CHIC_SECCE
ID CHIC_SECCE Reviewed; 266 AA.
AC Q9FRV0;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Basic endochitinase C;
DE EC=3.2.1.14;
DE AltName: Full=Rye seed chitinase-c;
DE Short=RSC-c;
DE Flags: Precursor;
GN Name=rscc {ECO:0000312|EMBL:BAB18520.1};
OS Secale cereale (Rye).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Secale.
OX NCBI_TaxID=4550;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB18520.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-28, FUNCTION, CATALYTIC
RP ACTIVITY, AND MUTAGENESIS OF GLU-90; TRP-95; GLU-112; ASP-118 AND SER-143.
RC TISSUE=Seed {ECO:0000269|PubMed:11999399};
RX PubMed=11999399; DOI=10.1271/bbb.66.277;
RA Ohnuma T., Yagi M., Yamagami T., Taira T., Aso Y., Ishiguro M.;
RT "Molecular cloning, functional expression, and mutagenesis of cDNA encoding
RT rye (Secale cereale) seed chitinase-c.";
RL Biosci. Biotechnol. Biochem. 66:277-284(2002).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 24-266, AND DISULFIDE BONDS.
RC TISSUE=Seed {ECO:0000269|PubMed:7764335};
RX PubMed=7764335; DOI=10.1271/bbb.57.1854;
RA Yamagami T., Funatsu G.;
RT "The complete amino acid sequence of chitinase-c from the seeds of rye
RT (Secale cereal).";
RL Biosci. Biotechnol. Biochem. 57:1854-1861(1993).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 24-30, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=7763659; DOI=10.1271/bbb.57.643;
RA Yamagami T., Funatsu G.;
RT "Purification and some properties of three chitinases from the seeds of rye
RT (Secale cereale).";
RL Biosci. Biotechnol. Biochem. 57:643-647(1993).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 114-133 AND 254-260, AND ROLE OF ASP-118 IN SUBSTRATE
RP BINDING.
RX PubMed=9532801; DOI=10.1271/bbb.62.383;
RA Yamagami T., Funatsu G.;
RT "Identification of the aspartic acid residue located at or near substrate-
RT binding site of rye seed chitinase-c.";
RL Biosci. Biotechnol. Biochem. 62:383-385(1998).
RN [5] {ECO:0000305}
RP ROLE OF TRP-95 IN SUBSTRATE BINDING.
RA Yamagami T., Funatsu G.;
RT "Identification of the tryptophan residue located at the substrate-binding
RT site of rye seed chitinase-c.";
RL Biosci. Biotechnol. Biochem. 59:1076-1081(1995).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11826968; DOI=10.1271/bbb.65.2710;
RA Taira T., Yamagami T., Aso Y., Ishiguro M., Ishihara M.;
RT "Localization, accumulation, and antifungal activity of chitinases in rye
RT (Secale cereale) seed.";
RL Biosci. Biotechnol. Biochem. 65:2710-2718(2001).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=12092848; DOI=10.1271/bbb.66.970;
RA Taira T., Ohnuma T., Yamagami T., Aso Y., Ishiguro M., Ishihara M.;
RT "Antifungal activity of rye (Secale cereale) seed chitinases: the different
RT binding manner of class I and class II chitinases to the fungal cell
RT walls.";
RL Biosci. Biotechnol. Biochem. 66:970-977(2002).
CC -!- FUNCTION: Defense against chitin-containing fungal pathogens. Binds the
CC hyphal tips of fungi and degrades nascent chitin.
CC {ECO:0000269|PubMed:11826968, ECO:0000269|PubMed:11999399,
CC ECO:0000269|PubMed:12092848}.
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:11999399, ECO:0000269|PubMed:7763659};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is about 5.0. Stable between pH 4-8.
CC {ECO:0000269|PubMed:7763659};
CC Temperature dependence:
CC Enzyme activity is retained almost fully under 40 degrees Celsius and
CC completely destroyed at 70 degrees Celsius. At 60 degrees Celsius the
CC activity was 15-30% compared to the untreated enzyme.
CC {ECO:0000269|PubMed:7763659};
CC -!- TISSUE SPECIFICITY: Localized to the starchy endoderm of the seed May
CC localize to other parts of the seed including the aleurone cells (at
CC protein level). {ECO:0000269|PubMed:11826968}.
CC -!- DEVELOPMENTAL STAGE: Levels increase from 23 to 40 days after
CC flowering, and are maintained until maturation (at protein level).
