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P39457 (PLB1_PENCH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 64. 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):
Phospholipase B
OrganismPenicillium chrysogenum (Penicillium notatum)
Taxonomic identifier5076 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex

Protein attributes

Sequence length612 AA.
Sequence statusFragment.
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

Secreted.

Post-translational modification

N-glycosylated.

Sequence similarities

Belongs to the lysophospholipase family.

Contains 1 PLA2c domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
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 peptide‹1 – 9›9 Ref.1
Chain10 – 612603Lysophospholipase
PRO_0000024639

Regions

Domain24 – 571548PLA2c

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Potential
Glycosylation3061N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation4271N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential
Glycosylation4461N-linked (GlcNAc...) Potential
Glycosylation4771N-linked (GlcNAc...) Potential
Glycosylation4981N-linked (GlcNAc...) Potential
Glycosylation5261N-linked (GlcNAc...) Potential
Glycosylation5321N-linked (GlcNAc...) Potential
Glycosylation5671N-linked (GlcNAc...) Potential
Glycosylation5711N-linked (GlcNAc...) Potential
Disulfide bond25 ↔ ? Potential

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P39457 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 7C32F819C3C1ABE5

FASTA61265,751
        10         20         30         40         50         60 
DITFAGVQRA LPNAPDGYVP TSVSCPASRP TVRSAAKLST NETSWLEVRR GKTLSALKDF 

        70         80         90        100        110        120 
FGHVKVGDYD VGAYLDKHSG NSSSLPNIGI AVSGGGWRAL MNGAGAVKAF DSRTDNATAT 

       130        140        150        160        170        180 
GHLGGLLQSA TYISGLSGGS WLLGSIYINN FTTVDKLQTH EAGSVWQFGN SIIEGPDAGG 

       190        200        210        220        230        240 
IQLLDSAGYY KDLADAVDGK KKAGFDTTLT DIWGRALSYQ MFNASNGGLS YTWSSIADTP 

       250        260        270        280        290        300 
EFQDGDYPMP FVVADGRNPG ELVIGSNSTV YEFNPWEFGT FDPTIFGFVP LEYLGSKFEG 

       310        320        330        340        350        360 
GSLPSNESCI RGFDSAGFVI GTSSSLFNQF LLQINTTSLP SFIKDVFNGI LFDLDKSQND 

       370        380        390        400        410        420 
IASYDPNPFY KYNEHSSPYA AQKLLDVVDG GEDGQNVPLH PLIQPERHVD VIFAVDSSAD 

       430        440        450        460        470        480 
TDYFWPNGTS LVATYERSLN SSGIANGTAF PAVPDQNTFI NLGLSTRPSF FGCDSSNQTG 

       490        500        510        520        530        540 
PSPLVVYIPN APYSYHSNIS TFQLSTDDAE RDNIILNGYE VATMANSTLD DNWTACVACA 

       550        560        570        580        590        600 
ILSRSFERTG TTLPDICSQC FDRYCWNGTV NSTRPESYDP AFYLADNSMA SVSLPTMLST 

       610 
VVAAGLAMLI LV 

« Hide

References

[1]"Primary structure of protein moiety of Penicillium notatum phospholipase B deduced from the cDNA."
Masuda N., Kitamura N., Saito K.
Eur. J. Biochem. 202:783-787(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-20 AND 185-199.
Strain: ATCC 34514 / NBRC 4640.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60348 mRNA. Translation: CAA42906.1.
PIRS29318.

3D structure databases

ProteinModelPortalP39457.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_PENCH
AccessionPrimary (citable) accession number: P39457
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 13, 2013
This is version 64 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