ID   CHIT_CARPA              Reviewed;         243 AA.
AC   P85084;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   04-NOV-2026, entry version 64.
DE   RecName: Full=Endochitinase;
DE            EC=3.2.1.14;
OS   Carica papaya (Papaya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Caricaceae; Carica.
OX   NCBI_TaxID=3649;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND MASS SPECTROMETRY.
RC   TISSUE=Latex {ECO:0000269|PubMed:17115118};
RX   PubMed=17115118; DOI=10.1007/s00018-006-6320-3;
RA   Huet J., Wyckmans J., Wintjens R., Boussard P., Raussens V.,
RA   Vandenbussche G., Ruysschaert J.M., Azarkan M., Looze Y.;
RT   "Structural characterization of two papaya chitinases, a family GH19 of
RT   glycosyl hydrolases.";
RL   Cell. Mol. Life Sci. 63:3042-3054(2006).
CC   -!- FUNCTION: Defense against chitin-containing fungal pathogens. Shows
CC       activity on chitin, tetra-N-acetylglucosamine and chitosan.
CC       {ECO:0000269|PubMed:17115118}.
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:17115118};
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:P19171}.
CC       Note=Vacuolar and protoplast. {ECO:0000250|UniProtKB:P19171}.
CC   -!- MASS SPECTROMETRY: Mass=26534; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17115118};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000255}.
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DR   PDB; 3CQL; X-ray; 1.50 A; A/B=1-243.
DR   AlphaFoldDB; P85084; -.
DR   SMR; P85084; -.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   BRENDA; 3.2.1.14; 1191.
DR   EvolutionaryTrace; P85084; -.
DR   GO; GO:0005773; C:vacuole; ISS:UniProtKB.
DR   GO; GO:0008843; F:endochitinase activity; EXP:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IEA:TreeGrafter.
DR   CDD; cd00325; chitinase_GH19; 1.
DR   FunFam; 3.30.20.10:FF:000001; Endochitinase (Chitinase); 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PANTHER; PTHR22595:SF79; CHITINASE 12; 1.
DR   PANTHER; PTHR22595; CHITINASE-RELATED; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00773; CHITINASE_19_1; 1.
DR   PROSITE; PS00774; CHITINASE_19_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Plant defense; Polysaccharide degradation; Vacuole.
FT   CHAIN           1..243
FT                   /note="Endochitinase"
FT                   /id="PRO_0000285971"
FT   ACT_SITE        67
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        23..85
FT                   /evidence="ECO:0000250|UniProtKB:Q9FRV1"
FT   DISULFID        97..105
FT                   /evidence="ECO:0000250|UniProtKB:Q9FRV1"
FT   DISULFID        223..236
FT                   /evidence="ECO:0000250|UniProtKB:Q9FRV1"
FT   HELIX           2..4
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           8..14
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   TURN            15..19
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   TURN            24..28
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           31..39
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   TURN            42..45
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           50..67
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   TURN            115..118
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           122..132
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           140..144
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           147..159
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           168..173
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           180..185
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           191..203
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   STRAND          204..207
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           210..226
FT                   /evidence="ECO:0007829|PDB:3CQL"
FT   HELIX           239..242
FT                   /evidence="ECO:0007829|PDB:3CQL"
SQ   SEQUENCE   243 AA;  26541 MW;  51F48F5F9A722703 CRC64;
     GIEKIISRSM FDQMLKHRNN PACPAKGFYT YDAFLAAAKS FPSFGTTGST DVRKRELAAF
     LGQTSHETTG GWPSAPDGPY AWGYCFLKER NPSSNYCAPS PRYPCAPGKS YYGRGPLQLS
     WNYNYGPCGE ALRVNLLGNP DLVATDRVLS FKTALWFWMT PQAPKPSCHD VLTGRWQPSA
     ADTAAGRLPG YGVLTNLLNG GLECGKGPNP QVADRLGFFR RYCGLLGVGT GNNLDCYNQR
     PFG
//