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PGLR_CUPSE
ID   PGLR_CUPSE              Reviewed;         164 AA.
AC   C0HKB1;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2017, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Polygalacturonase {ECO:0000303|PubMed:28439939};
DE            EC=3.2.1.15 {ECO:0000250|UniProtKB:P05117};
DE   AltName: Allergen=Cup s 2 {ECO:0000303|PubMed:28439939};
DE   Flags: Fragments;
OS   Cupressus sempervirens (Italian cypress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC   Cupressus.
OX   NCBI_TaxID=13469 {ECO:0000303|PubMed:22287175};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-10, ALLERGEN, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Pollen {ECO:0000303|PubMed:28439939};
RX   PubMed=28439939; DOI=10.1111/all.13191;
RA   Shahali Y., Sutra J.P., Hilger C., Swiontek K., Haddad I., Vinh J.,
RA   Guilloux L., Charpin D., Senechal H., Poncet P.;
RT   "Identification of a polygalacturonase (Cup s 2) as the major CCD-bearing
RT   allergen in Cupressus sempervirens pollen.";
RL   Allergy 72:1806-1810(2017).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 11-164, ALLERGEN, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Pollen {ECO:0000303|PubMed:22287175};
RX   PubMed=22287175; DOI=10.1002/elps.201100324;
RA   Shahali Y., Sutra J.P., Haddad I., Vinh J., Guilloux L., Peltre G.,
RA   Senechal H., Poncet P.;
RT   "Proteomics of cypress pollen allergens using double and triple one-
RT   dimensional electrophoresis.";
RL   Electrophoresis 33:462-469(2012).
RN   [3] {ECO:0000305}
RP   ALLERGEN, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Pollen {ECO:0000303|PubMed:22813879};
RX   PubMed=22813879; DOI=10.1016/j.jprot.2012.07.010;
RA   Shahali Y., Sutra J.P., Fasoli E., D'Amato A., Righetti P.G., Futamura N.,
RA   Boschetti E., Senechal H., Poncet P.;
RT   "Allergomic study of cypress pollen via combinatorial peptide ligand
RT   libraries.";
RL   J. Proteomics 77:101-110(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC         galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC         Evidence={ECO:0000250|UniProtKB:P05117};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000250|UniProtKB:P05117}.
CC   -!- MASS SPECTROMETRY: Mass=56835; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:22813879};
CC   -!- ALLERGEN: Causes an allergenic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:22287175, ECO:0000269|PubMed:22813879,
CC       ECO:0000269|PubMed:28439939}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HKB1; -.
DR   Allergome; 10177; Cup s 2.
DR   Allergome; 11995; Cup s 2.0101.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 2.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   1: Evidence at protein level;
KW   Allergen; Cell wall; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Secreted.
FT   CHAIN           <1..>164
FT                   /note="Polygalacturonase"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000438848"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000303|PubMed:22287175"
FT   NON_CONS        23..24
FT                   /evidence="ECO:0000303|PubMed:22287175"
FT   NON_CONS        36..37
FT                   /evidence="ECO:0000303|PubMed:22287175"
FT   NON_CONS        43..44
FT                   /evidence="ECO:0000303|PubMed:22287175"
FT   NON_CONS        62..63
FT                   /evidence="ECO:0000303|PubMed:22287175"
FT   NON_CONS        90..91
FT                   /evidence="ECO:0000303|PubMed:22287175"
FT   NON_CONS        96..97
FT                   /evidence="ECO:0000303|PubMed:22287175"
FT   NON_CONS        138..139
FT                   /evidence="ECO:0000303|PubMed:22287175"
FT   NON_CONS        149..150
FT                   /evidence="ECO:0000303|PubMed:22287175"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:22287175"
FT   NON_TER         164
FT                   /evidence="ECO:0000303|PubMed:22287175"
SQ   SEQUENCE   164 AA;  17996 MW;  477646F12FD615DA CRC64;
     DVAIVFNVEH TLSAVFLVPA NKKVDGIIAA YPDPVKIWMH FARTVCNDKG RPTAIKIDFS
     KSELTLMNSP EFHLVFGECD GVKIQGIKIK RFEIEKDLTC GPGHGMSIGS LGKGNSRSEV
     SFVHLDGAKF IDTQNGLRSA VKIEDVTFKN ANGYYTNPLN PPCK
 
 
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