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O59863 (PLB_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 79. 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

EC=3.1.1.5
Alternative name(s):
KlPLB
Phospholipase B
Gene names
Name:PLB
Ordered Locus Names:KLLA0C05940g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length640 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. At acidic pH the enzyme hydrolyzes all phospholipid substrates without metal ion. On the other hand, at alkaline pH the enzyme shows substrate specificity for phosphatidylcholine and lysophosphatidylcholine and requires Ca2+, Fe3+, or Al3+ for the activity.

Catalytic activity

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Subcellular location

Secreted Probable.

Post-translational modification

Highly glycosylated.

Sequence similarities

Belongs to the lysophospholipase family.

Contains 1 PLA2c domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 2.0 and 7.5.

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 – 2525 Potential
Chain26 – 640615Lysophospholipase
PRO_0000024637

Regions

Domain38 – 589552PLA2c

Amino acid modifications

Glycosylation841N-linked (GlcNAc...) Potential
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2801N-linked (GlcNAc...) Potential
Glycosylation3101N-linked (GlcNAc...) Potential
Glycosylation3171N-linked (GlcNAc...) Potential
Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation3911N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation5161N-linked (GlcNAc...) Potential
Glycosylation5441N-linked (GlcNAc...) Potential
Glycosylation5681N-linked (GlcNAc...) Potential
Glycosylation5851N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis1121R → A: Loss of activity. Ref.1
Mutagenesis4061D → A: Loss of activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O59863 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 90A696CB5D7FF9E3

FASTA64069,983
        10         20         30         40         50         60 
MWFLNSVNLL FLVCSVALHL DAVNAWSPTN GYAPGVVDCD ENINLVRKAD AVSDDEADWL 

        70         80         90        100        110        120 
KVRHESTVPA LKDFLQRGFK GFTNDTSIID KLLATQDTAP KVAIACSGGG YRAMLSGAGM 

       130        140        150        160        170        180 
ISAMDNRTDG ANDHGLGGLL QSSTYLAGLS GGNWLVGTLA YNNWTSVQAI INNMTDDNSI 

       190        200        210        220        230        240 
WDISNSIVNP GGINIFSSIS RWDDISDAVE EKKKAGFNTS ITDVWGRALS YNFFPSLDEG 

       250        260        270        280        290        300 
GVGYTWNTLR DVDVFKNGEM PFPISVAVGR YPGTQVVNLN ATVFEFNPFE MGSWDYTLHT 

       310        320        330        340        350        360 
FTDVRYAGTN VTNGTPNVTG KCVAGFDNTG FVMGTSSSLF NQFLLQLNTT DLPSFLYNLL 

       370        380        390        400        410        420 
HGFLTDASDD YDDISIWAPN PFYEITNIPS NYSQSISEDD TLYLVDGGED GQNIPLTPLL 

       430        440        450        460        470        480 
QTEREIDVIF ALDNSADTDQ SWPDGFSLTQ TYARQFGLQG KGIAFPYVPD VNTFTNLGLN 

       490        500        510        520        530        540 
TRPTFFGCDA RNLTDLESIP PLVVYMPNTR ESFNSNTSTF KMSYSTSERF KMIQNGFEAV 

       550        560        570        580        590        600 
TMKNLTKDEN FMGCISCAIL RRKQESLNYT LPSECDACFE KYCWNGTVDA TTPISSTTSS 

       610        620        630        640 
SASSTSTSDS GNKENSARIL APRSTLSLLI GGLASVFISF 

« Hide

References

« Hide 'large scale' references
[1]"Purification and characterization of phospholipase B from Kluyveromyces lactis, and cloning of phospholipase B gene."
Oishi H., Morimoto T., Watanabe Y., Tamai Y.
Biosci. Biotechnol. Biochem. 63:83-90(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, MUTAGENESIS OF ARG-112 AND ASP-406.
Strain: ATCC 56498 / CBS 683 / DSM 4394 / IFO 1090 / NRRL Y-8279.
[2]"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB014495 mRNA. Translation: BAA28619.1.
CR382123 Genomic DNA. Translation: CAH01313.1.
RefSeqXP_452462.1. XM_452462.1.

3D structure databases

ProteinModelPortalO59863.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.O59863.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2892361.
KEGGkla:KLLA0C05940g.

Phylogenomic databases

eggNOGNOG271081.
HOGENOMHOG000189547.
KOK13333.
OMAEDSNSTW.
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 namePLB_KLULA
AccessionPrimary (citable) accession number: O59863
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: August 1, 1998
Last modified: November 13, 2013
This is version 79 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