYYLSAAPQC PYPDASVGDL LENADIDFAF IQFYNNYCSV SGQFNWDTWL TYAQTVSPNK
NIKLFLGLPG SASAAGSGYI SDTSLLESTI ADIASSSSFG GIALWDASQA FSNELNGEPY
VEILKNLLTS ASQTATTTVA TSKTSAASTS SASTSSASTS QKKTTQSTTS TQSKSKVTLS
PTASSAIKTS ITQTTKTLTS STKTKSSLGT TTTESTLNSV AITSMKTTLS SQITSAALVT
PQTTTTSIVS SAPIQTAITS TLSPATKSSS VVSLQTATTS TLSPTTTSTS SGSTSSGSTS
SDSTARTLAK ELNAQYAAGK LNGKSTCTEG EIACSADGKF AVCDHSAWVY MECASGTTCY
AYDSGDSVYT QCNFSYLESN YF
