CHI5_ARATH
ID CHI5_ARATH Reviewed; 273 AA.
AC Q9M2U5; O23248; Q42085;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Endochitinase EP3 {ECO:0000303|PubMed:11525512};
DE EC=3.2.1.14;
DE AltName: Full=Chitinase class IV {ECO:0000303|PubMed:11525512};
DE Short=AtchitIV {ECO:0000303|PubMed:11525512};
DE AltName: Full=Protein HOMOLOG OF CARROT EP3-3 CHITINASE {ECO:0000303|PubMed:11525512};
DE Short=AtEP3 {ECO:0000303|PubMed:11525512};
DE Flags: Precursor;
GN Name=EP3 {ECO:0000303|PubMed:11525512};
GN Synonyms=CHIV {ECO:0000303|PubMed:11525512};
GN OrderedLocusNames=At3g54420 {ECO:0000312|EMBL:AEE79228.1};
GN ORFNames=T12E18.110 {ECO:0000312|EMBL:CAB81807.1};
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION BY XANTHOMONAS CAMPESTRIS.
RC STRAIN=cv. Columbia;
RX PubMed=9426222; DOI=10.1016/s0014-5793(97)01332-x;
RA Gerhardt L.B.A., Sachetto-Martins G., Contarini M.G., Sandroni M.,
RA Ferreira R.P., de Lima V.M., Cordeiro M.C., de Oliveira D.E.,
RA Margis-Pinheiro M.;
RT "Arabidopsis thaliana class IV chitinase is early induced during the
RT interaction with Xanthomonas campestris.";
RL FEBS Lett. 419:69-75(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-72.
RA Philipps G., Gigot C.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP GENE FAMILY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
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 [8]
RP TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING.
RC STRAIN=cv. Columbia;
RX PubMed=19420714; DOI=10.1271/bbb.80837;
RA Takenaka Y., Nakano S., Tamoi M., Sakuda S., Fukamizo T.;
RT "Chitinase gene expression in response to environmental stresses in
RT Arabidopsis thaliana: chitinase inhibitor allosamidin enhances stress
RT tolerance.";
RL Biosci. Biotechnol. Biochem. 73:1066-1071(2009).
CC -!- FUNCTION: Probably involved in hypersensitive reaction upon Xanthomonas
CC campestris infection. {ECO:0000269|PubMed:9426222}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.8. {ECO:0000269|PubMed:11525512};
CC -!- TISSUE SPECIFICITY: Expressed in cells surrounding embryos, stems,
CC seedlings, pollen, roots, shoots, inflorescence, flowers, siliques and
CC leaves (PubMed:11525512, PubMed:19420714). Present in seedpods and seed
CC embryos, but not in roots, inflorescence stems, leaves and flowers
CC (PubMed:9426222). {ECO:0000269|PubMed:11525512,
CC ECO:0000269|PubMed:19420714, ECO:0000269|PubMed:9426222}.
CC -!- DEVELOPMENTAL STAGE: Expressed during somatic embryogenesis in nursing
CC cells surrounding the embryos but not in embryos. Accumulates in mature
CC pollen and growing pollen tubes until they enter the receptive
CC synergid, but not in endosperm and integuments. In adult plants,
CC present in hydathodes, stipules, root epidermis and emerging root
CC hairs. {ECO:0000269|PubMed:11525512}.
CC -!- INDUCTION: Accumulates rapidly and transiently in leaves after
CC inoculation with Xanthomonas campestris (PubMed:9426222). Slightly
CC repressed by wounding (PubMed:19420714). {ECO:0000269|PubMed:19420714,
CC ECO:0000269|PubMed:9426222}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA81243.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y14590; CAA74930.1; -; Genomic_DNA.
DR EMBL; AL132971; CAB81807.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79228.1; -; Genomic_DNA.
DR EMBL; BT010422; AAQ62423.1; -; mRNA.
DR EMBL; AK176488; BAD44251.1; -; mRNA.
DR EMBL; Z26409; CAA81243.1; ALT_INIT; mRNA.
DR PIR; T47601; T47601.
DR RefSeq; NP_191010.1; NM_115302.3.
DR AlphaFoldDB; Q9M2U5; -.
DR SMR; Q9M2U5; -.
DR STRING; 3702.AT3G54420.1; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; Q9M2U5; -.
DR PRIDE; Q9M2U5; -.
DR ProteomicsDB; 245186; -.
DR EnsemblPlants; AT3G54420.1; AT3G54420.1; AT3G54420.
DR GeneID; 824608; -.
DR Gramene; AT3G54420.1; AT3G54420.1; AT3G54420.
DR KEGG; ath:AT3G54420; -.
DR Araport; AT3G54420; -.
DR TAIR; locus:2096159; AT3G54420.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_1_1; -.
DR InParanoid; Q9M2U5; -.
DR OMA; INGAYEC; -.
DR OrthoDB; 1574413at2759; -.
DR PhylomeDB; Q9M2U5; -.
DR BioCyc; ARA:AT3G54420-MON; -.
DR PRO; PR:Q9M2U5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2U5; baseline and differential.
DR Genevisible; Q9M2U5; AT.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; ISS:TAIR.
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 GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR GO; GO:0010262; P:somatic embryogenesis; 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; 2.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR PRINTS; PR00451; CHITINBINDNG.
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 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..273
FT /note="Endochitinase EP3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433911"
FT DOMAIN 29..63
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REGION 70..273
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 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 33..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 38..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 56..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT CONFLICT 139
FT /note="H -> RN (in Ref. 1; CAA74930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 29436 MW; 1DB0A002F4EF44EC CRC64;
MLTPTISKSI SLVTILLVLQ AFSNTTKAQN CGCSSELCCS QFGFCGNTSD YCGVGCQQGP
CFAPPPANGV SVAEIVTQEF FNGIISQAAS SCAGNRFYSR GAFLEALDSY SRFGRVGSTD
DSRREIAAFF AHVTHETGHF CYIEEIDGAS KDYCDENATQ YPCNPNKGYY GRGPIQLSWN
FNYGPAGTAI GFDGLNAPET VATDPVISFK TALWYWTNRV QPVISQGFGA TIRAINGALE
CDGANTATVQ ARVRYYTDYC RQLGVDPGNN LTC
