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CHI61_ARATH
ID   CHI61_ARATH             Reviewed;         281 AA.
AC   O22842;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Endochitinase At2g43610 {ECO:0000305};
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   OrderedLocusNames=At2g43610 {ECO:0000312|EMBL:AAL62349.1};
GN   ORFNames=F18O19.28 {ECO:0000312|EMBL:AEC10295.1};
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   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   -!- 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   -!- INTERACTION:
CC       O22842; Q9SZU7: KAI2; NbExp=3; IntAct=EBI-25530116, EBI-25519488;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
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DR   EMBL; AC002333; AAB64045.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10295.1; -; Genomic_DNA.
DR   EMBL; AY072357; AAL62349.1; -; mRNA.
DR   EMBL; AY114724; AAM48043.1; -; mRNA.
DR   PIR; C84868; C84868.
DR   RefSeq; NP_181889.1; NM_129923.4.
DR   AlphaFoldDB; O22842; -.
DR   SMR; O22842; -.
DR   IntAct; O22842; 1.
DR   STRING; 3702.AT2G43610.1; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   MetOSite; O22842; -.
DR   SwissPalm; O22842; -.
DR   PaxDb; O22842; -.
DR   PRIDE; O22842; -.
DR   ProteomicsDB; 246780; -.
DR   EnsemblPlants; AT2G43610.1; AT2G43610.1; AT2G43610.
DR   GeneID; 818963; -.
DR   Gramene; AT2G43610.1; AT2G43610.1; AT2G43610.
DR   KEGG; ath:AT2G43610; -.
DR   Araport; AT2G43610; -.
DR   TAIR; locus:2043934; AT2G43610.
DR   eggNOG; KOG4742; Eukaryota.
DR   HOGENOM; CLU_045506_1_1_1; -.
DR   InParanoid; O22842; -.
DR   OMA; ISSACKG; -.
DR   OrthoDB; 1574413at2759; -.
DR   PhylomeDB; O22842; -.
DR   BioCyc; ARA:AT2G43610-MON; -.
DR   PRO; PR:O22842; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22842; baseline and differential.
DR   Genevisible; O22842; AT.
DR   GO; GO:0005886; C:plasma membrane; 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:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; 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; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 2.
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   1: Evidence at protein 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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..281
FT                   /note="Endochitinase At2g43610"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000433915"
FT   DOMAIN          29..66
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   REGION          86..281
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   ACT_SITE        148
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        31..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   281 AA;  29999 MW;  2E397E39A7762CCD CRC64;
     MATQNAILKK ALIIFLFTLT IMTGTAFSQN CGTNGCKGNM CCSRWGYCGT TKAYCGTGCQ
     SGPCNSKPKP TPTPSGSGGL NAGPRGTIAS VITPAFFNSI MSKVGSGCPA KGFYTRQAFI
     AAAESFAAYK GTVAKREIAA MLAQFSHESG SFCYKEEIAR GRYCSPSTTY PCQPGKNYYG
     RGPIQITWNY NYGAAGKFLG LPLLKDPDMV ARSPTVAFQC AMWFWNKNVR PVLSQGFGAT
     TRRINGGECN GGRPAAVQSR VNHYLDFCKK LGVTPGTNLS C
 
 
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