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Reviewed, UniProtKB/Swiss-Prot P32946 (LIP2_CANRU)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    Lipase 2
    EC=3.1.1.3
Gene names
Name: LIP2
OrganismCandida rugosa (Yeast) (Candida cylindracea)
Taxonomic identifier5481 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

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Ontologies

Keywords
   Biological processLipid degradation
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1414
Chain15 – 548534Lipase 2
PRO_0000008620

Sites

Active site2231Acyl-ester intermediate
Active site3551Charge relay system
Active site4631Charge relay system

Amino acid modifications

Glycosylation3651N-linked (GlcNAc...) Ref.3
Disulfide bond74 ↔ 111 Ref.3
Disulfide bond282 ↔ 291 Ref.3

Secondary structure

1 ................................................................................................. 548
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P32946-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: E0DBCFF2501E7614

FASTA54858,865
        10         20         30         40         50         60 
MKLCLLALGA AVAAAPTATL ANGDTITGLN AIVNEKFLGI PFAEPPVGTL RFKPPVPYSA 

        70         80         90        100        110        120 
SLNGQQFTSY GPSCMQMNPM GSFEDTLPKN ARHLVLQSKI FQVVLPNDED CLTINVIRPP 

       130        140        150        160        170        180 
GTRASAGLPV MLWIFGGGFE LGGSSLFPGD QMVAKSVLMG KPVIHVSMNY RVASWGFLAG 

       190        200        210        220        230        240 
PDIQNEGSGN AGLHDQRLAM QWVADNIAGF GGDPSKVTIY GESAGSMSTF VHLVWNDGDN 

       250        260        270        280        290        300 
TYNGKPLFRA AIMQSGCMVP SDPVDGTYGT EIYNQVVASA GCGSASDKLA CLRGLSQDTL 

       310        320        330        340        350        360 
YQATSDTPGV LAYPSLRLSY LPRPDGTFIT DDMYALVRDG KYAHVPVIIG DQNDEGTLFG 

       370        380        390        400        410        420 
LSSLNVTTDA QARAYFKQSF IHASDAEIDT LMAAYTSDIT QGSPFDTGIF NAITPQFKRI 

       430        440        450        460        470        480 
SALLGDLAFT LARRYFLNYY QGGTKYSFLS KQLSGLPVLG TFHGNDIIWQ DYLVGSGSVI 

       490        500        510        520        530        540 
YNNAFIAFAN DLDPNKAGLW TNWPTYTSSS QSGNNLMQIN GLGLYTGKDN FRPDAYSALF 


SNPPSFFV

« Hide

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References

[1]"Cloning and nucleotide sequences of two lipase genes from Candida cylindracea."
Longhi S., Fusetti F., Grandori R., Lotti M., Vanoni M., Alberghina L.
Biochim. Biophys. Acta 1131:227-232(1992) [PubMed: 1610906] [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.
[3]"Structural insights into the lipase/esterase behavior in the Candida rugosa lipases family: crystal structure of the lipase 2 isoenzyme at 1.97A resolution."
Mancheno J.M., Pernas M.A., Martinez M.J., Ochoa B., Rua M.L., Hermoso J.A.
J. Mol. Biol. 332:1059-1069(2003) [PubMed: 14499609] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 15-548, DISULFIDE BONDS, GLYCOSYLATION AT ASN-365.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X64704 Genomic DNA. Translation: CAA45958.1.
PIRS32615.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GZ7X-ray1.97A/B/C/D15-548[»]
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...

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Entry information

Entry nameLIP2_CANRU
AccessionPrimary (citable) accession number: P32946
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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