CHI60_ARATH
ID CHI60_ARATH Reviewed; 273 AA.
AC O24654;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Inactive endochitinase At2g43600 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At2g43600 {ECO:0000312|EMBL:AEC10294.1};
GN ORFNames=F18O19.29 {ECO:0000312|EMBL:AEC10294.1};
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 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).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Glu residue that is essential for
CC catalytic activity, suggesting it lacks enzyme activity. {ECO:0000305}.
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DR EMBL; AC002333; AAB64046.1; -; Genomic_DNA.
DR EMBL; AC002335; AAM14809.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10294.1; -; Genomic_DNA.
DR PIR; B84868; B84868.
DR RefSeq; NP_001318415.1; NM_001337048.1.
DR AlphaFoldDB; O24654; -.
DR SMR; O24654; -.
DR STRING; 3702.AT2G43600.1; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; O24654; -.
DR PRIDE; O24654; -.
DR EnsemblPlants; AT2G43600.1; AT2G43600.1; AT2G43600.
DR GeneID; 818962; -.
DR Gramene; AT2G43600.1; AT2G43600.1; AT2G43600.
DR KEGG; ath:AT2G43600; -.
DR Araport; AT2G43600; -.
DR TAIR; locus:2043954; AT2G43600.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_1_1; -.
DR InParanoid; O24654; -.
DR PhylomeDB; O24654; -.
DR PRO; PR:O24654; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O24654; baseline and differential.
DR Genevisible; O24654; AT.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Chitin-binding; Disulfide bond; Glycoprotein; Plant defense;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..273
FT /note="Inactive endochitinase At2g43600"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433914"
FT DOMAIN 23..61
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REGION 78..273
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 25..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 30..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 36..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 54..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 273 AA; 30920 MW; C8096D4C6B13FD2F CRC64;
MTIKNVIFSL FILAILAETV FSQNCMDTSC PGLKECCSRW GFCGTKDEYC GFFCFSGPCN
IKGKSYGYDY NVDAGPRGKI ETVITSALFD SIMSKVESNC SAKGFYTYEA FITAFKSFGA
YKGKVAKREI AAILAHFSYG SKSFCYKEEI SNERYCSKSK KYPCEPGKNY YGRGLLQSIT
WNEYYGAGKH LGLPLLKDPD LVSRSPEVAF KFAMWFWNRN VRPALYLGFG EITKRVDGRE
CGNWRRDDTK NKVKQYIEFC EMLGVTPDQG LDC