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Protein

Lysophospholipase 3

Gene

PLB3

Organism
Candida albicans (Yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the release of fatty acids from lysophospholipids. Phospholipase B may well contribute to pathogenicity by abetting the fungus in damaging and traversing host cell membranes, processes which likely increase the rapidity of disseminated infection (By similarity).By similarity

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 3 (EC:3.1.1.5)
Alternative name(s):
Phospholipase B 3
Gene namesi
Name:PLB3
Synonyms:PLB1
ORF Names:Ca41C10.12
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

Secreted Curated

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 peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 754735Lysophospholipase 3PRO_0000024632Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi510 – 5101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi560 – 5601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi577 – 5771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi597 – 5971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi625 – 6251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ9UVX1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 670557PLA2cPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG271081.

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.

Q9UVX1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVNLKLIIG SILISQAQAI WPFDSSGSSS SSDSSPSETG SSGGTFPFDL
60 70 80 90 100
FGSGSSLTQS SSAQASSTKS TSDSASSTDS SLFSSSNSGS SWYQTFLDGD
110 120 130 140 150
SGDQKTDYAP FNLTCPSKKT FIRTASELSQ QEKDYIHKRQ ETTNKNLIDF
160 170 180 190 200
LSKRANLSDF DAKSFINDNA PNHNITIGLS FSGGGYRAML AGAGQILGLD
210 220 230 240 250
GRYEDANKHG LGGLLDSSTY VVGLSGGNWL VGSLALNDWL SVGDIVNGKS
260 270 280 290 300
TIWQLQDSIL NPSGMRIDKT IAYYYGLAQA VQAKEDAGFQ TSVTDTWGRA
310 320 330 340 350
LSYQFFEEDD SGTGGANITW SSIRNLSSFQ DHSMPYPIVV ANGRTPGTYI
360 370 380 390 400
INENSTIFEI SPYELGSWDP SLKSFSNIQY LGSSVNNGNP NNTDICVNNF
410 420 430 440 450
DNAGFIMGTS SSLFNQILLQ LDNYSINSII KMILEKVLTD VSDEEYDIAV
460 470 480 490 500
YEPNPFFGAD SAGIKSITTN DTLYLCDGGE DLQNVPFYPL IQNKRGVDVI
510 520 530 540 550
FAFDNSADTN SSWPNGTSIQ ETYKRQFSKQ GKGTPFPFAP DYKTFLDKNM
560 570 580 590 600
GDKPVFFGCN SSDLEDLVAW HENDKINVTD VPLVVYTSNT RMSYNSNFST
610 620 630 640 650
FKLSYSDQEK FGAIRNGFET VTRNNLTDDE NWSTCVGCAI IRRQQERLGE
660 670 680 690 700
EQSDECKKCF QEYCWTGGFK DAASVSSVSG ISGLAAKTHT SGGTSSTTQQ
710 720 730 740 750
TSTTTGSSAN GGSSSTGSSS SSKKKNGGDL VNGGVPSSIF LVFNSLLGLI

IAYL
Length:754
Mass (Da):81,412
Last modified:October 10, 2003 - v2
Checksum:i8291D959B005B554
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti377 – 3771N → D in AAF08980 (Ref. 1) Curated
Sequence conflicti494 – 4941K → E in AAF08980 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038128 Genomic DNA. Translation: AAF08980.1.
AL033501 Genomic DNA. Translation: CAA21996.1.
PIRiT18238.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038128 Genomic DNA. Translation: AAF08980.1.
AL033501 Genomic DNA. Translation: CAA21996.1.
PIRiT18238.

3D structure databases

ProteinModelPortaliQ9UVX1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG271081.

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. "Putative phospholipase B precursor of Candida albicans."
    Theiss S., Koehler G.A.
    Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SS.
  2. "Candida albicans strain 1161 genome pilot sequencing project."
    Taylor K., Harris D., Barrell B.G., Rajandream M.A.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1161.

Entry informationi

Entry nameiPLB3_CANAX
AccessioniPrimary (citable) accession number: Q9UVX1
Secondary accession number(s): O94046
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 10, 2003
Last modified: January 7, 2015
This is version 52 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.