CHI_ARATH
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 03-AUG-2022, entry version 156.
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-amino-
CC 1,2,4-triazole (3-AT) and silver nitrate (PubMed:12947053). Induced by
CC viral infection (e.g. cucumber mosaic cucumovirus, oil seed rape
CC 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}.
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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.AT2G43570.1; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; O24603; -.
DR PRIDE; O24603; -.
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; locus:2044024; AT2G43570.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_1_1; -.
DR InParanoid; O24603; -.
DR OMA; ANRIRYF; -.
DR OrthoDB; 1574413at2759; -.
DR PhylomeDB; O24603; -.
DR BioCyc; ARA:AT2G43570-MON; -.
DR PRO; PR:O24603; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O24603; baseline and differential.
DR Genevisible; O24603; AT.
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; 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: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 Gene3D; 3.30.60.10; -; 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 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; SSF53955; 1.
DR SUPFAM; SSF57016; SSF57016; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS00773; CHITINASE_19_1; 1.
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
