ID   CHIT_SOLTU              Reviewed;         328 AA.
AC   P05315;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   24-JAN-2024, entry version 137.
DE   RecName: Full=Endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Russet Burbank-0; TISSUE=Leaf;
RX   PubMed=3387233; DOI=10.1093/nar/16.11.5210;
RA   Gaynor J.J.;
RT   "Primary structure of an endochitinase mRNA from Solanum tuberosum.";
RL   Nucleic Acids Res. 16:5210-5210(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Russet Burbank-0;
RX   PubMed=2762165; DOI=10.1093/nar/17.14.5855;
RA   Gaynor J.J., Unkenholz K.M.;
RT   "Sequence analysis of a genomic clone encoding an endochitinase from
RT   Solanum tuberosum.";
RL   Nucleic Acids Res. 17:5855-5855(1989).
CC   -!- FUNCTION: Defense against chitin-containing fungal pathogens.
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: Vacuole {ECO:0000250}. Note=Vacuolar and
CC       protoplast. {ECO:0000250}.
CC   -!- INDUCTION: By ethylene.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
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DR   EMBL; X07130; CAA30142.1; -; mRNA.
DR   EMBL; X15494; CAA33517.1; -; Genomic_DNA.
DR   PIR; S05426; S05426.
DR   AlphaFoldDB; P05315; -.
DR   SMR; P05315; -.
DR   STRING; 4113.P05315; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   InParanoid; P05315; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P05315; baseline and differential.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00325; chitinase_GH19; 1.
DR   CDD; cd00035; ChtBD1; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 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   PANTHER; PTHR22595; CHITINASE-RELATED; 1.
DR   PANTHER; PTHR22595:SF166; ENDOCHITINASE; 1.
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; Lysozyme-like; 1.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Disulfide bond; Glycosidase; Hydrolase; Plant defense;
KW   Polysaccharide degradation; Reference proteome; Signal; Vacuole.
FT   SIGNAL          1..26
FT   CHAIN           27..321
FT                   /note="Endochitinase"
FT                   /id="PRO_0000005327"
FT   PROPEP          322..328
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000005328"
FT   DOMAIN          27..68
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        144
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        29..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        38..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        43..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        62..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        100..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        174..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        281..313
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   328 AA;  35407 MW;  669B82159BC176EF CRC64;
     MRRHKEVNFV AYLLFSLLVL VSAALAQNCG SQGGGKACAS GQCCSKFGWC GNTNDYCGSG
     NCQSQCPGGG PGPGPGGDLG SAISNSMFDQ MLKHRNENSC QGKNFYSYNA FINAARSFPG
     FGTSGDINAR KREIAAFFAQ TSHETTGGWA SAPDGPYAWG YCFLRERGNP GDYCPPSSQW
     PCAPGRKYFG RGPIQISHNY NYGPCGRAIG VDLLNNPDLV ATDPVISFKT ALWFWMTPQS
     PKPSCHDVII GRWNPSSADR AANRLPGFGV ITNIINGGLE CGRGTDNRVQ DRIGFYRRYC
     SILGVTPGDN LDCVNQRWFG NALLVDTL
//