PLA1_PLAAC
ID PLA1_PLAAC Reviewed; 179 AA.
AC Q8GT41; P82817;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Putative invertase inhibitor;
DE AltName: Full=Pollen allergen Pla a 1 {ECO:0000303|PubMed:11906336, ECO:0000303|PubMed:12859456, ECO:0000303|PubMed:16179793, ECO:0000303|PubMed:17177673, ECO:0000303|Ref.4};
DE AltName: Allergen=Pla a 1.0101 {ECO:0000305};
DE Flags: Precursor;
OS Platanus acerifolia (London plane tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Platanaceae; Platanus.
OX NCBI_TaxID=140101;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-35; 49-55; 61-71;
RP 113-121 AND 151-158, TISSUE SPECIFICITY, AND ALLERGEN.
RC TISSUE=Pollen {ECO:0000303|PubMed:12859456};
RX PubMed=12859456; DOI=10.1046/j.1365-2222.2003.01707.x;
RA Asturias J.A., Ibarrola I., Eraso E., Arilla M.C., Martinez A.;
RT "The major Platanus acerifolia pollen allergen Pla a 1 has sequence
RT homology to invertase inhibitors.";
RL Clin. Exp. Allergy 33:978-985(2003).
RN [2]
RP PROTEIN SEQUENCE OF 24-35, SUBUNIT, TISSUE SPECIFICITY, PTM, AND ALLERGEN.
RC TISSUE=Pollen {ECO:0000303|PubMed:11906336};
RX PubMed=11906336; DOI=10.1034/j.1398-9995.2002.03406.x;
RA Asturias J.A., Ibarrola I., Bartolome B., Ojeda I., Malet A., Martinez A.;
RT "Purification and characterization of Pla a 1, a major allergen from
RT Platanus acerifolia pollen.";
RL Allergy 57:221-227(2002).
RN [3]
RP TISSUE SPECIFICITY, ALLERGEN, AND BIOTECHNOLOGY.
RX PubMed=16179793; DOI=10.1159/000088434;
RA Arilla M.C., Ibarrola I., Mir A., Monteseirin J., Conde J., Martinez A.,
RA Asturias J.A.;
RT "Development of a sandwich-type ELISA for measuring Pla a 1, the major
RT allergen of Platanus acerifolia pollen.";
RL Int. Arch. Allergy Immunol. 138:127-133(2005).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX DOI=10.1007/s00497-005-0002-4;
RA Suarez-Cervera M., Asturias J.A., Vega-Maray A., Castells T.,
RA Lopez-Iglesias C., Ibarrola I., Arilla M.C., Gabarayeva N.,
RA Seoane-Camba J.A.;
RT "The role of allergenic proteins Pla a 1 and Pla a 2 in the germination of
RT Platanus acerifolia pollen grains.";
RL Sex. Plant Reprod. 18:101-112(2005).
RN [5]
RP TISSUE SPECIFICITY, ALLERGEN, AND BIOTECHNOLOGY.
RX PubMed=17177673; DOI=10.1111/j.1365-2222.2006.02591.x;
RA Asturias J.A., Ibarrola I., Amat P., Tella R., Malet A., Cistero-Bahima A.,
RA Enrique E., Malek T., Martinez A.;
RT "Purified allergens vs. complete extract in the diagnosis of plane tree
RT pollen allergy.";
RL Clin. Exp. Allergy 36:1505-1512(2006).
CC -!- FUNCTION: Invertase inhibitor (Probable). {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11906336}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.4}. Secreted, cell wall
CC {ECO:0000269|Ref.4}. Endoplasmic reticulum {ECO:0000269|Ref.4}.
CC Note=After 5 min in germination medium, detected as a soluble protein
CC and released from apertural and non-apertural regions of pollen grain
CC wall. In mature, non-hydrated pollen grains, predominantly associated
CC with the endoplasmic reticulum (ER) concentric cisternae, which are
CC situated between the vegetative nucleus and the generative cell. After
CC 5, 15 and 30 min as well as 2 h of hydration, localization to this ER
CC region is noticeably decreased. {ECO:0000269|Ref.4}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level)
CC (PubMed:12859456, PubMed:11906336, PubMed:16179793, Ref.4,
CC PubMed:17177673). Expressed in stem, but not leaves (at protein level)
CC (PubMed:12859456). Expressed in pollen (PubMed:12859456).
CC {ECO:0000269|PubMed:11906336, ECO:0000269|PubMed:12859456,
CC ECO:0000269|PubMed:16179793, ECO:0000269|PubMed:17177673,
CC ECO:0000269|Ref.4}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:11906336}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to London plane tree pollen (PubMed:12859456,
CC PubMed:11906336, PubMed:16179793, PubMed:17177673). Binds to IgE in 83%
CC of the 42 patients tested (PubMed:12859456). Binds to IgE in 92% of the
CC 12 patients tested (PubMed:11906336). Binds to IgE in 79% of the 47
CC Spanish patients tested (PubMed:16179793). Binds to IgE in 75% of the
CC 26 patients tested (PubMed:17177673). Binds to IgE in 83% of the 18
CC patients tested allergic London plane tree pollen as well as other
CC pollens including grass and olive (PubMed:11906336).
CC {ECO:0000269|PubMed:11906336, ECO:0000269|PubMed:12859456,
CC ECO:0000269|PubMed:16179793, ECO:0000269|PubMed:17177673}.
CC -!- BIOTECHNOLOGY: The developed two-site sandwich ELISA assay to quantify
CC this protein in P.acerifolia pollen extracts could be useful for the
CC quality control of allergen preparations intended for clinical use
CC (PubMed:16179793). Could be used together with allergen Pla a 2 for a
CC reliable diagnosis of London plane tree (P.acerifolia) pollen allergy
CC by skin prick test (SPT) in most patients of the cohort of 47 tested
CC with a sensitivity of over 90% and a specificity of 100%
CC (PubMed:17177673). {ECO:0000269|PubMed:16179793,
CC ECO:0000269|PubMed:17177673}.
CC -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
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DR EMBL; AJ427413; CAD20556.1; -; mRNA.
DR AlphaFoldDB; Q8GT41; -.
DR SMR; Q8GT41; -.
DR Allergome; 3425; Pla a 1.0101.
DR Allergome; 572; Pla a 1.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0043667; C:pollen wall; IDA:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:InterPro.
DR GO; GO:0009555; P:pollen development; IEP:UniProtKB.
DR GO; GO:0009846; P:pollen germination; IEP:UniProtKB.
DR CDD; cd15795; PMEI-Pla_a_1_like; 1.
DR Gene3D; 1.20.140.40; -; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR InterPro; IPR034088; Pla_a_1-like.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 1.
PE 1: Evidence at protein level;
KW Allergen; Cell wall; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:11906336,
FT ECO:0000269|PubMed:12859456"
FT CHAIN 24..179
FT /note="Putative invertase inhibitor"
FT /evidence="ECO:0000305|PubMed:11906336,
FT ECO:0000305|PubMed:12859456"
FT /id="PRO_0000024708"
FT DISULFID 31..46
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT DISULFID 102..142
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
SQ SEQUENCE 179 AA; 19282 MW; 152B025E98879C5A CRC64;
MKLSFSLCIF FFNLLLLLQA VISADIVQGT CKKVAQRSPN VNYDFCVKSL GADPKSHTAD
LQGLGVISAN LAIQHGSKIQ TFIGRILKSK VDPALKKYLN DCVGLYADAK SSVQEAIADF
KSKDYASANV KMSAALDDSV TCEDGFKEKK GIVSPVTKEN KDYVQLTAIS LAITKLLGA
