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O94091 (LIP1_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lipase 1

EC=3.1.1.3
Gene names
Name:LIP1
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Hydrolyzes triglycerides.

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subcellular location

Secreted Ref.1.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontriglyceride lipase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 468452Lipase 1
PRO_0000017820

Sites

Active site1961Charge relay system By similarity
Active site3441Charge relay system By similarity

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation3191N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4221N-linked (GlcNAc...) Potential
Glycosylation4511N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O94091 [UniParc].

Last modified November 21, 2003. Version 2.
Checksum: 4FF3C05A948B14DA

FASTA46850,811
        10         20         30         40         50         60 
MRGIAVFLAF ISLIFASPLT VKSPLVDDFY TAPDGYESAK LGEILKLRKT PSKLSSMFFE 

        70         80         90        100        110        120 
IDIKNSWQLL VRSEDSFGNA TAIVTTVIEP YNADPSKVLS YQTFEDSANI ECSPSYGMQY 

       130        140        150        160        170        180 
GAPWSTVATQ IDMALMVPML KQGYYVVSPD YEGPKSTFTV GRQSGKATLD SIRAILKSNK 

       190        200        210        220        230        240 
FTGIKSDAKV AMWGYSGGSL ASGWAAALQP KYAPELKKNL IGAALGGFVT NITATAEATD 

       250        260        270        280        290        300 
GTLFAGLVPN ALSGLANEYP EFKEILYQKV SKAATDNLRQ GTEHCIGGAI LYFAEDQYFT 

       310        320        330        340        350        360 
GDDRAFPGGY GLLKEEVVNK TISENNLMQM DKDYLPDIPI FVYHGALDSI VPISNVHVTY 

       370        380        390        400        410        420 
KNWCDWGINS FEFSEDLLNG HITETIVGAP AAITWLEARF DGEPVVKGCK KTSRITNFSY 

       430        440        450        460 
PNISDSTSSI FEGILNSVTG SELGPGVTSD NITLDGLTGF LGNFIDLK 

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References

[1]"Secreted lipases of Candida albicans: cloning, characterisation and expression analysis of a new gene family with at least ten members."
Hube B., Stehr F., Bossenz M., Mazur A., Kretschmar M., Schaefer W.
Arch. Microbiol. 174:362-374(2000) [PubMed: 11131027] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
Strain: 1161.
[2]"Cloning and characterization of a gene (LIP1) which encodes a lipase from the pathogenic yeast Candida albicans."
Fu Y., Ibrahim A.S., Fonzi W., Zhou X., Ramos C.F., Ghannoum M.A.
Microbiology 143:331-340(1997) [PubMed: 9043110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-468.
Strain: ATCC 36082.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF188894 Genomic DNA. Translation: AAF35171.1.
U34807 Genomic DNA. Translation: AAC99990.1.

3D structure databases

ProteinModelPortalO94091.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OMASAMWELL.

Family and domain databases

InterProIPR005152. Lipase_secreted.
[Graphical view]
PfamPF03583. LIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLIP1_CANAX
AccessionPrimary (citable) accession number: O94091
Secondary accession number(s): Q9P8W6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 21, 2003
Last modified: October 19, 2011
This is version 48 of the entry and version 2 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