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Protein

Lysophospholipase 3

Gene

plb3

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 4 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

Enzyme and pathway databases

BRENDAi3.1.1.5. 508.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipase 3 (EC:3.1.1.5)
Alternative name(s):
Phospholipase B 3
Gene namesi
Name:plb3
ORF Names:AFUB_034540
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001699 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Protein family/group databases

Allergomei8988. Asp f LPL3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 606590Lysophospholipase 3PRO_0000372613Add
BLAST
Propeptidei607 – 63024Removed in mature formSequence AnalysisPRO_0000372614Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi56 – 561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi390 – 3901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi456 – 4561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi514 – 5141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi542 – 5421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi566 – 5661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi583 – 5831N-linked (GlcNAc...)Sequence Analysis
Lipidationi606 – 6061GPI-like-anchor amidated asparagineSequence Analysis

Post-translational modificationi

The GPI-like anchor contains a phosphoceramide lipid group.

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Expressioni

Inductioni

Strongly induced by lecithin.1 Publication

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 587549PLA2cPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000189547.
OrthoDBiEOG7N37NC.
PhylomeDBiB0XZV8.

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: Complete.

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

B0XZV8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALLSLLTA VAVATATPLD LSLRALPNAP DGYTPAKVSC PATRPSIRGA
60 70 80 90 100
GSLSPNETSW LEIRRKNTVQ PMTDLLGRLN LGFDAAGYID RVSSNASNLP
110 120 130 140 150
NIAIAVSGGG YRALTNGAGA IKAFDSRTQG STQSGHLGGL LQSATYVSGL
160 170 180 190 200
SGGGWLVGSV YLNNFTTIAD LQSGDHGNVW QFSTSILEGP KAKHLQFLST
210 220 230 240 250
ADYWKDLLKA VDGKSDAGFN TSLTDYWGRA LSYQFINDRT GNGGLSYTWS
260 270 280 290 300
SIALTDPFRR GEMPLPILVA DGRNPGELLI GSNSTVYEFN PWEFGSFDPS
310 320 330 340 350
IFGFAPLEYL GSRFDNGQLP RGEPCVRGFD NAGFVMGTSS SLFNQFILRL
360 370 380 390 400
NKTDLPDLAK DVFSKILTAI GRDGDDIAVY GPNPFYGYRN STAAYSRSRE
410 420 430 440 450
LDVVDGGEDG QNIPLHPLIQ PVRHVDVIFA VDSSADGPYS WPNGSALVAT
460 470 480 490 500
YERSLNSSGI GNGTVFPAVP DVNTFVNLGL NTRPTFFGCD PANLSAPAPL
510 520 530 540 550
VVYLPNAPYS THSNTSTFQL AYSDSERDEI ITNGYNVVTR GNATVDKSWP
560 570 580 590 600
SCVGCAILQR SMYRTNTSMP AVCNSCFKEY CWNGTVDSKT PRTYEPTLLL
610 620 630
GSTSTNAAYT QGVTWLVGIL AVGVAMGMTA
Length:630
Mass (Da):67,417
Last modified:April 8, 2008 - v1
Checksum:i0E83E7D7F149CA08
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701Q → E in AAQ85123 (PubMed:15451105).Curated
Sequence conflicti542 – 5421N → D in AAQ85123 (PubMed:15451105).Curated
Sequence conflicti618 – 6181G → S in AAQ85123 (PubMed:15451105).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY376593 mRNA. Translation: AAQ85123.1.
DS499596 Genomic DNA. Translation: EDP52290.1.

Genome annotation databases

EnsemblFungiiCADAFUBT00003440; CADAFUBP00003378; CADAFUBG00003440.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY376593 mRNA. Translation: AAQ85123.1.
DS499596 Genomic DNA. Translation: EDP52290.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei8988. Asp f LPL3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUBT00003440; CADAFUBP00003378; CADAFUBG00003440.

Phylogenomic databases

HOGENOMiHOG000189547.
OrthoDBiEOG7N37NC.
PhylomeDBiB0XZV8.

Enzyme and pathway databases

BRENDAi3.1.1.5. 508.

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

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiPLB3_ASPFC
AccessioniPrimary (citable) accession number: B0XZV8
Secondary accession number(s): Q4WYY4, Q6U819
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: April 8, 2008
Last modified: April 1, 2015
This is version 32 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

Complete proteome

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.