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B0Y665 (PLB1_ASPFC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Lysophospholipase 1

EC=3.1.1.5
Alternative name(s):
Phospholipase B 1
Gene names
Name:plb1
ORF Names:AFUB_065820
OrganismNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]
Taxonomic identifier451804 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length633 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the release of fatty acids from lysophospholipids.

Catalytic activity

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Ref.3 Ref.4.

Induction

Induced by lecithin. Ref.1

Post-translational modification

The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.

Sequence similarities

Belongs to the lysophospholipase family.

Contains 1 PLA2c domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processphospholipid catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

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 – 2020 Potential
Chain21 – 609589Lysophospholipase 1
PRO_0000372611
Propeptide610 – 63324Removed in mature form Potential
PRO_0000372612

Regions

Domain47 – 594548PLA2c

Amino acid modifications

Lipidation6091GPI-like-anchor amidated serine Potential
Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation2461N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential
Glycosylation3581N-linked (GlcNAc...) Potential
Glycosylation3971N-linked (GlcNAc...) Potential
Glycosylation4501N-linked (GlcNAc...) Potential
Glycosylation4631N-linked (GlcNAc...) Potential
Glycosylation4691N-linked (GlcNAc...) Potential
Glycosylation4971N-linked (GlcNAc...) Potential
Glycosylation5001N-linked (GlcNAc...) Potential
Glycosylation5211N-linked (GlcNAc...) Potential
Glycosylation5491N-linked (GlcNAc...) Potential
Glycosylation5551N-linked (GlcNAc...) Potential
Glycosylation5941N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
B0Y665 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 277A47E29FD74796

FASTA63368,144
        10         20         30         40         50         60 
MKTTTVACAV AGLLFSCVSG APDPVHVEIQ QRALPNAPDG YTPSTVGCPA SRPTIRSAAS 

        70         80         90        100        110        120 
LSPNETSWLE TRRGKTTSAM KDFFNHVKIQ DFDAAGYIDR HSSNSSDLPN IGIAVSGGGY 

       130        140        150        160        170        180 
RALMNGAGAI KAFDSRTPNS TSAGQLGGLL QSATYLSGLS GGSWLVGSIY INNFTTISAL 

       190        200        210        220        230        240 
QTHQKGTVWQ FQNSIFEGPD GGSIQILDSA TYYRDISNAV SGKSDAGYPT SITDYWGRAL 

       250        260        270        280        290        300 
SYQMINATNG GPSYTWSSIA LTDAFQKAEM PMPLVVADGR YPGELLISSN ATVYEFNPWE 

       310        320        330        340        350        360 
FGTFDPTVFG FAPLEYLGTK FNGGSVPSNE SCVRGFDNVG FVMGTSSTLF NQFLLQINST 

       370        380        390        400        410        420 
ALPDWLKSVF TDILKDIGEN DEDIAQYAPN PFYHFSNTTN PSAAELELDL VDGGEDLQNI 

       430        440        450        460        470        480 
PLHPLIQPER HVDVIFAVDS SADTTYSWPN GTALVATYER SLNSSGIANG TSFPAIPDQN 

       490        500        510        520        530        540 
TFVNKGLNTR PTFFGCNSSN TTGPSPLIVY LPNYPYTAYS NFSTFQPDYT EQERDSTILN 

       550        560        570        580        590        600 
GYDVVTMGNS TRDGNWSTCV GCAILSRSLE RTNTNVPEIC KQCFQRYCWD GSLNSTTPAG 

       610        620        630 
YEPVTILDSA ASGIIPSIST VAMAVVFAAW TIF 

« Hide

References

« Hide 'large scale' references
[1]"Characterisation and expression of phospholipases B from the opportunistic fungus Aspergillus fumigatus."
Shen D.-K., Noodeh A.D., Kazemi A., Grillot R., Robson G.D., Brugere J.-F.
FEMS Microbiol. Lett. 239:87-93(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[2]"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus."
Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. expand/collapse author list , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C.
PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CEA10 / CBS 144.89 / FGSC A1163.
[3]"Proteome analysis of Aspergillus fumigatus identifies glycosylphosphatidylinositol-anchored proteins associated to the cell wall biosynthesis."
Bruneau J.-M., Magnin T., Tagat E., Legrand R., Bernard M., Diaquin M., Fudali C., Latge J.-P.
Electrophoresis 22:2812-2823(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 89-100 AND 122-131, GPI-ANCHOR.
[4]"Structures of the glycosylphosphatidylinositol membrane anchors from Aspergillus fumigatus membrane proteins."
Fontaine T., Magnin T., Melhert A., Lamont D., Latge J.-P., Ferguson M.A.J.
Glycobiology 13:169-177(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 90-98, STRUCTURE OF GPI-ANCHOR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY376592 mRNA. Translation: AAQ85122.1.
DS499598 Genomic DNA. Translation: EDP50250.1.

3D structure databases

ProteinModelPortalB0Y665.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome8989. Asp f LPL1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUBT00006532; CADAFUBP00006407; CADAFUBG00006532.

Phylogenomic databases

HOGENOMHOG000189547.
OrthoDBEOG7N37NC.
PhylomeDBB0Y665.

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_ASPFC
AccessionPrimary (citable) accession number: B0Y665
Secondary accession number(s): Q4WPC0, Q6U820, Q9P8P5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: April 8, 2008
Last modified: April 16, 2014
This is version 28 of the entry and version 1 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