PRR3_JUNAS
ID PRR3_JUNAS Reviewed; 225 AA.
AC P81295;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Pathogenesis-related 5 protein Jun a 3.0101 {ECO:0000305};
DE Short=PR-5 protein Jun a 3.0101 {ECO:0000305};
DE AltName: Full=Pollen allergen Jun a 3 {ECO:0000303|PubMed:10657673};
DE AltName: Allergen=Jun a 3.0101 {ECO:0000305};
DE Flags: Precursor;
OS Juniperus ashei (Ozark white cedar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Juniperus.
OX NCBI_TaxID=13101;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-70; 72-74; 84-112;
RP 178-190; 192-193 AND 195, TISSUE SPECIFICITY, AND ALLERGEN.
RC TISSUE=Pollen {ECO:0000303|PubMed:10657673};
RX PubMed=10657673; DOI=10.4049/jimmunol.164.4.2188;
RA Midoro-horiuti T., Goldblum R.M., Kurosky A., Goetz D.W., Brooks E.G.;
RT "Variable expression of pathogenesis-related protein allergen in mountain
RT cedar (Juniperus ashei) pollen.";
RL J. Immunol. 164:2188-2192(2000).
RN [2]
RP TISSUE SPECIFICITY, ALLERGEN, REGIONS, 3D-STRUCTURE MODELING, AND CIRCULAR
RP DICHROISM ANALYSIS.
RX PubMed=10969020; DOI=10.1016/s0006-3495(00)76410-1;
RA Soman K.V., Midoro-Horiuti T., Ferreon J.C., Goldblum R.M., Brooks E.G.,
RA Kurosky A., Braun W., Schein C.H.;
RT "Homology modeling and characterization of IgE binding epitopes of mountain
RT cedar allergen Jun a 3.";
RL Biophys. J. 79:1601-1609(2000).
RN [3]
RP ALLERGEN, AND BIOTECHNOLOGY.
RX PubMed=18270658; DOI=10.1007/s10529-008-9665-x;
RA Moehnke M.H., Midoro-Horiuti T., Goldblum R.M., Kearney C.M.;
RT "The expression of a mountain cedar allergen comparing plant-viral
RT apoplastic and yeast expression systems.";
RL Biotechnol. Lett. 30:1259-1264(2008).
CC -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level).
CC {ECO:0000269|PubMed:10657673, ECO:0000269|PubMed:10969020}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in
CC patients allergic to the pollen of cedar tree (PubMed:10657673,
CC PubMed:10969020, PubMed:18270658). Native protein binds to IgE in 43%
CC of the 14 patients and in 33% of the 36 patients tested allergic to the
CC pollen of mountain cedar or Japanese cedar, respectively
CC (PubMed:10657673). Recombinant protein binds to IgE of patients
CC allergic to mountain cedar pollen (PubMed:18270658).
CC {ECO:0000269|PubMed:10657673, ECO:0000269|PubMed:10969020,
CC ECO:0000269|PubMed:18270658}.
CC -!- BIOTECHNOLOGY: Extracting this recombinant allergen by vacuum
CC infiltration from the plant (Nicotiana benthamiana) apoplast via
CC tobacco mosaic virus vector could be useful in diagnostic and/or
CC immunotherapeutic strategies for cedar allergy as it is a more
CC convenient and inexpensive method than expression in the yeast (Pichia
CC pastoris) secretion system. {ECO:0000269|PubMed:18270658}.
CC -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00699}.
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DR EMBL; AF121776; AAF31759.1; -; mRNA.
DR AlphaFoldDB; P81295; -.
DR SMR; P81295; -.
DR Allergome; 3340; Jun a 3.0101.
DR Allergome; 429; Jun a 3.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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; Direct protein sequencing; Disulfide bond;
KW Pathogenesis-related protein; Plant defense; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:10657673"
FT CHAIN 27..225
FT /note="Pathogenesis-related 5 protein Jun a 3.0101"
FT /evidence="ECO:0000305|PubMed:10657673"
FT /id="PRO_0000034030"
FT REGION 146..157
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:10969020"
FT REGION 158..170
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:10969020"
FT REGION 178..191
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:10969020"
FT DISULFID 35..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 76..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 91..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 139..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 144..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 152..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 166..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 176..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT CONFLICT 58
FT /note="T -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 23720 MW; A24099C8E2B127F6 CRC64;
MARVSELAFL LAATLAISLH MQEAGVVKFD IKNQCGYTVW AAGLPGGGKR LDQGQTWTVN
LAAGTASARF WGRTGCTFDA SGKGSCQTGD CGGQLSCTVS GAVPATLAEY TQSDQDYYDV
SLVDGFNIPL AINPTNAQCT APACKADINA VCPSELKVDG GCNSACNVFK TDQYCCRNAY
VDNCPATNYS KIFKNQCPQA YSYAKDDTAT FACASGTDYS IVFCP
