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Protein

Lysophospholipase

Gene
N/A
Organism
Penicillium chrysogenum (Penicillium notatum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the release of fatty acids from lysophospholipids.

Catalytic activityi

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

GO - Molecular functioni

  1. lysophospholipase activity Source: UniProtKB-EC

GO - Biological processi

  1. phospholipid catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipase (EC:3.1.1.5)
Alternative name(s):
Phospholipase B
OrganismiPenicillium chrysogenum (Penicillium notatum)
Taxonomic identifieri5076 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 9›91 Publication
Chaini10 – 612603LysophospholipasePRO_0000024639Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ ?Sequence Analysis
Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi446 – 4461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi477 – 4771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi526 – 5261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi532 – 5321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi567 – 5671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi571 – 5711N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP39457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 571548PLA2cPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the lysophospholipase family.Curated
Contains 1 PLA2c domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTiSM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.
PROSITEiPS51210. PLA2C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39457-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DITFAGVQRA LPNAPDGYVP TSVSCPASRP TVRSAAKLST NETSWLEVRR
60 70 80 90 100
GKTLSALKDF FGHVKVGDYD VGAYLDKHSG NSSSLPNIGI AVSGGGWRAL
110 120 130 140 150
MNGAGAVKAF DSRTDNATAT GHLGGLLQSA TYISGLSGGS WLLGSIYINN
160 170 180 190 200
FTTVDKLQTH EAGSVWQFGN SIIEGPDAGG IQLLDSAGYY KDLADAVDGK
210 220 230 240 250
KKAGFDTTLT DIWGRALSYQ MFNASNGGLS YTWSSIADTP EFQDGDYPMP
260 270 280 290 300
FVVADGRNPG ELVIGSNSTV YEFNPWEFGT FDPTIFGFVP LEYLGSKFEG
310 320 330 340 350
GSLPSNESCI RGFDSAGFVI GTSSSLFNQF LLQINTTSLP SFIKDVFNGI
360 370 380 390 400
LFDLDKSQND IASYDPNPFY KYNEHSSPYA AQKLLDVVDG GEDGQNVPLH
410 420 430 440 450
PLIQPERHVD VIFAVDSSAD TDYFWPNGTS LVATYERSLN SSGIANGTAF
460 470 480 490 500
PAVPDQNTFI NLGLSTRPSF FGCDSSNQTG PSPLVVYIPN APYSYHSNIS
510 520 530 540 550
TFQLSTDDAE RDNIILNGYE VATMANSTLD DNWTACVACA ILSRSFERTG
560 570 580 590 600
TTLPDICSQC FDRYCWNGTV NSTRPESYDP AFYLADNSMA SVSLPTMLST
610
VVAAGLAMLI LV
Length:612
Mass (Da):65,751
Last modified:February 1, 1995 - v1
Checksum:i7C32F819C3C1ABE5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60348 mRNA. Translation: CAA42906.1.
PIRiS29318.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60348 mRNA. Translation: CAA42906.1.
PIRiS29318.

3D structure databases

ProteinModelPortaliP39457.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTiSM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.
PROSITEiPS51210. PLA2C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPLB1_PENCH
AccessioniPrimary (citable) accession number: P39457
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.