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CRJ34_CRYJA
ID   CRJ34_CRYJA             Reviewed;         248 AA.
AC   Q5DWG2;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Pathogenesis-related thaumatin-like protein 3.4 {ECO:0000305};
DE   AltName: Allergen=Cry j 3.4 {ECO:0000303|PubMed:16203714};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   INDUCTION BY ETHYLENE; SALT STRESS; ARACHIDONIC ACID AND SALICYLIC 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   [2]
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   [3]
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   [4]
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   [5]
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: Mainly expressed in male and female strobili, and,
CC       at lower levels, in roots of seedlings and saplings.
CC       {ECO:0000269|PubMed:16203714}.
CC   -!- DEVELOPMENTAL STAGE: Mostly abundant in mature female strobili, with
CC       lower expression in developing female strobili and in mature male
CC       strobili. {ECO:0000269|PubMed:16203714}.
CC   -!- INDUCTION: Induced by ethylene (ethephon), salt stress and salicylic
CC       acid (SA) (PubMed:16203714). Strongly induced by arachidonic acid
CC       (PubMed:16203714). {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; AB186384; BAD90813.1; -; mRNA.
DR   AlphaFoldDB; Q5DWG2; -.
DR   SMR; Q5DWG2; -.
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   GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR   GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
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; Glycoprotein; Pathogenesis-related protein;
KW   Plant defense; Signal; Stress response.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..248
FT                   /note="Pathogenesis-related thaumatin-like protein 3.4"
FT                   /id="PRO_5004254470"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        34..227
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        75..85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        90..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        141..216
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        146..199
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        154..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        168..177
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        178..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
SQ   SEQUENCE   248 AA;  26513 MW;  C8D8204C019832E5 CRC64;
     MARAILWVLL TVMAVSLLLH AGVEGVNFDI ENQCPYTVWA AGTPFGGGIE LKRGQSWRVN
     VPGGARGRFW GRTGCSFDGN GRGRCNTGDC GGLLNCQGSG GVPSTLLEYA LNQYQNLDFY
     DISLVDGFNL RMTVVLSNTN CKRIACNSDI NSKCPGELKV VDGCRSACAA FNTPAYCCTG
     SFLDNCPPTG YSQFFKRECP LAYSYAKDDP TSTFTCPGGS DYKIIFCGNG DSQSNSTSTS
     SGSLYAVE
 
 
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