CRJ33_CRYJA
ID CRJ33_CRYJA Reviewed; 230 AA.
AC Q8H994;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Pathogenesis-related thaumatin-like protein 3.3 {ECO:0000305};
DE AltName: Allergen=Cry j 3.3 {ECO:0000303|PubMed:12506996, ECO:0000303|PubMed:16203714};
DE Flags: Precursor; Fragment;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Boka-sugi; TISSUE=Pollen;
RX PubMed=12506996; DOI=10.1271/bbb.66.2495;
RA Futamura N., Mukai Y., Sakaguchi M., Yasueda H., Inouye S.,
RA Midoro-Horiuti T., Goldblum R.M., Shinohara K.;
RT "Isolation and characterization of cDNAs that encode homologs of a
RT pathogenesis-related protein allergen from Cryptomeria japonica.";
RL Biosci. Biotechnol. Biochem. 66:2495-2500(2002).
RN [2]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY ARACHIDONIC ACID,
RP GENE FAMILY, AND NOMENCLATURE.
RC TISSUE=Pollen;
RX PubMed=16203714; DOI=10.1093/treephys/26.1.51;
RA Futamura N., Tani N., Tsumura Y., Nakajima N., Sakaguchi M., Shinohara K.;
RT "Characterization of genes for novel thaumatin-like proteins in Cryptomeria
RT japonica.";
RL Tree Physiol. 26:51-62(2006).
RN [3]
RP ALLERGEN.
RC TISSUE=Flower;
RX PubMed=17441795; DOI=10.1111/j.1398-9995.2007.01331.x;
RA Fujimura T., Futamura N., Midoro-Horiuti T., Togawa A., Goldblum R.M.,
RA Yasueda H., Saito A., Shinohara K., Masuda K., Kurata K., Sakaguchi M.;
RT "Isolation and characterization of native Cry j 3 from Japanese cedar
RT (Cryptomeria japonica) pollen.";
RL Allergy 62:547-553(2007).
RN [4]
RP REVIEW ON THAUMATIN-LIKE PROTEINS.
RX PubMed=20204373; DOI=10.1007/s00299-010-0826-8;
RA Liu J.-J., Sturrock R., Ekramoddoullah A.K.M.;
RT "The superfamily of thaumatin-like proteins: its origin, evolution, and
RT expression towards biological function.";
RL Plant Cell Rep. 29:419-436(2010).
RN [5]
RP ALLERGEN.
RC TISSUE=Pollen;
RX PubMed=22749702; DOI=10.1016/j.vetimm.2012.06.007;
RA Kubota S., Miyaji K., Shimo Y., Shimakura H., Takase Y., Okamoto N.,
RA Kiuchi A., Fujimura M., Fujimura T., DeBoer D.J., Tsukui T., Sakaguchi M.;
RT "IgE reactivity to a Cry j 3, an allergen of Japanese cedar (Cryptomeria
RT japonica) pollen in dogs with canine atopic dermatitis.";
RL Vet. Immunol. Immunopathol. 149:132-135(2012).
RN [6]
RP REVIEW ON ALLERGEN.
RX PubMed=26433527; DOI=10.1016/j.alit.2015.05.008;
RA Fujimura T., Kawamoto S.;
RT "Spectrum of allergens for Japanese cedar pollinosis and impact of
RT component-resolved diagnosis on allergen-specific immunotherapy.";
RL Allergol. Int. 64:312-320(2015).
CC -!- FUNCTION: May be involved in disease resistance.
CC {ECO:0000303|PubMed:20204373}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in female and male strobili,
CC and, to a lower extent, in cotyledons, leaves and pollen grains.
CC {ECO:0000269|PubMed:12506996, ECO:0000269|PubMed:16203714}.
CC -!- DEVELOPMENTAL STAGE: Mostly abundant in mature male strobili, with
CC strong expression in mature female strobili but absent from developing
CC strobili. {ECO:0000269|PubMed:16203714}.
CC -!- INDUCTION: Weakly induced by arachidonic acid.
CC {ECO:0000269|PubMed:16203714}.
CC -!- ALLERGEN: Causes an oral allergy syndrome (OAS) reaction in human and
CC animals (PubMed:22749702, PubMed:26433527, PubMed:17441795). Binds to
CC IgE and induces the release of histamine from leukocytes of allergic
CC patients (PubMed:17441795). Binds to IgE from canine atopic dermatitis
CC (CAD) sensitive dogs (PubMed:22749702). {ECO:0000269|PubMed:17441795,
CC ECO:0000269|PubMed:22749702, ECO:0000303|PubMed:26433527}.
CC -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00699}.
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DR EMBL; AB081305; BAC15616.1; -; mRNA.
DR AlphaFoldDB; Q8H994; -.
DR SMR; Q8H994; -.
DR Allergome; 805; Cry j 3.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1904550; P:response to arachidonic acid; IEP:UniProtKB.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR Gene3D; 2.60.110.10; -; 1.
DR InterPro; IPR037176; Osmotin/thaumatin-like_sf.
DR InterPro; IPR001938; Thaumatin.
DR InterPro; IPR017949; Thaumatin_CS.
DR PANTHER; PTHR31048; PTHR31048; 1.
DR Pfam; PF00314; Thaumatin; 1.
DR PIRSF; PIRSF002703; Thaumatin; 1.
DR PRINTS; PR00347; THAUMATIN.
DR SMART; SM00205; THN; 1.
DR SUPFAM; SSF49870; SSF49870; 1.
DR PROSITE; PS00316; THAUMATIN_1; 1.
DR PROSITE; PS51367; THAUMATIN_2; 1.
PE 1: Evidence at protein level;
KW Allergen; Disulfide bond; Pathogenesis-related protein; Plant defense;
KW Signal; Stress response.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..230
FT /note="Pathogenesis-related thaumatin-like protein 3.3"
FT /id="PRO_5004308266"
FT DISULFID 33..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 74..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 89..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 142..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 148..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 156..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 170..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 180..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:BAC15616.1"
SQ SEQUENCE 230 AA; 24463 MW; DC9B8BA19BC30C22 CRC64;
RAIGVWIALV AALSVFLHGM EVRAATFDIT NQCPYTVWAA ASPGGGQQLD QGQTWTIQVA
AGTTQARIWA RTGCSFDGSG RGTCQTGDCN GMLSCQGYGQ VPATLAEYAL NQYMNLDFYD
ISLVDGFNVP LSMTPTSTDP NCKGRIACLS DINSQCPSDL KVTGGCKSAC ARYNTPEYCC
TGASENTCGP TDYSKFFKGQ CPQAYSYAKD DATSTFTCPS GTNYKVVFCG
