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CHIT_ACTCC
ID   CHIT_ACTCC              Reviewed;         322 AA.
AC   P86473; A0A2R6RNH9;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 2.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Endochitinase {ECO:0000250|UniProtKB:P06215};
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   ORFNames=CEY00_Acc04863 {ECO:0000312|EMBL:PSS31588.1};
OS   Actinidia chinensis var. chinensis (Chinese soft-hair kiwi).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Actinidiaceae; Actinidia.
OX   NCBI_TaxID=1590841;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Red5;
RX   PubMed=29661190; DOI=10.1186/s12864-018-4656-3;
RA   Pilkington S.M., Crowhurst R., Hilario E., Nardozza S., Fraser L., Peng Y.,
RA   Gunaseelan K., Simpson R., Tahir J., Deroles S.C., Templeton K., Luo Z.,
RA   Davy M., Cheng C., McNeilage M., Scaglione D., Liu Y., Zhang Q., Datson P.,
RA   De Silva N., Gardiner S.E., Bassett H., Chagne D., McCallum J.,
RA   Dzierzon H., Deng C., Wang Y.Y., Barron L., Manako K., Bowen J.,
RA   Foster T.M., Erridge Z.A., Tiffin H., Waite C.N., Davies K.M.,
RA   Grierson E.P., Laing W.A., Kirk R., Chen X., Wood M., Montefiori M.,
RA   Brummell D.A., Schwinn K.E., Catanach A., Fullerton C., Li D.,
RA   Meiyalaghan S., Nieuwenhuizen N., Read N., Prakash R., Hunter D., Zhang H.,
RA   McKenzie M., Knabel M., Harris A., Allan A.C., Gleave A., Chen A.,
RA   Janssen B.J., Plunkett B., Ampomah-Dwamena C., Voogd C., Leif D.,
RA   Lafferty D., Souleyre E.J.F., Varkonyi-Gasic E., Gambi F., Hanley J.,
RA   Yao J.L., Cheung J., David K.M., Warren B., Marsh K., Snowden K.C.,
RA   Lin-Wang K., Brian L., Martinez-Sanchez M., Wang M., Ileperuma N.,
RA   Macnee N., Campin R., McAtee P., Drummond R.S.M., Espley R.V.,
RA   Ireland H.S., Wu R., Atkinson R.G., Karunairetnam S., Bulley S.,
RA   Chunkath S., Hanley Z., Storey R., Thrimawithana A.H., Thomson S.,
RA   David C., Testolin R., Huang H., Hellens R.P., Schaffer R.J.;
RT   "A manually annotated Actinidia chinensis var. chinensis (kiwifruit) genome
RT   highlights the challenges associated with draft genomes and gene prediction
RT   in plants.";
RL   BMC Genomics 19:257-257(2018).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 22-29, AND ALLERGEN.
RC   STRAIN=cv. Hort 16A {ECO:0000269|PubMed:15536427};
RC   TISSUE=Fruit {ECO:0000269|PubMed:15536427};
RX   PubMed=15536427; DOI=10.1016/j.jaci.2004.07.016;
RA   Bublin M., Mari A., Ebner C., Knulst A., Scheiner O.,
RA   Hoffmann-Sommergruber K., Breiteneder H., Radauer C.;
RT   "IgE sensitization profiles toward green and gold kiwifruits differ among
RT   patients allergic to kiwifruit from 3 European countries.";
RL   J. Allergy Clin. Immunol. 114:1169-1175(2004).
CC   -!- FUNCTION: Defense against chitin-containing fungal pathogens.
CC       {ECO:0000250|UniProtKB:P06215}.
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:P06215};
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds IgE.
CC       {ECO:0000269|PubMed:15536427}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000255}.
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DR   EMBL; NKQK01000004; PSS31588.1; -; Genomic_DNA.
DR   AlphaFoldDB; P86473; -.
DR   SMR; P86473; -.
DR   STRING; 1590841.P86473; -.
DR   Allergome; 2408; Act c Chitinase_I.
DR   EnsemblPlants; PSS31588; PSS31588; CEY00_Acc04863.
DR   Gramene; PSS31588; PSS31588; CEY00_Acc04863.
DR   OMA; CEPSATW; -.
DR   Proteomes; UP000241394; Chromosome lg4.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
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; 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; 1.
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; 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   Allergen; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Plant defense; Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:15536427"
FT   CHAIN           22..322
FT                   /note="Endochitinase"
FT                   /id="PRO_0000393867"
FT   DOMAIN          22..62
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        24..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..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   322 AA;  34459 MW;  DDB619209291C285 CRC64;
     MKMRYCVLVS VLAILVIRGS AENCGRQAGG ALCPGGQCCS KWGWCGTTPD HCGTDCQSQC
     GGTPSPGPSG SDITNLIPRS TFDRMLLHRN DGACPGKNFY TYDGFIAAAR SFGAFATTGD
     TDTRKREIAA FLAQTSHETT GGWASAPDGP YSWGYCFLRE QGNPGAYCTP SAQWPCAPGR
     KYFGRGPIQI THNYNYGPAG KALGVDLLNN PDLVATDPAI SFKTALWFWM TPQSPKPSCH
     DVITGRWTPS AADRSAGRLP GFGVITNIIN GGLECGHGSD SRVQDRIGFY KRYCQIFGIG
     TGDNLDCGNQ RSFGSGRLVD TM
 
 
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