PRR3_HESAR
ID PRR3_HESAR Reviewed; 199 AA.
AC Q9FY35;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Pathogenesis-related 5 protein Cup a 3 {ECO:0000303|PubMed:15080828};
DE Short=PR-5 protein Cup a 3 {ECO:0000303|PubMed:15080828};
DE AltName: Full=Pollen protein Cup a 3 {ECO:0000303|PubMed:15080828};
DE AltName: Full=Thaumatin-like protein Cup a 3 {ECO:0000303|PubMed:18681086};
DE Short=TLP Cup a 3 {ECO:0000303|PubMed:18681086};
DE AltName: Allergen=Cup a 3 {ECO:0000303|PubMed:15080828, ECO:0000303|PubMed:18681086};
DE Flags: Fragment;
OS Hesperocyparis arizonica (Arizona cypress) (Cupressus arizonica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Hesperocyparis.
OX NCBI_TaxID=49011 {ECO:0000312|EMBL:CAC05258.1};
RN [1] {ECO:0000312|EMBL:CAC05258.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, AND ALLERGEN.
RC TISSUE=Pollen {ECO:0000303|PubMed:15080828};
RX PubMed=15080828; DOI=10.1046/j.1398-9995.2003.00363.x;
RA Cortegano I., Civantos E., Aceituno E., del Moral A., Lopez E.,
RA Lombardero M., del Pozo V., Lahoz C.;
RT "Cloning and expression of a major allergen from Cupressus arizonica
RT pollen, Cup a 3, a PR-5 protein expressed under polluted environment.";
RL Allergy 59:485-490(2004).
RN [2]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=18681086; DOI=10.1016/s1081-1206(10)60836-8;
RA Suarez-Cervera M., Castells T., Vega-Maray A., Civantos E., del Pozo V.,
RA Fernandez-Gonzalez D., Moreno-Grau S., Moral A., Lopez-Iglesias C.,
RA Lahoz C., Seoane-Camba J.A.;
RT "Effects of air pollution on cup a 3 allergen in Cupressus arizonica pollen
RT grains.";
RL Ann. Allergy Asthma Immunol. 101:57-66(2008).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15080828,
CC ECO:0000269|PubMed:18681086}. Secreted, extracellular space,
CC extracellular matrix, pollen coat {ECO:0000269|PubMed:18681086}.
CC Cytoplasm {ECO:0000269|PubMed:18681086}. Nucleus
CC {ECO:0000269|PubMed:18681086}. Mitochondrion
CC {ECO:0000269|PubMed:18681086}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:18681086}. Golgi apparatus, Golgi stack
CC {ECO:0000269|PubMed:18681086}. Vesicle {ECO:0000269|PubMed:18681086}.
CC Vacuole {ECO:0000269|PubMed:18681086}. Note=Localizes in orbicules,
CC walls, nucleus and to condensed dormant structures in the cytoplasm of
CC the mature nonhydrated pollen grains. Upon germination, localizes in
CC mitochondria, nucleus, endoplasmic reticulum, Golgi cisterns and
CC vesicles, vacuoles, lipid inclusions and the intine wall.
CC {ECO:0000269|PubMed:18681086}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen. {ECO:0000269|PubMed:15080828,
CC ECO:0000269|PubMed:18681086}.
CC -!- DEVELOPMENTAL STAGE: Expressed during dehydration, dormancy, air
CC dispersion, hydrated preactivated and germination stages. In hydrated
CC pollen grains, expressed in discarded exine, the exudates, and the
CC orbicules. Expressed in developing lamellate structures of the
CC microspore cell cytoplasm. {ECO:0000269|PubMed:18681086}.
CC -!- INDUCTION: By air pollution. {ECO:0000269|PubMed:15080828,
CC ECO:0000269|PubMed:18681086}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 63% of
CC 104 patients allergic to cypress pollen. {ECO:0000269|PubMed:15080828}.
CC -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00699, ECO:0000305}.
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DR EMBL; AJ294411; CAC05258.1; -; mRNA.
DR AlphaFoldDB; Q9FY35; -.
DR SMR; Q9FY35; -.
DR Allergome; 898; Cup a 3.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0043668; C:exine; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0031985; C:Golgi cisterna; IDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IDA:UniProtKB.
DR GO; GO:0043678; C:intine; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070505; C:pollen coat; IDA:UniProtKB.
DR GO; GO:0070645; C:Ubisch body; IDA:UniProtKB.
DR GO; GO:0005773; C:vacuole; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0009846; P:pollen germination; IEP:UniProtKB.
DR GO; GO:0009859; P:pollen hydration; IDA:UniProtKB.
DR Gene3D; 2.60.110.10; -; 1.
DR InterPro; IPR037176; Osmotin/thaumatin-like_sf.
DR InterPro; IPR001938; Thaumatin.
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; PS51367; THAUMATIN_2; 1.
PE 1: Evidence at protein level;
KW Allergen; Cytoplasm; Disulfide bond; Endoplasmic reticulum;
KW Extracellular matrix; Golgi apparatus; Mitochondrion; Nucleus; Secreted;
KW Stress response; Vacuole.
FT CHAIN <1..199
FT /note="Pathogenesis-related 5 protein Cup a 3"
FT /id="PRO_0000446451"
FT DISULFID 9..198
FT /evidence="ECO:0000255|PIRSR:PIRSR002703-1,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 50..60
FT /evidence="ECO:0000255|PIRSR:PIRSR002703-1,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 65..71
FT /evidence="ECO:0000255|PIRSR:PIRSR002703-1,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 113..187
FT /evidence="ECO:0000255|PIRSR:PIRSR002703-1,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 118..171
FT /evidence="ECO:0000255|PIRSR:PIRSR002703-1,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 126..136
FT /evidence="ECO:0000255|PIRSR:PIRSR002703-1,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 140..149
FT /evidence="ECO:0000255|PIRSR:PIRSR002703-1,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 150..158
FT /evidence="ECO:0000255|PIRSR:PIRSR002703-1,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:CAC05258.1"
SQ SEQUENCE 199 AA; 21010 MW; C12BB1DCDF663848 CRC64;
VKFDIKNQCG YTVWAAGLPG GGKEFDQGQT WTVNLAAGTA SARFWGRTGC TFDASGKGSC
RSGDCGGQLS CTVSGAVPAT LAEYTQSDQD YYDVSLVDGF NIPLAINPTN TKCTAPACKA
DINAVCPSEL KVDGGCNSAC NVLQTDQYCC RNAYVNNCPA TNYSKIFKNQ CPQAYSYAKD
DTATFACASG TDYSIVFCP
