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Reviewed, UniProtKB/Swiss-Prot P32949 (LIP5_CANRU)

Last modified June 16, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lipase 5
    EC=3.1.1.3
Gene names
Name: LIP5
OrganismCandida rugosa (Yeast) (Candida cylindracea)
Taxonomic identifier5481 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length549 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processLipid degradation
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 1515
Chain16 – 549534Lipase 5
PRO_0000008623

Sites

Active site2241Acyl-ester intermediate By similarity
Active site3561Charge relay system By similarity
Active site4641Charge relay system By similarity

Amino acid modifications

Glycosylation3291N-linked (GlcNAc...) Potential
Glycosylation3661N-linked (GlcNAc...) Potential
Disulfide bond75 ↔ 112 By similarity
Disulfide bond283 ↔ 292 By similarity

Sequences

Sequence LengthMass (Da)Tools
P32949-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 0F3D04C9716F6F22

FASTA54958,420
        10         20         30         40         50         60 
MKLALALSLI ASVAAAPTAT LANGDTITGL NAIINEAFLG IPFAEPPVGN LRFKDPVPYR 

        70         80         90        100        110        120 
GSLNGQSFTA YGPSCMQQNP EGTYEENLPK VALDLVMQSK VFQAVLPNSE DCLTINVVRP 

       130        140        150        160        170        180 
PGTKAGANLP VMLWIFGGGF EIGSPTIFPP AQMVSKSVLM GKPIIHVAVN YRLASFGFLA 

       190        200        210        220        230        240 
GPDIKAEGSS NAGLKDQRLG MQWVADNIAG FGGDPSKVTI FGESAGSMSV LCHLLWNGGD 

       250        260        270        280        290        300 
NTYKGKPLFR AGIMQSGAMV PSDPVDGTYG TQIYDTLVAS TGCSSASNKL ACLRGLSTQA 

       310        320        330        340        350        360 
LLDATNDTPG FLSYTSLRLS YLPRPDGANI TDDMYKLVRD GKYASVPVII GDQNDEGFLF 

       370        380        390        400        410        420 
GLSSLNTTTE ADAEAYLRKS FIHATDADIT ALKAAYPSDV TQGSPFDTGI LNALTPQLKR 

       430        440        450        460        470        480 
INAVLGDLTF TLSRRYFLNH YTGGPKYSFL SKQLSGLPIL GTFHANDIVW QHFLLGSGSV 

       490        500        510        520        530        540 
IYNNAFIAFA TDLDPNTAGL SVQWPKSTSS SQAGDNLMQI SALGLYTGKD NFRTAGYNAL 


FADPSHFFV 

« Hide

References

[1]"Cloning and analysis of Candida cylindracea lipase sequences."
Lotti M., Grandori R., Fusetti F., Longhi S., Brocca S., Tramontano A., Alberghina L.
Gene 124:45-55(1993) [PubMed: 8440480] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506.
[2]"Candida rugosa lipases: molecular biology and versatility in biotechnology."
Benjamin S., Pandey A.
Yeast 14:1069-1087(1998) [PubMed: 9778794] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

X66008 Genomic DNA. Translation: CAA46807.1.
PIRJN0553.

3D structure databases

HSSPHSSP built from PDB template 1LLF based on UniProtKB P32947.
SMRP32949. Positions 16-549.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.1.3. 3604.

Family and domain databases

InterProIPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PANTHERPTHR11559. CarbesteraseB. 1 hit.
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLIP5_CANRU
AccessionPrimary (citable) accession number: P32949
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents