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P18632 (PLY1_CRYJA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pectate lyase 1

EC=4.2.2.2
Alternative name(s):
Allergen Cry j I
Major allergen Cry j 1
Sugi basic protein
Short name=SBP
Allergen=Cry j 1
OrganismCryptomeria japonica (Japanese cedar) (Cupressus japonica)
Taxonomic identifier3369 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaeCupressalesCupressaceaeCryptomeria

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has pectate lyase activity. Ref.5

Catalytic activity

Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends. Ref.5

Cofactor

Binds 1 calcium ion. Ref.5

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.

Post-translational modification

N-glycosylated; contains fucose and xylose. Ref.6 Ref.7

Allergenic properties

Causes an allergic reaction in human. This is one of the major allergens of Japanese cedar pollen, the most common pollen allergen in Japan.

Sequence similarities

Belongs to the polysaccharide lyase 1 family. Amb a subfamily.

Biophysicochemical properties

pH dependence:

Optimum pH is 10. Ref.5

Temperature dependence:

Optimum temperature is 60-70 degrees Celsius.

Ontologies

Keywords
   DiseaseAllergen
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processpectin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pectate lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.4
Chain22 – 374353Pectate lyase 1
PRO_0000024906

Sites

Active site2501 Potential
Metal binding1701Calcium By similarity
Metal binding1941Calcium By similarity
Metal binding1981Calcium By similarity

Amino acid modifications

Glycosylation1581N-linked (GlcNAc...) Potential
Glycosylation1911N-linked (GlcNAc...) (complex) Ref.6
CAR_000135
Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation3541N-linked (GlcNAc...) (complex) Ref.6
CAR_000136
Disulfide bond28 ↔ 45 By similarity
Disulfide bond128 ↔ 147 By similarity
Disulfide bond306 ↔ 312 By similarity

Experimental info

Sequence conflict121F → L in BAA05542. Ref.1
Sequence conflict1431Y → H in BAA05542. Ref.1
Sequence conflict2021T → S in BAA05542. Ref.1
Sequence conflict2211L → S in BAA05543. Ref.1
Sequence conflict3581Q → H in BAA05543. Ref.1
Sequence conflict3611K → Q in BAA05543. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P18632 [UniParc].

Last modified April 16, 2014. Version 3.
Checksum: 90D0085D24BF2BD4

FASTA37440,720
        10         20         30         40         50         60 
MDSPCLVALL VFSFVIGSCF SDNPIDSCWR GDSNWAQNRM KLADCAVGFG SSTMGGKGGD 

        70         80         90        100        110        120 
LYTVTNSDDD PVNPAPGTLR YGATRDRPLW IIFSGNMNIK LKMPMYIAGY KTFDGRGAQV 

       130        140        150        160        170        180 
YIGNGGPCVF IKRVSNVIIH GLYLYGCSTS VLGNVLINES FGVEPVHPQD GDALTLRTAT 

       190        200        210        220        230        240 
NIWIDHNSFS NSSDGLVDVT LTSTGVTISN NLFFNHHKVM LLGHDDAYSD DKSMKVTVAF 

       250        260        270        280        290        300 
NQFGPNCGQR MPRARYGLVH VANNNYDPWT IYAIGGSSNP TILSEGNSFT APNESYKKQV 

       310        320        330        340        350        360 
TIRIGCKTSS SCSNWVWQST QDVFYNGAYF VSSGKYEGGN IYTKKEAFNV ENGNATPQLT 

       370 
KNAGVLTCSL SKRC 

« Hide

References

[1]"Cloning and sequencing of cDNA coding for Cry j I, a major allergen of Japanese cedar pollen."
Sone T., Komiyama N., Shimizu K., Kusakabe T., Morikubo K., Kino K.
Biochem. Biophys. Res. Commun. 199:619-625(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Pollen.
[2]Namba M., Kurose M., Torigoe K., Fukuda S., Kurimoto M.
Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pollen.
[3]"Isolation and characterization of cDNAs encoding major allergen Cry j 1 from Cryptomeria japonica pollen."
Futamura N., Shinohara K.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pollen.
[4]"N-terminal amino acid sequence of a major allergen of Japanese cedar pollen (Cry j I)."
Taniai M., Ando S., Usui M., Kurimoto M., Sakaguchi M., Inouye S., Matuhasi T.
FEBS Lett. 239:329-332(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-41.
Tissue: Pollen.
[5]"Cry j I, a major allergen of Japanese cedar pollen, has pectate lyase enzyme activity."
Taniguchi Y., Ono A., Sawatani M., Nanba M., Kohno K., Usui M., Kurimoto M., Matuhasi T.
Allergy 50:90-93(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 250-266, FUNCTION AS A PECTATE LYASE, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
Tissue: Pollen.
[6]"Antigenicity of the oligosaccharide moiety of the Japanese cedar (Cryptomeria japonica) pollen allergen, Cry jI."
Hijikata A., Matsumoto I., Kojima K., Ogawa H.
Int. Arch. Allergy Immunol. 105:198-202(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-191 AND ASN-354.
Tissue: Pollen.
[7]"Carbohydrate structures of the glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen."
Hino K., Yamamoto S., Sano O., Taniguchi Y., Kohno K., Usui M., Fukuda S., Hanzawa H., Haruyama H., Kurimoto M.
J. Biochem. 117:289-295(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
Tissue: Pollen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D26544 mRNA. Translation: BAA05542.1.
D26545 mRNA. Translation: BAA05543.1.
D34639 mRNA. Translation: BAA07020.1.
AB081309 mRNA. Translation: BAB86286.1.
AB081310 mRNA. Translation: BAB86287.1.
PIRA44773.
JC2123.
JC2124.

3D structure databases

ProteinModelPortalP18632.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome248. Cry j 1.
3223. Cry j 1.0101.
3224. Cry j 1.0102.
3225. Cry j 1.0103.
CAZyPL1. Polysaccharide Lyase Family 1.

PTM databases

UniCarbKBP18632.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00545; UER00824.

Family and domain databases

Gene3D2.160.20.10. 1 hit.
InterProIPR002022. Amb_allergen_dom.
IPR018082. AmbAllergen.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
PRINTSPR00807. AMBALLERGEN.
SMARTSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMSSF51126. SSF51126. 1 hit.
ProtoNetSearch...

Entry information

Entry namePLY1_CRYJA
AccessionPrimary (citable) accession number: P18632
Secondary accession number(s): Q8RUR1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: April 16, 2014
Last modified: July 9, 2014
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Allergens

Nomenclature of allergens and list of entries