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Q9P8P2 (PLB1_CRYNH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exhibits phospholipase B (PLB), lysophospholipase (LPL) and lysophospholipase/transacylase (LPTA) activities.

Catalytic activity

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Enzyme regulation

Inhibited by Fe3+ ion.

Subcellular location

Secreted.

Post-translational modification

N-glycosylated.

Sequence similarities

Belongs to the lysophospholipase family.

Contains 1 PLA2c domain.

Caution

Ref.3 describes peptide sequences that do not match PLB1, but originate from a copurified, contaminating chitin deacetylase.

Biophysicochemical properties

pH dependence:

Active only at acidic pHs.

Sequence caution

The sequence AFR98312.2 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processphospholipid catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlysophospholipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 637618Phospholipase B
PRO_0000024636

Regions

Domain46 – 572527PLA2c

Amino acid modifications

Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation561N-linked (GlcNAc...) Potential
Glycosylation1221N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation2461N-linked (GlcNAc...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential
Glycosylation3141N-linked (GlcNAc...) Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation3871N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential
Glycosylation4811N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Glycosylation5281N-linked (GlcNAc...) Potential
Glycosylation5531N-linked (GlcNAc...) Potential
Glycosylation5721N-linked (GlcNAc...) Potential
Glycosylation5941N-linked (GlcNAc...) Potential
Glycosylation6061N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict61A → G in AAF65220. Ref.1
Sequence conflict6191K → N in AAF65220. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9P8P2 [UniParc].

Last modified February 6, 2013. Version 2.
Checksum: 7C052A69669B2276

FASTA63768,818
        10         20         30         40         50         60 
MSIATATFAF SLFATIAFAV PPETPRIELQ AERGLGDKSY APWQVDCPSN VTWIRNATTG 

        70         80         90        100        110        120 
LGSGERAYIE AREKLVQPVI EQMMAARGLE TPPRTPNIGV ALSGGGYRAM LTGLGGIMGM 

       130        140        150        160        170        180 
MNESTEASES ETGGWLDGVS YWAGLSGGSW ATGTFMSNGG QLPTNLLENL WNIDSNLVFP 

       190        200        210        220        230        240 
DDDKLSFYTE LYTETNAKSD LGFPIQITDV WGLAIGSHVL PERYQLSNTP NLTFSSLPSV 

       250        260        270        280        290        300 
VSALGNASLP MPIIIAADRK RREAGELVIA ENATVWEFTP YEFGSWAFGS QYKSPGAFTP 

       310        320        330        340        350        360 
IEYLGTSVDD GSPNGTCWKG FDQLSFVMGT SATLFNGAFL ELNGTDSGLL TNLITAFLAD 

       370        380        390        400        410        420 
LGEDQADISR IPNTFSNYNS GENPIYNLTY ITLVDAGETN QNIPLEPLLV PTRDVDAIVA 

       430        440        450        460        470        480 
FDSSYDTDYI WPNGTALRTT YERAKVLAEH ENTRVLMPEV PSMNGFVNGG YNSRPTFFGC 

       490        500        510        520        530        540 
NDTTTPLIIY VPSYPWSFAA NTSTYQLSYE NDEANEMLLN GMRSLTLNHS VPTWPTCFAC 

       550        560        570        580        590        600 
ALTDRSFMYT SENRSTTCQK CFDTWCWAGD DNTTEPATYE PVINSVPPWL VANNLSIGVA 

       610        620        630 
DAPASNESTA GTASSGAAKA DVSMGMVALA AGLGLML 

« Hide

References

« Hide 'large scale' references
[1]"Extracellular phospholipase activity is a virulence factor for Cryptococcus neoformans."
Cox G.M., McDade H.C., Chen S.C.A., Tucker S.C., Gottfredsson M., Wright L.C., Sorrell T.C., Leidich S.D., Casadevall A., Ghannoum M.A., Perfect J.R.
Mol. Microbiol. 39:166-175(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: H99 / ATCC 208821 / CBS 10515 / FGSC 9487.
[2]"Analysis of the genome and transcriptome of Cryptococcus neoformans var. grubii reveals complex RNA expression and microevolution leading to virulence attenuation."
Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V., Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F., Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A., Gaillardin C., Gerik K.J. expand/collapse author list , Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A., Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A., Cuomo C.A., Dietrich F.S.
PLoS Genet. 10:E1004261-E1004261(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H99 / ATCC 208821 / CBS 10515 / FGSC 9487.
[3]"Purification and characterization of secretory phospholipase B, lysophospholipase and lysophospholipase/transacylase from a virulent strain of the pathogenic fungus Cryptococcus neoformans."
Chen S.C.A., Wright L.C., Golding J.C., Sorrell T.C.
Biochem. J. 347:431-439(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: BL-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF223383 Genomic DNA. Translation: AAF65220.1.
CP003831 Genomic DNA. Translation: AFR98312.2. Sequence problems.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OrthoDBEOG7N37NC.

Family and domain databases

InterProIPR016035. Acyl_Trfase/lysoPLipase.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamPF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTSM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMSSF52151. SSF52151. 1 hit.
PROSITEPS51210. PLA2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLB1_CRYNH
AccessionPrimary (citable) accession number: Q9P8P2
Secondary accession number(s): J9VV08
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: February 6, 2013
Last modified: June 11, 2014
This is version 47 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families