CHI4_CRYJA
ID CHI4_CRYJA Reviewed; 281 AA.
AC Q5NTA4;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Endochitinase 4 {ECO:0000305};
DE EC=3.2.1.14 {ECO:0000269|PubMed:15725197, ECO:0000269|PubMed:29756783};
DE AltName: Full=Chitinase class IV {ECO:0000303|PubMed:15725197, ECO:0000303|PubMed:18691438, ECO:0000303|PubMed:28032262, ECO:0000303|PubMed:29459179, ECO:0000303|PubMed:29756783, ECO:0000312|EMBL:BAD77932.1};
DE Short=CJP-4 {ECO:0000303|PubMed:15725197, ECO:0000303|PubMed:18691438, ECO:0000303|PubMed:28032262, ECO:0000303|PubMed:29459179, ECO:0000303|PubMed:29756783};
DE AltName: Allergen=Cry j Chitinase {ECO:0000305};
DE Flags: Precursor;
OS Cryptomeria japonica (Japanese cedar) (Cupressus japonica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Cryptomeria.
OX NCBI_TaxID=3369 {ECO:0000312|EMBL:BAD77932.1};
RN [1] {ECO:0000312|EMBL:BAD77932.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 178-186 AND 247-259,
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, PTM, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND ALLERGEN.
RC TISSUE=Anther {ECO:0000303|PubMed:15725197};
RX PubMed=15725197; DOI=10.1111/j.1365-2222.2005.02167.x;
RA Fujimura T., Shigeta S., Suwa T., Kawamoto S., Aki T., Masubuchi M.,
RA Hayashi T., Hide M., Ono K.;
RT "Molecular cloning of a class IV chitinase allergen from Japanese cedar
RT (Cryptomeria japonica) pollen and competitive inhibition of its
RT immunoglobulin E-binding capacity by latex C-serum.";
RL Clin. Exp. Allergy 35:234-243(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-273.
RC TISSUE=Cone {ECO:0000303|PubMed:18691438};
RX PubMed=18691438; DOI=10.1186/1471-2164-9-383;
RA Futamura N., Totoki Y., Toyoda A., Igasaki T., Nanjo T., Seki M.,
RA Sakaki Y., Mari A., Shinozaki K., Shinohara K.;
RT "Characterization of expressed sequence tags from a full-length enriched
RT cDNA library of Cryptomeria japonica male strobili.";
RL BMC Genomics 9:383-383(2008).
RN [3]
RP 3D-STRUCTURE MODELING, ACTIVE SITE, AND MUTAGENESIS OF GLU-142.
RX PubMed=28032262; DOI=10.1007/s12104-016-9725-4;
RA Takashima T., Ohnuma T., Fukamizo T.;
RT "NMR assignments and ligand-binding studies on a two-domain family GH19
RT chitinase allergen from Japanese cedar (Cryptomeria japonica) pollen.";
RL Biomol. NMR. Assign. 11:85-90(2017).
RN [4]
RP DOMAIN.
RX PubMed=29459179; DOI=10.1016/j.carres.2018.02.004;
RA Takashima T., Ohnuma T., Fukamizo T.;
RT "NMR analysis of substrate binding to a two-domain chitinase: Comparison
RT between soluble and insoluble chitins.";
RL Carbohydr. Res. 458:52-59(2018).
RN [5] {ECO:0007744|PDB:5H7T}
RP X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS) OF 77-281, FUNCTION, CATALYTIC
RP ACTIVITY, DOMAIN, DISULFIDE BONDS, AND MUTAGENESIS OF 1-MET--THR-76.
RX PubMed=29756783; DOI=10.1021/acs.jafc.8b01140;
RA Takashima T., Numata T., Taira T., Fukamizo T., Ohnuma T.;
RT "Structure and Enzymatic Properties of a Two-Domain Family GH19 Chitinase
RT from Japanese Cedar (Cryptomeria japonica) Pollen.";
RL J. Agric. Food Chem. 66:5699-5706(2018).
CC -!- FUNCTION: Has endochitinase activity (PubMed:15725197). Hydrolyzes
CC chitin oligosaccharides, GlcNAc(n), with different degrees of
CC polymerization (n=2-6), a soluble substrate glycol chitin, and an
CC insoluble substrate beta-chitin nanofiber in vitro. GlcNAc(6) is
CC hydrolyzed at the second glycosidic linkage from the reducing end in
CC addition to the middle linkage. GlcNAc(4) is further hydrolyzed to
CC GlcNAc(2). Has antifungal activity against hyphal growth of H.rufa
CC (PubMed:29756783). {ECO:0000269|PubMed:15725197,
CC ECO:0000269|PubMed:29756783}.
