Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pectate lyase 1

Gene
N/A
Organism
Cryptomeria japonica (Japanese cedar) (Cupressus japonica)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has pectate lyase activity.1 Publication

Catalytic activityi

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.1 Publication

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion.1 Publication

pH dependencei

Optimum pH is 10.1 Publication

Temperature dependencei

Optimum temperature is 60-70 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi170 – 1701CalciumBy similarity
Metal bindingi194 – 1941CalciumBy similarity
Metal bindingi198 – 1981CalciumBy similarity
Active sitei250 – 2501Sequence Analysis

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. pectate lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. pectin catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00545; UER00824.

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Names & Taxonomyi

Protein namesi
Recommended 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
OrganismiCryptomeria japonica (Japanese cedar) (Cupressus japonica)
Taxonomic identifieri3369 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaeCupressalesCupressaceaeCryptomeria

Pathology & Biotechi

Allergenic propertiesi

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

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei248. Cry j 1.
3223. Cry j 1.0101.
3224. Cry j 1.0102.
3225. Cry j 1.0103.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 374353Pectate lyase 1PRO_0000024906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 45By similarity
Disulfide bondi128 ↔ 147By similarity
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi191 – 1911N-linked (GlcNAc...) (complex)1 PublicationCAR_000135
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi306 ↔ 312By similarity
Glycosylationi354 – 3541N-linked (GlcNAc...) (complex)1 PublicationCAR_000136

Post-translational modificationi

N-glycosylated; contains fucose and xylose.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP18632.

Structurei

3D structure databases

ProteinModelPortaliP18632.
SMRiP18632. Positions 22-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR018082. AmbAllergen.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
PRINTSiPR00807. AMBALLERGEN.
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18632-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSPCLVALL VFSFVIGSCF SDNPIDSCWR GDSNWAQNRM KLADCAVGFG
60 70 80 90 100
SSTMGGKGGD LYTVTNSDDD PVNPAPGTLR YGATRDRPLW IIFSGNMNIK
110 120 130 140 150
LKMPMYIAGY KTFDGRGAQV YIGNGGPCVF IKRVSNVIIH GLYLYGCSTS
160 170 180 190 200
VLGNVLINES FGVEPVHPQD GDALTLRTAT NIWIDHNSFS NSSDGLVDVT
210 220 230 240 250
LTSTGVTISN NLFFNHHKVM LLGHDDAYSD DKSMKVTVAF NQFGPNCGQR
260 270 280 290 300
MPRARYGLVH VANNNYDPWT IYAIGGSSNP TILSEGNSFT APNESYKKQV
310 320 330 340 350
TIRIGCKTSS SCSNWVWQST QDVFYNGAYF VSSGKYEGGN IYTKKEAFNV
360 370
ENGNATPQLT KNAGVLTCSL SKRC
Length:374
Mass (Da):40,720
Last modified:April 16, 2014 - v3
Checksum:i90D0085D24BF2BD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121F → L in BAA05542 (PubMed:8135802).Curated
Sequence conflicti143 – 1431Y → H in BAA05542 (PubMed:8135802).Curated
Sequence conflicti202 – 2021T → S in BAA05542 (PubMed:8135802).Curated
Sequence conflicti221 – 2211L → S in BAA05543 (PubMed:8135802).Curated
Sequence conflicti358 – 3581Q → H in BAA05543 (PubMed:8135802).Curated
Sequence conflicti361 – 3611K → Q in BAA05543 (PubMed:8135802).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA44773.
JC2123.
JC2124.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA44773.
JC2123.
JC2124.

3D structure databases

ProteinModelPortaliP18632.
SMRiP18632. Positions 22-367.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei248. Cry j 1.
3223. Cry j 1.0101.
3224. Cry j 1.0102.
3225. Cry j 1.0103.
CAZyiPL1. Polysaccharide Lyase Family 1.

PTM databases

UniCarbKBiP18632.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00545; UER00824.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR018082. AmbAllergen.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
PRINTSiPR00807. AMBALLERGEN.
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPLY1_CRYJA
AccessioniPrimary (citable) accession number: P18632
Secondary accession number(s): Q8RUR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: April 16, 2014
Last modified: November 26, 2014
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.