ID CHIA_SOLCI Reviewed; 253 AA. AC Q40114; Q40113; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 16-JUN-2009, entry version 56. DE RecName: Full=Acidic endochitinase pcht28; DE EC=3.2.1.14; DE Flags: Precursor; OS Solanum chilense (Tomato) (Lycopersicon chilense). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; OC Solanum; Lycopersicon. OX NCBI_TaxID=4083; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. LA1930; TISSUE=Leaf; RX MEDLINE=95115667; PubMed=7816027; DOI=10.1007/BF00283267; RA Chen R.D., Yu L.X., Greer A.F., Cheriti H., Tabaeizadeh Z.; RT "Isolation of an osmotic stress- and abscisic acid-induced gene RT encoding an acidic endochitinase from Lycopersicon chilense."; RL Mol. Gen. Genet. 245:195-202(1994). CC -!- FUNCTION: Defense against chitin containing fungal pathogens. CC -!- CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D- CC glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- INDUCTION: By osmotic stress and abscisic acid (ABA). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase CC class II subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L19342; AAA64999.1; -; mRNA. DR EMBL; M97210; AAA64998.1; -; mRNA. DR PIR; S51588; S51588. DR PIR; S51589; S51589. DR HSSP; P23951; 2BAA. DR CAZy; GH19; Glycoside Hydrolase Family 19. DR BRENDA; 3.2.1.14; 292969. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0004568; F:chitinase activity; IEA:EC. 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 InterPro; IPR016283; Glyco_hydro_19. DR InterPro; IPR000726; Glyco_hydro_19_cat. DR PANTHER; PTHR22595; Glyco_hydro_19_cat; 1. DR Pfam; PF00182; Glyco_hydro_19; 1. DR PIRSF; PIRSF001060; Endochitinase; 1. DR ProDom; PD354900; Glyco_hydro_19; 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; Disulfide bond; KW Glycosidase; Hydrolase; Plant defense; Polysaccharide degradation; KW Secreted; Signal; Stress response. FT SIGNAL 1 24 By similarity. FT CHAIN 25 253 Acidic endochitinase pcht28. FT /FTId=PRO_0000005298. FT DISULFID 212 244 By similarity. FT CONFLICT 94 94 K -> N (in Ref. 1; AAA64998). FT CONFLICT 160 160 R -> K (in Ref. 1; AAA64998). FT CONFLICT 170 171 QD -> HH (in Ref. 1; AAA64998). SQ SEQUENCE 253 AA; 27569 MW; D48C269D5A794E60 CRC64; MKFNIVSPVA LSCLFFLFLT GTLAQNAGSI VTRELFEQML SFRNNDACPA KGFYTYDAFI AAANSFPGFG TTGDDTARKK EIAAFFGQTS HETKGGSAGT FTGGYCFVRQ IDQSDRYYGR GPIQLTHQSN YERAGQGIGV GQDLVNNPDL VATDPIISFR TAIWFWMTAQ DNKPSCHNVI IGQWTPSPAD TAANRVPGYG VITNIINGGL ECNMGPNTAV ESRIGFYRRY CGMLNVPTGE NLDCNNQKNF AQG //