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B0XZV8 (PLB3_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 3

EC=3.1.1.5
Alternative name(s):
Phospholipase B 3
Gene names
Name:plb3
ORF Names:AFUB_034540
OrganismNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]
Taxonomic identifier451804 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length630 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.

Induction

Strongly induced by lecithin. Ref.1

Post-translational modification

The GPI-like anchor contains a phosphoceramide lipid group.

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
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 – 1616 Potential
Chain17 – 606590Lysophospholipase 3
PRO_0000372613
Propeptide607 – 63024Removed in mature form Potential
PRO_0000372614

Regions

Domain39 – 587549PLA2c

Amino acid modifications

Lipidation6061GPI-like-anchor amidated asparagine Potential
Glycosylation561N-linked (GlcNAc...) Potential
Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation3511N-linked (GlcNAc...) Potential
Glycosylation3901N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Glycosylation4621N-linked (GlcNAc...) Potential
Glycosylation4931N-linked (GlcNAc...) Potential
Glycosylation5141N-linked (GlcNAc...) Potential
Glycosylation5421N-linked (GlcNAc...) Potential
Glycosylation5661N-linked (GlcNAc...) Potential
Glycosylation5831N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict701Q → E in AAQ85123. Ref.1
Sequence conflict5421N → D in AAQ85123. Ref.1
Sequence conflict6181G → S in AAQ85123. Ref.1

Sequences

Sequence LengthMass (Da)Tools
B0XZV8 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 0E83E7D7F149CA08

FASTA63067,417
        10         20         30         40         50         60 
MKALLSLLTA VAVATATPLD LSLRALPNAP DGYTPAKVSC PATRPSIRGA GSLSPNETSW 

        70         80         90        100        110        120 
LEIRRKNTVQ PMTDLLGRLN LGFDAAGYID RVSSNASNLP NIAIAVSGGG YRALTNGAGA 

       130        140        150        160        170        180 
IKAFDSRTQG STQSGHLGGL LQSATYVSGL SGGGWLVGSV YLNNFTTIAD LQSGDHGNVW 

       190        200        210        220        230        240 
QFSTSILEGP KAKHLQFLST ADYWKDLLKA VDGKSDAGFN TSLTDYWGRA LSYQFINDRT 

       250        260        270        280        290        300 
GNGGLSYTWS SIALTDPFRR GEMPLPILVA DGRNPGELLI GSNSTVYEFN PWEFGSFDPS 

       310        320        330        340        350        360 
IFGFAPLEYL GSRFDNGQLP RGEPCVRGFD NAGFVMGTSS SLFNQFILRL NKTDLPDLAK 

       370        380        390        400        410        420 
DVFSKILTAI GRDGDDIAVY GPNPFYGYRN STAAYSRSRE LDVVDGGEDG QNIPLHPLIQ 

       430        440        450        460        470        480 
PVRHVDVIFA VDSSADGPYS WPNGSALVAT YERSLNSSGI GNGTVFPAVP DVNTFVNLGL 

       490        500        510        520        530        540 
NTRPTFFGCD PANLSAPAPL VVYLPNAPYS THSNTSTFQL AYSDSERDEI ITNGYNVVTR 

       550        560        570        580        590        600 
GNATVDKSWP SCVGCAILQR SMYRTNTSMP AVCNSCFKEY CWNGTVDSKT PRTYEPTLLL 

       610        620        630 
GSTSTNAAYT QGVTWLVGIL AVGVAMGMTA 

« 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]"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: STRUCTURE OF GPI-ANCHOR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY376593 mRNA. Translation: AAQ85123.1.
DS499596 Genomic DNA. Translation: EDP52290.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome8988. Asp f LPL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUBT00003440; CADAFUBP00003378; CADAFUBG00003440.

Phylogenomic databases

HOGENOMHOG000189547.
OrthoDBEOG7N37NC.
PhylomeDBB0XZV8.

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 namePLB3_ASPFC
AccessionPrimary (citable) accession number: B0XZV8
Secondary accession number(s): Q4WYY4, Q6U819
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