ID   CHIA_SECCE              Reviewed;         321 AA.
AC   Q9FRV1;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Basic endochitinase A;
DE            EC=3.2.1.14;
DE   AltName: Full=Rye seed chitinase-a;
DE            Short=RSC-a;
DE   Flags: Precursor;
GN   Name=rsca {ECO:0000312|EMBL:BAB18519.1};
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:BAB18519.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-24, FUNCTION, CATALYTIC
RP   ACTIVITY, AND MUTAGENESIS OF TRP-42 AND GLU-145.
RC   TISSUE=Seed {ECO:0000269|PubMed:14981295};
RX   PubMed=14981295; DOI=10.1271/bbb.68.324;
RA   Ohnuma T., Taira T., Yamagami T., Aso Y., Ishiguro M.;
RT   "Molecular cloning, functional expression, and mutagenesis of cDNA encoding
RT   class I chitinase from rye (Secale cereale) seeds.";
RL   Biosci. Biotechnol. Biochem. 68:324-332(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 20-321.
RX   PubMed=7764543; DOI=10.1271/bbb.58.322;
RA   Yamagami T., Funatsu G.;
RT   "The complete amino acid sequence of chitinase-a from the seeds of rye
RT   (Secale cereal).";
RL   Biosci. Biotechnol. Biochem. 58:322-329(1994).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 20-26, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL 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   DISULFIDE BONDS.
RX   PubMed=10923812; DOI=10.1271/bbb.64.1313;
RA   Yamagami T., Funatsu G., Ishiguro M.;
RT   "Positions of disulfide bonds in rye (Secale cereale) seed chitinase-a.";
RL   Biosci. Biotechnol. Biochem. 64:1313-1316(2000).
RN   [5] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, 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   [6] {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, lateral walls and septa of fungi and degrades mature
CC       chitin. {ECO:0000269|PubMed:11826968, ECO:0000269|PubMed:12092848,
CC       ECO:0000269|PubMed:14981295, ECO:0000269|PubMed:7763659}.
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:11826968, ECO:0000269|PubMed:14981295,
CC         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 over 80% compared to the untreated enzyme.
CC         {ECO:0000269|PubMed:7763659};
CC   -!- TISSUE SPECIFICITY: Localized in the aleurone cells of the seed
CC       endosperm (at 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 I subfamily. {ECO:0000269|PubMed:14981295}.
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; AB051578; BAB18519.1; -; mRNA.
DR   PIR; JC2071; JC2071.
DR   AlphaFoldDB; Q9FRV1; -.
DR   SMR; Q9FRV1; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   PRIDE; Q9FRV1; -.
DR   BRENDA; 3.2.1.14; 5654.
DR   GO; GO:0005576; C:extracellular region; IC:UniProtKB.
DR   GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
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   Gene3D; 3.30.60.10; -; 1.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF57016; SSF57016; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR   PROSITE; PS00773; CHITINASE_19_1; 1.
DR   PROSITE; PS00774; CHITINASE_19_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Glycosidase;
KW   Hydrolase; Plant defense; Polysaccharide degradation; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:14981295,
FT                   ECO:0000269|PubMed:7763659, ECO:0000269|PubMed:7764543"
FT   CHAIN           20..321
FT                   /note="Basic endochitinase A"
FT                   /evidence="ECO:0000269|PubMed:14981295"
FT                   /id="PRO_0000042670"
FT   DOMAIN          20..60
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   REGION          62..79
FT                   /note="Hinge region (Gly/Pro/Thr-rich)"
FT                   /evidence="ECO:0000255"
FT   REGION          80..321
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        145
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        22..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:10923812"
FT   DISULFID        31..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:10923812"
FT   DISULFID        34..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:10923812"
FT   DISULFID        36..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:10923812"
FT   DISULFID        54..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:10923812"
FT   DISULFID        101..163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:10923812"
FT   DISULFID        175..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:10923812"
FT   DISULFID        301..314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:10923812"
FT   MUTAGEN         42
FT                   /note="W->A: Reduces chitinase activity towards soluble
FT                   chitin to 65.5% and towards insoluble chitin. Reduces
FT                   chitin-binding activity and anti-fungal activity."
FT                   /evidence="ECO:0000269|PubMed:14981295"
FT   MUTAGEN         145
FT                   /note="E->Q: Abolishes chitinase activity towards insoluble
FT                   and soluble chitin. Abolishes chitin-binding activity and
FT                   anti-fungal activity."
FT                   /evidence="ECO:0000269|PubMed:14981295"
FT   CONFLICT        305
FT                   /note="R -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   321 AA;  33642 MW;  76E5902BBC337C8E CRC64;
     MGAFALFAVL AMAVTMAVAE QCGSQAGGAT CPNCLCCSRF GWCGSTSDYC GDGCQSQCAG
     CGGGGTPVTP TPTPSGGGGV SSIVSRALFD RMLLHRNDGA CQAKGFYTYD AFVAAAGAFP
     GFGTTGSTDT RKREVAAFLA QTSHETTGGW ATAPDGAFAW GYCFKQERGA TSNYCTPSAQ
     WPCAPGKSYY GRGPIQLSHN YNYGPAGRAI GVDLLRNPDL VATDPTVSFK TAMWFWMTAQ
     APKPSSHAVI TGQWSPSGTD RAAGRVPGFG VITNIVNGGI ECGHGQDSRV ADRIGFYKRY
     CDILRVGYGN NLDCYNQRPF A