CC {ECO:0000269|PubMed:11826968}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class II subfamily. {ECO:0000269|PubMed:11999399, 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; AB051579; BAB18520.1; -; mRNA.
DR PIR; JC7816; JC7816.
DR PIR; JN0884; JN0884.
DR PDB; 4DWX; X-ray; 1.80 A; A/B=24-266.
DR PDB; 4DYG; X-ray; 1.70 A; A/B=24-266.
DR PDB; 4J0L; X-ray; 1.90 A; A=24-266.
DR PDBsum; 4DWX; -.
DR PDBsum; 4DYG; -.
DR PDBsum; 4J0L; -.
DR AlphaFoldDB; Q9FRV0; -.
DR BMRB; Q9FRV0; -.
DR SMR; Q9FRV0; -.
DR MINT; Q9FRV0; -.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PRIDE; Q9FRV0; -.
DR GO; GO:0005576; C:extracellular region; IC:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IDA:UniProtKB.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00773; CHITINASE_19_1; 1.
DR PROSITE; PS00774; CHITINASE_19_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Carbohydrate metabolism; Chitin degradation;
KW Chitin-binding; Direct protein sequencing; Disulfide bond; Fungicide;
KW Glycosidase; Hydrolase; Plant defense; Polysaccharide degradation; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:11999399,
FT ECO:0000269|PubMed:7763659, ECO:0000269|PubMed:7764335"
FT CHAIN 24..266
FT /note="Basic endochitinase C"
FT /evidence="ECO:0000269|PubMed:11999399"
FT /id="PRO_0000042671"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT SITE 95
FT /note="May be involved in substrate-binding"
FT /evidence="ECO:0000269|Ref.5"
FT SITE 118
FT /note="May be involved in substrate-binding"
FT /evidence="ECO:0000269|PubMed:9532801"
FT DISULFID 46..108
FT /evidence="ECO:0000269|PubMed:7764335"
FT DISULFID 120..128
FT /evidence="ECO:0000269|PubMed:7764335"
FT DISULFID 246..259
FT /evidence="ECO:0000269|PubMed:7764335"
FT MUTAGEN 90
FT /note="E->Q: Abolishes chitinase activity."
FT /evidence="ECO:0000269|PubMed:11999399"
FT MUTAGEN 95
FT /note="W->A: Chitinase activity is reduced to 51.2% of
FT wild-type. Decreased anti-fungal activity."
FT /evidence="ECO:0000269|PubMed:11999399"
FT MUTAGEN 112
FT /note="E->Q: Chitinase activity is reduced to 0.33% of
FT wild-type. Decreased anti-fungal activity."
FT /evidence="ECO:0000269|PubMed:11999399"
FT MUTAGEN 118
FT /note="D->A: Chitinase activity is reduced to 79% of wild-
FT type. Decreased anti-fungal activity."
FT /evidence="ECO:0000269|PubMed:11999399"
FT MUTAGEN 143
FT /note="S->A: Chitinase activity is reduced to 1.2% of wild-
FT type. Decreased anti-fungal activity."
FT /evidence="ECO:0000269|PubMed:11999399"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:4DYG"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:4DYG"
FT TURN 38..42
FT /evidence="ECO:0007829|PDB:4DYG"
FT TURN 47..51
FT /evidence="ECO:0007829|PDB:4DYG"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:4DYG"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:4DYG"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:4DYG"
FT HELIX 73..90
FT /evidence="ECO:0007829|PDB:4DYG"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4DYG"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4DYG"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:4DYG"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:4DYG"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:4DYG"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4DYG"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:4DYG"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:4DYG"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:4DYG"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:4DYG"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:4DYG"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:4DYG"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:4DYG"
SQ SEQUENCE 266 AA; 28302 MW; E5E22C5BE43DB589 CRC64;
MRSLAVVVAV VATVAMAIGT AHGSVSSIIS HAQFDRMLLH RNDGACQAKG FYTYDAFVAA
ANAFPGFGAT GSTDARKRDV AAFLAQTSHE TTGGWATAPD GAFAWGYCFK QERGAAADYC
TPSAQWPCAP GKRYYGRGPI QLSHNYNYGP AGRAIGVDLL RNPDLVATDP TVSFKTALWF
WMTAQAPKPS SHAVITGKWS PSGADRAAGR APGFGVITNI INGGLECGHG QDSRVADRIG
FYKRYCDILG VGYGDNLDCY NQRPFA
