CHIA_ARATH
ID CHIA_ARATH Reviewed; 302 AA.
AC P19172; O22065; O22066; O22067; O22068; O22069; O22070; O22071; O22072;
AC O22073; O24614; Q5HYZ8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Acidic endochitinase;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=CHIB1; OrderedLocusNames=At5g24090; ORFNames=MZF18.2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=16667600; DOI=10.1104/pp.93.3.907;
RA Samac D.A., Hironaka C.M., Yallaly P.E., Shah D.M.;
RT "Isolation and characterization of the genes encoding basic and acidic
RT chitinase in Arabidopsis thaliana.";
RL Plant Physiol. 93:907-914(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POLYMORPHISM.
RC STRAIN=cv. Al-0, cv. Bl-1, cv. Bla-10, cv. Bs-1, cv. Chi-0, cv. Ci-0,
RC cv. Es-0, cv. Gr-1, cv. Hiroshima, cv. Ita-0, cv. Kn-0, cv. Mt-0,
RC cv. Pog-0, cv. Shokei, and cv. Yo-0;
RX PubMed=9402740; DOI=10.1093/oxfordjournals.molbev.a025740;
RA Kawabe A., Innan H., Terauchi R., Miyashita N.T.;
RT "Nucleotide polymorphism in the acidic chitinase locus (ChiA) region of the
RT wild plant Arabidopsis thaliana.";
RL Mol. Biol. Evol. 14:1303-1315(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein functions as a defense against chitin containing
CC 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: Secreted, extracellular space. Note=Intercellular
CC space of infected plants.
CC -!- INDUCTION: Expression of the acidic chitinase gene was not detected in
CC normal, untreated plants nor in plants treated with ethylene or
CC salicylic acid.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
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DR EMBL; M34107; AAA32768.1; -; Genomic_DNA.
DR EMBL; AB006055; BAA21860.1; -; Genomic_DNA.
DR EMBL; AB006056; BAA21861.1; -; Genomic_DNA.
DR EMBL; AB006057; BAA21862.1; -; Genomic_DNA.
DR EMBL; AB006058; BAA21863.1; -; Genomic_DNA.
DR EMBL; AB006059; BAA21864.1; -; Genomic_DNA.
DR EMBL; AB006060; BAA21865.1; -; Genomic_DNA.
DR EMBL; AB006061; BAA21866.1; -; Genomic_DNA.
DR EMBL; AB006062; BAA21867.1; -; Genomic_DNA.
DR EMBL; AB006063; BAA21868.1; -; Genomic_DNA.
DR EMBL; AB006064; BAA21869.1; -; Genomic_DNA.
DR EMBL; AB006065; BAA21870.1; -; Genomic_DNA.
DR EMBL; AB006066; BAA21871.1; -; Genomic_DNA.
DR EMBL; AB006067; BAA21872.1; -; Genomic_DNA.
DR EMBL; AB006068; BAA21873.1; -; Genomic_DNA.
DR EMBL; AB006069; BAA21874.1; -; Genomic_DNA.
DR EMBL; AB009056; BAB08732.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93255.1; -; Genomic_DNA.
DR EMBL; BT020526; AAW49295.1; -; mRNA.
DR EMBL; BT021931; AAX49380.1; -; mRNA.
DR PIR; A45511; A45511.
DR RefSeq; NP_197797.1; NM_122314.3.
DR AlphaFoldDB; P19172; -.
DR SMR; P19172; -.
DR STRING; 3702.AT5G24090.1; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PaxDb; P19172; -.
DR PRIDE; P19172; -.
DR ProteomicsDB; 245175; -.
DR EnsemblPlants; AT5G24090.1; AT5G24090.1; AT5G24090.
DR GeneID; 832474; -.
DR Gramene; AT5G24090.1; AT5G24090.1; AT5G24090.
DR KEGG; ath:AT5G24090; -.
DR Araport; AT5G24090; -.
DR TAIR; locus:2178702; AT5G24090.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_007818_0_1_1; -.
DR InParanoid; P19172; -.
DR OMA; WDVTQAY; -.
DR OrthoDB; 923272at2759; -.
DR PhylomeDB; P19172; -.
DR BioCyc; ARA:AT5G24090-MON; -.
DR PRO; PR:P19172; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P19172; baseline and differential.
DR Genevisible; P19172; AT.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:TAIR.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR GO; GO:0003796; F:lysozyme activity; IMP:TAIR.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:TAIR.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:TAIR.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009642; P:response to light intensity; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Chitin degradation; Disulfide bond; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..30
FT CHAIN 31..302
FT /note="Acidic endochitinase"
FT /id="PRO_0000011913"
FT DOMAIN 31..302
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 156
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 49..96
FT /evidence="ECO:0000250"
FT DISULFID 79..86
FT /evidence="ECO:0000250"
FT DISULFID 188..217
FT /evidence="ECO:0000250"
FT VARIANT 22
FT /note="S -> T (in strain: cv. Ci-0)"
FT VARIANT 42
FT /note="E -> A (in strain: cv. Es-0)"
FT VARIANT 69
FT /note="Q -> R (in strain: cv. Ci-0)"
FT VARIANT 120
FT /note="E -> K (in strain: cv. Ci-0)"
FT VARIANT 125
FT /note="I -> V (in strain: cv. Ci-0)"
FT VARIANT 169
FT /note="T -> S (in strain: cv. Ci-0, cv. Ita-0 and cv. Pog-
FT 0)"
FT VARIANT 173
FT /note="F -> Y (in strain: cv. Ci-0)"
FT VARIANT 174
FT /note="S -> T (in strain: cv. Yo-0)"
FT VARIANT 180
FT /note="I -> V (in strain: cv. Ita-0 and cv. Pog-0)"
FT VARIANT 217
FT /note="C -> W (in strain: cv. Mt-0)"
FT VARIANT 220
FT /note="S -> T (in strain: cv. Ita-0 and cv. Pog-0)"
FT VARIANT 239
FT /note="A -> T (in strain: cv. Chi-0)"
FT VARIANT 243
FT /note="F -> I (in strain: cv. Ita-0)"
FT VARIANT 243
FT /note="F -> L (in strain: cv. Pog-0)"
FT VARIANT 257
FT /note="G -> V (in strain: cv. Yo-0)"
FT VARIANT 274
FT /note="K -> N (in strain: cv. Ci-0)"
FT VARIANT 299
FT /note="L -> S (in strain: cv. Bla-10)"
FT VARIANT 299
FT /note="L -> V (in strain: cv. Bs-1)"
FT CONFLICT 255
FT /note="G -> D (in Ref. 1; AAA32768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 33097 MW; 522AEB092E6EDCA8 CRC64;
MTNMTLRKHV IYFLFFISCS LSKPSDASRG GIAIYWGQNG NEGNLSATCA TGRYAYVNVA
FLVKFGNGQT PELNLAGHCN PAANTCTHFG SQVKDCQSRG IKVMLSLGGG IGNYSIGSRE
DAKVIADYLW NNFLGGKSSS RPLGDAVLDG IDFNIELGSP QHWDDLARTL SKFSHRGRKI
YLTGAPQCPF PDRLMGSALN TKRFDYVWIQ FYNNPPCSYS SGNTQNLFDS WNKWTTSIAA
QKFFLGLPAA PEAAGSGYIP PDVLTSQILP TLKKSRKYGG VMLWSKFWDD KNGYSSSILA
SV
