PLY1_CRYJA
ID PLY1_CRYJA Reviewed; 374 AA.
AC P18632; Q8RUR1;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 3.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Pectate lyase 1;
DE EC=4.2.2.2;
DE AltName: Full=Allergen Cry j I;
DE AltName: Full=Major allergen Cry j 1;
DE AltName: Full=Sugi basic protein;
DE Short=SBP;
DE AltName: Allergen=Cry j 1;
DE Flags: Precursor;
OS Cryptomeria japonica (Japanese cedar) (Cupressus japonica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Cryptomeria.
OX NCBI_TaxID=3369;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Pollen;
RX PubMed=8135802; DOI=10.1006/bbrc.1994.1273;
RA Sone T., Komiyama N., Shimizu K., Kusakabe T., Morikubo K., Kino K.;
RT "Cloning and sequencing of cDNA coding for Cry j I, a major allergen of
RT Japanese cedar pollen.";
RL Biochem. Biophys. Res. Commun. 199:619-625(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pollen;
RA Namba M., Kurose M., Torigoe K., Fukuda S., Kurimoto M.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pollen;
RA Futamura N., Shinohara K.;
RT "Isolation and characterization of cDNAs encoding major allergen Cry j 1
RT from Cryptomeria japonica pollen.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 22-41.
RC TISSUE=Pollen;
RX PubMed=3181436; DOI=10.1016/0014-5793(88)80945-1;
RA Taniai M., Ando S., Usui M., Kurimoto M., Sakaguchi M., Inouye S.,
RA Matuhasi T.;
RT "N-terminal amino acid sequence of a major allergen of Japanese cedar
RT pollen (Cry j I).";
RL FEBS Lett. 239:329-332(1988).
RN [5]
RP PROTEIN SEQUENCE OF 250-266, FUNCTION AS A PECTATE LYASE, CATALYTIC
RP ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Pollen;
RX PubMed=7741195; DOI=10.1111/j.1398-9995.1995.tb02489.x;
RA Taniguchi Y., Ono A., Sawatani M., Nanba M., Kohno K., Usui M.,
RA Kurimoto M., Matuhasi T.;
RT "Cry j I, a major allergen of Japanese cedar pollen, has pectate lyase
RT enzyme activity.";
RL Allergy 50:90-93(1995).
RN [6]
RP GLYCOSYLATION AT ASN-191 AND ASN-354.
RC TISSUE=Pollen;
RX PubMed=7920021; DOI=10.1159/000236826;
RA Hijikata A., Matsumoto I., Kojima K., Ogawa H.;
RT "Antigenicity of the oligosaccharide moiety of the Japanese cedar
RT (Cryptomeria japonica) pollen allergen, Cry jI.";
RL Int. Arch. Allergy Immunol. 105:198-202(1994).
RN [7]
RP STRUCTURE OF CARBOHYDRATES.
RC TISSUE=Pollen;
RX PubMed=7608114; DOI=10.1093/jb/117.2.289;
RA Hino K., Yamamoto S., Sano O., Taniguchi Y., Kohno K., Usui M., Fukuda S.,
RA Hanzawa H., Haruyama H., Kurimoto M.;
RT "Carbohydrate structures of the glycoprotein allergen Cry j I from Japanese
RT cedar (Cryptomeria japonica) pollen.";
RL J. Biochem. 117:289-295(1995).
CC -!- FUNCTION: Has pectate lyase activity. {ECO:0000269|PubMed:7741195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC their non-reducing ends.; EC=4.2.2.2;
CC Evidence={ECO:0000269|PubMed:7741195};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:7741195};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:7741195};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 10. {ECO:0000269|PubMed:7741195};
CC Temperature dependence:
CC Optimum temperature is 60-70 degrees Celsius.
CC {ECO:0000269|PubMed:7741195};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 2/5.
CC -!- PTM: N-glycosylated; contains fucose and xylose.
CC {ECO:0000269|PubMed:7920021}.
CC -!- ALLERGEN: Causes an allergic reaction in human. This is one of the
CC major allergens of Japanese cedar pollen, the most common pollen
CC allergen in Japan.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. Amb a
CC subfamily. {ECO:0000305}.
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DR EMBL; D26544; BAA05542.1; -; mRNA.
DR EMBL; D26545; BAA05543.1; -; mRNA.
DR EMBL; D34639; BAA07020.1; -; mRNA.
DR EMBL; AB081309; BAB86286.1; -; mRNA.
DR EMBL; AB081310; BAB86287.1; -; mRNA.
DR PIR; A44773; A44773.
DR PIR; JC2123; JC2123.
DR PIR; JC2124; JC2124.
DR AlphaFoldDB; P18632; -.
DR SMR; P18632; -.
DR Allergome; 248; Cry j 1.
DR Allergome; 3223; Cry j 1.0101.
DR Allergome; 3224; Cry j 1.0102.
DR Allergome; 3225; Cry j 1.0103.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR GlyConnect; 580; 4 N-Linked glycans (2 sites).
DR UniPathway; UPA00545; UER00824.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR018082; AmbAllergen.
DR InterPro; IPR002022; Pec_lyase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045032; PEL.
DR PANTHER; PTHR31683; PTHR31683; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR PRINTS; PR00807; AMBALLERGEN.
DR SMART; SM00656; Amb_all; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW Allergen; Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lyase; Metal-binding; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:3181436"
FT CHAIN 22..374
FT /note="Pectate lyase 1"
FT /id="PRO_0000024906"
FT ACT_SITE 250
FT /evidence="ECO:0000255"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:7920021"
FT /id="CAR_000135"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:7920021"
FT /id="CAR_000136"
FT DISULFID 28..45
FT /evidence="ECO:0000250"
FT DISULFID 128..147
FT /evidence="ECO:0000250"
FT DISULFID 306..312
FT /evidence="ECO:0000250"
FT CONFLICT 12
FT /note="F -> L (in Ref. 1; BAA05542)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="Y -> H (in Ref. 1; BAA05542)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="T -> S (in Ref. 1; BAA05542)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="L -> S (in Ref. 1; BAA05543)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="Q -> H (in Ref. 1; BAA05543)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="K -> Q (in Ref. 1; BAA05543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 40720 MW; 90D0085D24BF2BD4 CRC64;
MDSPCLVALL VFSFVIGSCF SDNPIDSCWR GDSNWAQNRM KLADCAVGFG SSTMGGKGGD
LYTVTNSDDD PVNPAPGTLR YGATRDRPLW IIFSGNMNIK LKMPMYIAGY KTFDGRGAQV
YIGNGGPCVF IKRVSNVIIH GLYLYGCSTS VLGNVLINES FGVEPVHPQD GDALTLRTAT
NIWIDHNSFS NSSDGLVDVT LTSTGVTISN NLFFNHHKVM LLGHDDAYSD DKSMKVTVAF
NQFGPNCGQR MPRARYGLVH VANNNYDPWT IYAIGGSSNP TILSEGNSFT APNESYKKQV
TIRIGCKTSS SCSNWVWQST QDVFYNGAYF VSSGKYEGGN IYTKKEAFNV ENGNATPQLT
KNAGVLTCSL SKRC