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:0000269|PubMed:15725197, ECO:0000269|PubMed:29756783};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P29022}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level).
CC {ECO:0000269|PubMed:15725197}.
CC -!- DOMAIN: Contains an N-terminal substrate-binding domain (CBM18) and a
CC GH19 catalytic domain (PubMed:29756783). The CBM18 domain is involved
CC in binding of the insoluble substrate chitin nanofiber
CC (PubMed:29459179). The CBM18 domain is not required for catalytic
CC activity, but possesses antifungal activity (PubMed:29756783).
CC {ECO:0000269|PubMed:29459179, ECO:0000269|PubMed:29756783}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:15725197}.
CC -!- ALLERGEN: Causes an allergic reaction in human. The native protein
CC binds to IgE in all 31 patients tested allergic to Japanese cedar
CC pollen. {ECO:0000269|PubMed:15725197}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class IV subfamily. {ECO:0000305}.
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DR EMBL; AB196451; BAD77932.1; -; mRNA.
DR EMBL; BY896705; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 5H7T; X-ray; 1.19 A; A=77-281.
DR PDBsum; 5H7T; -.
DR AlphaFoldDB; Q5NTA4; -.
DR SMR; Q5NTA4; -.
DR Allergome; 2520; Cry j Chitinase.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0008843; F:endochitinase activity; IDA:UniProtKB.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; 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; 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.
DR PROSITE; PS00774; CHITINASE_19_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Antimicrobial; Carbohydrate metabolism;
KW Chitin degradation; Chitin-binding; Direct protein sequencing;
KW Disulfide bond; Fungicide; Glycosidase; Hydrolase; Plant defense;
KW Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..281
FT /note="Endochitinase 4"
FT /evidence="ECO:0000255"
FT /id="PRO_5004260555"
FT DOMAIN 35..68
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT ACT_SITE 142
FT /note="Proton donor"
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-1,
FT ECO:0000269|PubMed:28032262"
FT DISULFID 34..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 37..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 43..57
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-2,
FT ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 61..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 98..147
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-2,
FT ECO:0000269|PubMed:29756783, ECO:0007744|PDB:5H7T"
FT DISULFID 159..168
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-2,
FT ECO:0000269|PubMed:29756783, ECO:0007744|PDB:5H7T"
FT DISULFID 249..281
FT /evidence="ECO:0000255|PIRSR:PIRSR001060-2,
FT ECO:0000269|PubMed:29756783, ECO:0007744|PDB:5H7T"
FT MUTAGEN 1..76
FT /note="Missing: Does not significantly affect the
FT hydrolysis of chitin oligosaccharides, GlcNAc(n), with
FT different degrees of polymerization, but has a higher
FT activity than the full-length protein against a soluble
FT substrate glycol chitin and a lower activity against an
FT insoluble substrate beta-chitin nanofiber in vitro.
FT Significantly reduced fungal growth inhibition."
FT /evidence="ECO:0000269|PubMed:29756783"
FT MUTAGEN 142
FT /note="E->Q: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28032262"
FT CONFLICT 70
FT /note="S -> SS (in Ref. 2; BY896705)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="T -> P (in Ref. 2; BY896705)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="N -> Q (in Ref. 2; BY896705)"
FT /evidence="ECO:0000305"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5H7T"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:5H7T"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5H7T"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:5H7T"
FT TURN 117..121
FT /evidence="ECO:0007829|PDB:5H7T"
FT HELIX 125..142
FT /evidence="ECO:0007829|PDB:5H7T"
FT TURN 143..147
FT /evidence="ECO:0007829|PDB:5H7T"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5H7T"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:5H7T"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:5H7T"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:5H7T"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:5H7T"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:5H7T"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:5H7T"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:5H7T"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:5H7T"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:5H7T"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:5H7T"
FT HELIX 254..270
FT /evidence="ECO:0007829|PDB:5H7T"
SQ SEQUENCE 281 AA; 29355 MW; 4EE305D88FA07588 CRC64;
MQIMATQNSK SNIFWSSSAS VVLVLLLLVD VGVCQNCGCN GLCCSQYGYC GSGEAYCGAG
CKEGPCSSSS PPSTGTGVGS IVSSDVFNSI VGGAASGCAG NGFYTYDSFI SAANAFNGFG
TSGSSDVNKR EIAAFFANAA HETGGFCYIE EQNPTSIYCD ASNTQYPCAS GKTYHGRGPL
QLSWNYNYGA AGSYIQFDGL NNPEIVGTDS TISFKTAVWF WMVNSNCHTA ITSGQGFGAT
IRAINSMECD GGNAATVASR VNYYQKFCQQ LNVDTGSNLQ C
