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CHIT_ZIZMA
ID   CHIT_ZIZMA              Reviewed;         330 AA.
AC   Q2VST0;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Endochitinase Ziz m 1.0101 {ECO:0000305};
DE            EC=3.2.1.14 {ECO:0000269|PubMed:16122801};
DE   AltName: Full=Allergen Ziz m 1 {ECO:0000303|PubMed:16122801, ECO:0000303|PubMed:18435802, ECO:0000312|EMBL:AAX40948.1};
DE   AltName: Allergen=Ziz m 1.0101 {ECO:0000305};
DE   Flags: Precursor;
OS   Ziziphus mauritiana (Indian jujube).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rhamnaceae; Paliureae; Ziziphus.
OX   NCBI_TaxID=157914;
RN   [1] {ECO:0000312|EMBL:AAX40948.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 146-154, CATALYTIC
RP   ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   ALLERGEN.
RC   TISSUE=Flower bud {ECO:0000303|PubMed:16122801};
RX   PubMed=16122801; DOI=10.1016/j.molimm.2005.07.021;
RA   Lee M.F., Hwang G.Y., Chen Y.H., Lin H.C., Wu C.H.;
RT   "Molecular cloning of Indian jujube (Zizyphus mauritiana) allergen Ziz m 1
RT   with sequence similarity to plant class III chitinases.";
RL   Mol. Immunol. 43:1144-1151(2006).
RN   [2]
RP   ALLERGEN, AND REGIONS.
RX   PubMed=18435802; DOI=10.1111/j.1365-2249.2008.03661.x;
RA   Lee M.F., Tsai J.J., Hwang G.Y., Lin S.J., Chen Y.H.;
RT   "Identification of immunoglobulin E (IgE)-binding epitopes and recombinant
RT   IgE reactivities of a latex cross-reacting Indian jujube Ziz m 1
RT   allergen.";
RL   Clin. Exp. Immunol. 152:464-471(2008).
RN   [3]
RP   ALLERGEN.
RX   PubMed=22289730; DOI=10.1016/j.anai.2011.10.011;
RA   Lee M.F., Lin S.J., Wang N.M., Wu H.J., Chen Y.H.;
RT   "Plant chitinase III Ziz m 1 stimulates multiple cytokines, most
RT   predominantly interleukin-13, from peripheral blood mononuclear cells of
RT   latex-fruit allergic patients.";
RL   Ann. Allergy Asthma Immunol. 108:113-116(2012).
CC   -!- FUNCTION: Defense against chitin containing fungal pathogens
CC       (Probable). {ECO:0000305}.
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:16122801};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16122801}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC       patients allergic to both the Indian jujube and latex (PubMed:16122801,
CC       PubMed:18435802, PubMed:22289730). Natural protein binds to IgE of
CC       patients allergic to the fruit of the Indian jujube. Recombinant
CC       protein binds to IgE in 87.5% of the 8 latex- and Indian jujube-
CC       allergic patients tested (PubMed:16122801). May stimulate allergic
CC       inflammation by inducing T-helper type 2 (Th2)-specific immune
CC       responses including increased production of cytokines, most
CC       predominantly IL13, from peripheral blood mononuclear cells (PBMC) of
CC       patients allergic to both latex and the fruit of the Indian jujube.
CC       Chitinase activity is required for this function (PubMed:22289730).
CC       {ECO:0000269|PubMed:16122801, ECO:0000269|PubMed:18435802,
CC       ECO:0000269|PubMed:22289730}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; AY839230; AAX40948.1; -; mRNA.
DR   AlphaFoldDB; Q2VST0; -.
DR   SMR; Q2VST0; -.
DR   Allergome; 2487; Ziz m 1.
DR   Allergome; 3537; Ziz m 1.0101.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0008843; F:endochitinase activity; IDA:UniProtKB.
DR   GO; GO:0006040; P:amino sugar metabolic process; IDA:UniProtKB.
DR   GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IC:UniProtKB.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR   InterPro; IPR045321; Cts1-like.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Allergen; Carbohydrate metabolism; Chitin degradation;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Plant defense; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..330
FT                   /note="Endochitinase Ziz m 1.0101"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004217981"
FT   DOMAIN          26..330
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          72..86
FT                   /note="Binds to IgE in 70% of the 10 patients tested
FT                   allergic to Indian jujube and latex"
FT                   /evidence="ECO:0000269|PubMed:18435802"
FT   REGION          292..301
FT                   /note="Binds to IgE in 100% of the 10 patients tested
FT                   allergic to Indian jujube and latex; sufficient for
FT                   prediction of the presence of allergic reactions in these
FT                   patients"
FT                   /evidence="ECO:0000269|PubMed:18435802"
FT   REGION          300..311
FT                   /note="Binds to IgE in 70% of the 10 patients tested
FT                   allergic to Indian jujube and latex"
FT                   /evidence="ECO:0000269|PubMed:18435802"
FT   REGION          309..320
FT                   /note="Binds to IgE in 70% of the 10 patients tested
FT                   allergic to Indian jujube and latex"
FT                   /evidence="ECO:0000269|PubMed:18435802"
FT   DISULFID        47..90
FT                   /evidence="ECO:0000250|UniProtKB:P23472"
FT   DISULFID        77..80
FT                   /evidence="ECO:0000250|UniProtKB:P23472"
FT   DISULFID        187..219
FT                   /evidence="ECO:0000250|UniProtKB:P23472"
SQ   SEQUENCE   330 AA;  36424 MW;  C920E91F25A98C19 CRC64;
     MVPQAKLVVA SLILTSALIQ TSEAVGGIAT YWGQYTETEE GSLAEACASN LYSYINIAYL
     NIFGEGRYLS LNISGHCSDC TFLGEEIKAC QSQGVKIFLS LGGPYGDYHL TTDGDADRVA
     EQLWSSFLGG SKSTGVYQPL LGDVELDGID LDIQIGPPEE YDVLARNLKD LTKDRTRPFY
     LSAAPKCSAY NDSDAYLWTA VETGLFDFVW VKFYNDTSCQ YNNDTAAGLD AFYRSWYDWT
     VSLAEGNKLL IGIPASNETD NSPLGGYIPS DVLNDQIVSV IMTSSKFGGV NVWNRYYDLK
     TNYSSSIILE YVNSGTKYLP LRTKFMYQNA
 
 
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