ID CHI_ARATH Reviewed; 277 AA. AC O24603; DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 162. DE RecName: Full=Endochitinase CHI {ECO:0000305}; DE EC=3.2.1.14; DE Flags: Precursor; GN Name=CHI {ECO:0000312|EMBL:AEC10291.1}; GN Synonyms=LSC222 {ECO:0000303|PubMed:12947053}; GN OrderedLocusNames=At2g43570 {ECO:0000312|EMBL:AAM20661.1}; GN ORFNames=F18O19.32 {ECO:0000312|EMBL:AEC10291.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548}; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP GENE FAMILY. RX PubMed=11525512; DOI=10.1007/s004250000464; RA Passarinho P.A., Van Hengel A.J., Fransz P.F., de Vries S.C.; RT "Expression pattern of the Arabidopsis thaliana AtEP3/AtchitIV RT endochitinase gene."; RL Planta 212:556-567(2001). RN [6] RP INDUCTION BY SENESCENCE. RC STRAIN=cv. Columbia; RX PubMed=12947053; DOI=10.1093/jxb/erg267; RA Navabpour S., Morris K., Allen R., Harrison E., A-H-Mackerness S., RA Buchanan-Wollaston V.; RT "Expression of senescence-enhanced genes in response to oxidative stress."; RL J. Exp. Bot. 54:2285-2292(2003). RN [7] RP INDUCTION BY VIRUS. RC STRAIN=cv. Columbia; RX PubMed=12535341; DOI=10.1046/j.1365-313x.2003.01625.x; RA Whitham S.A., Quan S., Chang H.S., Cooper B., Estes B., Zhu T., Wang X., RA Hou Y.M.; RT "Diverse RNA viruses elicit the expression of common sets of genes in RT susceptible Arabidopsis thaliana plants."; RL Plant J. 33:271-283(2003). RN [8] RP INDUCTION BY PATHOGENS. RC STRAIN=cv. Columbia; RX PubMed=12920300; DOI=10.1126/science.1086716; RA Nishimura M.T., Stein M., Hou B.-H., Vogel J.P., Edwards H., RA Somerville S.C.; RT "Loss of a callose synthase results in salicylic acid-dependent disease RT resistance."; RL Science 301:969-972(2003). 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:0000250|UniProtKB:P29022}; CC -!- INDUCTION: Accumulates during senescence and in response to 3- CC amino-1,2,4-triazole (3-AT) and silver nitrate (PubMed:12947053). CC Induced by viral infection (e.g. cucumber mosaic cucumovirus, oil seed CC rape tobamovirus, turnip vein clearing tobamovirus, potato virus X CC potexvirus, and turnip mosaic potyvirus) (PubMed:12535341). Induced by CC pathogens (PubMed:12920300). {ECO:0000269|PubMed:12535341, CC ECO:0000269|PubMed:12920300, ECO:0000269|PubMed:12947053}. 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; AC002333; AAB64049.1; -; Genomic_DNA. DR EMBL; AC002335; AAM14808.1; -; Genomic_DNA. DR EMBL; CP002685; AEC10291.1; -; Genomic_DNA. DR EMBL; AY099810; AAM20661.1; -; mRNA. DR EMBL; BT003417; AAO30080.1; -; mRNA. DR EMBL; AK226201; BAE98366.1; -; mRNA. DR PIR; G84867; G84867. DR RefSeq; NP_181885.1; NM_129919.5. DR AlphaFoldDB; O24603; -. DR SMR; O24603; -. DR STRING; 3702.O24603; -. DR CAZy; CBM18; Carbohydrate-Binding Module Family 18. DR CAZy; GH19; Glycoside Hydrolase Family 19. DR GlyCosmos; O24603; 1 site, No reported glycans. DR PaxDb; 3702-AT2G43570-1; -. DR ProteomicsDB; 246879; -. DR EnsemblPlants; AT2G43570.1; AT2G43570.1; AT2G43570. DR GeneID; 818959; -. DR Gramene; AT2G43570.1; AT2G43570.1; AT2G43570. DR KEGG; ath:AT2G43570; -. DR Araport; AT2G43570; -. DR TAIR; AT2G43570; CHI. DR eggNOG; KOG4742; Eukaryota. DR HOGENOM; CLU_045506_1_1_1; -. DR InParanoid; O24603; -. DR OMA; ANRIRYF; -. DR OrthoDB; 650307at2759; -. DR PhylomeDB; O24603; -. DR BioCyc; ARA:AT2G43570-MONOMER; -. DR PRO; PR:O24603; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; O24603; baseline and differential. DR GO; GO:0048046; C:apoplast; HDA:TAIR. DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR. DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW. DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-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:0010150; P:leaf senescence; IEP:UniProtKB. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR GO; GO:0072722; P:response to amitrole; IEP:UniProtKB. DR GO; GO:0010272; P:response to silver ion; IEP:UniProtKB. DR GO; GO:0009615; P:response to virus; IEP:UniProtKB. DR GO; GO:0009627; P:systemic acquired resistance; IEP:TAIR. 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:SF147; ENDOCHITINASE CHI; 1. DR Pfam; PF00187; Chitin_bind_1; 1. DR Pfam; PF00182; Glyco_hydro_19; 1. DR PIRSF; PIRSF001060; Endochitinase; 1. 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 Genevisible; O24603; AT. PE 2: Evidence at transcript level; KW Carbohydrate metabolism; Chitin degradation; Chitin-binding; KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Plant defense; KW Polysaccharide degradation; Reference proteome; Signal. FT SIGNAL 1..31 FT /evidence="ECO:0000255" FT CHAIN 32..277 FT /note="Endochitinase CHI" FT /evidence="ECO:0000255" FT /id="PRO_0000433910" FT DOMAIN 32..66 FT /note="Chitin-binding type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT REGION 75..277 FT /note="Catalytic" FT /evidence="ECO:0000250|UniProtKB:P29022" FT ACT_SITE 136 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P29022" FT CARBOHYD 274 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 34..42 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 36..48 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 41..55 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 59..64 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" SQ SEQUENCE 277 AA; 29775 MW; 0D0910C34F5E0AA5 CRC64; MAKPTSRNDR FALFFITLIF LILTVSKPVA SQNCGCASDF CCSKYGYCGT TDEFCGEGCQ AGPCRSSGGG GDPAVSLEGT VTPDFFNSIL NQRGDCPGKG FYTHDTFMAA ANSYPSFGAS ISKREIAAFF AHVAQETGFM CYIEEIDGPA KAASGEYCDT EKPEFPCAQG KGYYGRGAIQ LSWNYNYGLC GKALDENLLA SPEKVAQDQV LAFKTAFWFW TTNVRTSFKS GFGATIRAVN SRECSGGDST AKAANRIKYF QDYCGKLGVA PGDNLTC //