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O59952 (LIP_THELA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipase

EC=3.1.1.3
Alternative name(s):
Triacylglycerol lipase
Gene names
Name:LIP
OrganismThermomyces lanuginosus (Humicola lanuginosa)
Taxonomic identifier5541 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeThermomyces

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Biotechnological use

Used as a detergent lipase. Sold under the name Lipolase by Novozymes. Engineered variants are sold under the names Lipolase Ultra and LipoPrime.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Biophysicochemical properties

pH dependence:

Active at alkaline pHs (up to pH 12 approximately).

Temperature dependence:

Active over a broad temperature range.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   DomainSignal
   Molecular functionHydrolase
   PTMCleavage on pair of basic residues
Zymogen
   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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 225
PRO_0000017737
Chain23 – 291269Lipase
PRO_0000017738

Sites

Active site1681Nucleophile
Active site2231Charge relay system By similarity
Active site2801Charge relay system By similarity

Experimental info

Mutagenesis1091E → A: 35-70% of wild-type activity. Ref.4
Mutagenesis1111W → E, F, G or L: Altered chain length specificity. Ref.2 Ref.4
Mutagenesis1681S → A: Decrease in liposome binding. Ref.5

Secondary structure

........................................................ 291
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O59952 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 170ACEDF791DB07B

FASTA29131,807
        10         20         30         40         50         60 
MRSSLVLFFV SAWTALASPI RREVSQDLFN QFNLFAQYSA AAYCGKNNDA PAGTNITCTG 

        70         80         90        100        110        120 
NACPEVEKAD ATFLYSFEDS GVGDVTGFLA LDNTNKLIVL SFRGSRSIEN WIGNLNFDLK 

       130        140        150        160        170        180 
EINDICSGCR GHDGFTSSWR SVADTLRQKV EDAVREHPDY RVVFTGHSLG GALATVAGAD 

       190        200        210        220        230        240 
LRGNGYDIDV FSYGAPRVGN RAFAEFLTVQ TGGTLYRITH TNDIVPRLPP REFGYSHSSP 

       250        260        270        280        290 
EYWIKSGTLV PVTRNDIVKI EGIDATGGNN QPNIPDIPAH LWYFGLIGTC L 

« Hide

References

[1]"Wild type Humicola lanuginosa cDNA encoding a lipolytic enzyme."
Boel E., Muller S., Sandal T., Kamp-Hansen P., Dalboge H.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Trp89 in the lid of Humicola lanuginosa lipase is important for efficient hydrolysis of tributyrin."
Holmquist M., Martinelle M., Clausen I.G., Patkar S.A., Svendsen A., Hult K.
Lipids 29:599-603(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TRP-111.
[3]"The importance of non-charged amino acids in antibody binding to Humicola lanuginosa lipase."
Naver H., Lovborg U.
Scand. J. Immunol. 41:443-448(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[4]"The role of Glu87 and Trp89 in the lid of Humicola lanuginosa lipase."
Martinelle M., Holmquist M., Clausen I.G., Patkar S.A., Svendsen A., Hult K.
Protein Eng. 9:519-524(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-109 AND TRP-111.
[5]"Active serine involved in the stabilization of the active site loop in the Humicola lanuginosa lipase."
Peters G.H., Svendsen A., Langberg H., Vind J., Patkar S.A., Toxvaerd S., Kinnunen P.K.J.
Biochemistry 37:12375-12383(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-168.
[6]"Conformational lability of lipases observed in the absence of an oil-water interface: crystallographic studies of enzymes from the fungi Humicola lanuginosa and Rhizopus delemar."
Derewenda U., Swenson L., Wei Y., Green R., Kobos P.M., Joerger R., Haas M.J., Derewenda Z.S.
J. Lipid Res. 35:524-534(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS).
[7]"Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase."
Brzozowski A.M., Savage H., Verma C.S., Turkenburg J.P., Lawson D.M., Svendsen A., Patkar S.A.
Biochemistry 39:15071-15082(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 23-291.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF054513 mRNA. Translation: AAC08588.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DT3X-ray2.60A/B23-291[»]
1DT5X-ray2.40A/B/C/D/E/F/G/H23-291[»]
1DTEX-ray2.35A/B23-291[»]
1DU4X-ray2.50A/B/C/D23-291[»]
1EINX-ray3.00A/B/C23-291[»]
1GT6X-ray2.20A/B23-291[»]
1TIBX-ray1.84A23-291[»]
4DYHX-ray2.00A/B23-291[»]
4EA6X-ray2.30A/B23-291[»]
4FLFX-ray2.15A/B23-291[»]
4GBGX-ray2.90A/B23-291[»]
4GHWX-ray2.60A/B23-291[»]
4GI1X-ray2.43A/B23-291[»]
4GLBX-ray2.69A/B23-291[»]
4GWLX-ray2.55A/B23-291[»]
4KJXX-ray2.10A/B23-291[»]
4N8SX-ray2.30A/B23-291[»]
ProteinModelPortalO59952.
SMRO59952. Positions 23-291.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2021756.

Protein family/group databases

Allergome904. The l Lipase.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002921. Lipase_3.
IPR005592. Mono/diacylglycerol_lipase_N.
[Graphical view]
PfamPF03893. Lipase3_N. 1 hit.
PF01764. Lipase_3. 1 hit.
[Graphical view]
PROSITEPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO59952.

Entry information

Entry nameLIP_THELA
AccessionPrimary (citable) accession number: O59952
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: August 1, 1998
Last modified: January 22, 2014
This is version 80 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references