ID   AL11B_OLEEU             Reviewed;         364 AA.
AC   B2VPR8;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Pectinesterase 2;
DE            EC=3.1.1.11;
DE   AltName: Full=Pollen allergen Ole e 11.0102;
DE            Short=Ole e 11-2;
DE   AltName: Allergen=Ole e 11.0102;
DE   Flags: Precursor;
OS   Olea europaea (Common olive).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Oleaceae; Oleeae; Olea.
OX   NCBI_TaxID=4146;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-32; 252-276 AND 354-359,
RP   GLYCOSYLATION AT ASN-103, 3D-STRUCTURE MODELING, AND TISSUE SPECIFICITY.
RC   TISSUE=Pollen;
RX   PubMed=20491902; DOI=10.1111/j.1742-4658.2010.07689.x;
RA   Salamanca G., Rodriguez R., Quiralte J., Moreno C., Pascual C.Y.,
RA   Barber D., Villalba M.;
RT   "Pectin methylesterases of pollen tissue, a major allergen in olive tree.";
RL   FEBS J. 277:2729-2739(2010).
RN   [2]
RP   3D-STRUCTURE MODELING.
RX   PubMed=22722698; DOI=10.1007/s00894-012-1492-2;
RA   Jimenez-Lopez J.C., Kotchoni S.O., Rodriguez-Garcia M.I., Alche J.D.;
RT   "Structure and functional features of olive pollen pectin methylesterase
RT   using homology modeling and molecular docking methods.";
RL   J. Mol. Model. 18:4965-4984(2012).
RN   [3]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=22385802; DOI=10.1016/j.talanta.2012.01.016;
RA   Esteve C., Montealegre C., Marina M.L., Garcia M.C.;
RT   "Analysis of olive allergens.";
RL   Talanta 92:1-14(2012).
CC   -!- FUNCTION: Catalyzes the demethylesterification of homogalacturonan
CC       components of pectin. May be involved in pollen tube development (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC         [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC         Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC         ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 1/5.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in pollen. {ECO:0000269|PubMed:20491902}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:20491902}.
CC   -!- POLYMORPHISM: Several isoforms of the allergen exist due to
CC       polymorphism.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Allergen from olive
CC       pollen. Important in Mediterranean countries and California. Its
CC       prevalence is related to the geographic area.
CC   -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR   EMBL; DQ026502; AAY88919.1; -; mRNA.
DR   AlphaFoldDB; B2VPR8; -.
DR   SMR; B2VPR8; -.
DR   Allergome; 5966; Ole e 11.
DR   Allergome; 8780; Ole e 11.0102.
DR   iPTMnet; B2VPR8; -.
DR   BRENDA; 3.1.1.11; 4398.
DR   UniPathway; UPA00545; UER00823.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR033131; Pectinesterase_Asp_AS.
DR   InterPro; IPR000070; Pectinesterase_cat.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS00503; PECTINESTERASE_2; 1.
PE   1: Evidence at protein level;
KW   Allergen; Aspartyl esterase; Direct protein sequencing; Glycoprotein;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..364
FT                   /note="Pectinesterase 2"
FT                   /id="PRO_5000371839"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:20491902"
SQ   SEQUENCE   364 AA;  39653 MW;  E4E8078B091FC92A CRC64;
     MSCIAVEAVL LGILLYIPIV LSDDRAPIPA NSAQLNSWFD GIIQPVAVRK ATMDPALVTA
     EGQAKVIKLK SDGSGDFKSI NEAIKSIPDD NTKRVILSFS PGNYSEKVKI GMYKHYITFY
     GEDPNNMPIL VFGGTAAEYG TVDSATLIVE SNYFSAVNLK IVNSAPRPDG KRVGAQAAAL
     RISGDKASFY NVKIYGFQDT LCDDKGKHFY KDCYIEGTVD FIFGSGKSIF LNTELHAVPG
     DQPAIITAQA RKTESEDTGY YFVNCRVTGG GAFLGRSWMP AAKVVFAYTE MGDAIHPEGW
     ILVKPEHEST VRFPEYNNKG PGANMEKRAK FVKRLSDAEA KQSISLGSIE ASKWLLPPRV
     VGLP