ID CHI3_SOLTU Reviewed; 318 AA. AC P52405; Q43179; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 127. DE RecName: Full=Endochitinase 3; DE EC=3.2.1.14; DE Flags: Precursor; Fragment; GN Name=CHTB3; 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. Datura; TISSUE=Leaf; RX PubMed=8111037; DOI=10.1007/bf00020173; RA Beerhues L., Kombrink E.; RT "Primary structure and expression of mRNAs encoding basic chitinase and RT 1,3-beta-glucanase in potato."; RL Plant Mol. Biol. 24:353-367(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-318. RX PubMed=2519115; DOI=10.1007/bf00016142; RA Laflamme D., Roxby R.; RT "Isolation and nucleotide sequence of cDNA clones encoding potato chitinase RT genes."; RL Plant Mol. Biol. 13:249-250(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 -!- DEVELOPMENTAL STAGE: Highest levels in younger leaves or stems segments CC and in older ones. Leaves and stems of intermediate age show a CC decreased expression. Appreciable amounts are also found in old root CC segments, and carpels. CC -!- INDUCTION: In response to infection, elicitor, ethylene, wounding. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase CC class I subfamily. {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; U02607; AAA17409.1; -; mRNA. DR EMBL; X14133; CAA32351.1; -; mRNA. DR PIR; S43317; S43317. DR AlphaFoldDB; P52405; -. DR SMR; P52405; -. DR FunCoup; P52405; 211. DR STRING; 4113.P52405; -. DR PaxDb; 4113-P52405; -. DR InParanoid; P52405; -. DR Proteomes; UP000011115; Unassembled WGS sequence. DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell. DR GO; GO:0008061; F:chitin binding; IEA:InterPro. DR GO; GO:0008843; F:endochitinase activity; IEA:UniProtKB-EC. 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:UniProtKB-ARBA. DR CDD; cd00325; chitinase_GH19; 1. DR CDD; cd06921; ChtBD1_GH19_hevein; 1. DR FunFam; 3.30.60.10:FF:000001; Basic endochitinase; 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 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:SF198; CHITIN-BINDING TYPE-1 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR22595; CHITINASE-RELATED; 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..18 FT /evidence="ECO:0000255" FT CHAIN 19..311 FT /note="Endochitinase 3" FT /id="PRO_0000005324" FT PROPEP 312..318 FT /note="Removed in mature form, vacuolar targeting" FT /evidence="ECO:0000255" FT /id="PRO_0000005325" FT DOMAIN 19..60 FT /note="Chitin-binding type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT ACT_SITE 134 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P29022" FT DISULFID 21..36 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 30..42 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 35..49 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 54..58 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 89..152 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 164..172 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 271..303 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT CONFLICT 18..27 FT /note="AEQCGSQAGG -> GSNVVHRPD (in Ref. 2; CAA32351)" FT /evidence="ECO:0000305" FT NON_TER 1 SQ SEQUENCE 318 AA; 33799 MW; BF587A8515534E71 CRC64; EFTIFSLLFS LLLLNASAEQ CGSQAGGALC APGLCCSKFG WCGNTNDYCG PGNCQSQCPG GPGPSGDLGG VISNSMFDQM LNHRNDNACQ GKNNFYSYNA FISAAGSFPG FGTTGDITAR KREIAAFLAQ TSHETTGGWP SAPDGPYAWG YCFLREQGSP GDYCTPSSQW PCAPGRKYFG RGPIQISHNY NYGPCGRAIG VDLLNNPDLV ATDSVISFKS AIWFWMTPQS PKPSCHDVIT GRWQPSGADQ AANRVPGFGV ITNIINGGLE CGHGSDSRVQ DRIGFYRRYC GILGVSPGDN LDCGNQRSFG NGLLVDTV //