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Protein

Lipase

Gene

LIP

Organism
Thermomyces lanuginosus (Humicola lanuginosa)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

pH dependencei

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

Temperature dependencei

Active over a broad temperature range.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei168 – 1681Nucleophile1 Publication
Active sitei223 – 2231Charge relay system1 PublicationPROSITE-ProRule annotation
Active sitei280 – 2801Charge relay system1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. triglyceride lipase activity Source: UniProtKB-EC

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

SABIO-RKO59952.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase (EC:3.1.1.3)
Alternative name(s):
Triacylglycerol lipase
Gene namesi
Name:LIP
OrganismiThermomyces lanuginosus (Humicola lanuginosa)
Taxonomic identifieri5541 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeThermomyces

Pathology & Biotechi

Biotechnological usei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091E → A: 35-70% of wild-type activity. 1 Publication
Mutagenesisi111 – 1111W → E, F, G or L: Altered chain length specificity. 2 Publications
Mutagenesisi168 – 1681S → A: Decrease in liposome binding. 1 Publication

Protein family/group databases

Allergomei904. The l Lipase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 225PRO_0000017737
Chaini23 – 291269LipasePRO_0000017738Add
BLAST

Keywords - PTMi

Cleavage on pair of basic residues, Zymogen

Structurei

Secondary structure

1
291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 4116Combined sources
Helixi45 – 473Combined sources
Beta strandi52 – 554Combined sources
Helixi59 – 613Combined sources
Helixi64 – 685Combined sources
Beta strandi72 – 809Combined sources
Turni81 – 844Combined sources
Beta strandi85 – 928Combined sources
Turni93 – 964Combined sources
Beta strandi97 – 1026Combined sources
Helixi109 – 1124Combined sources
Beta strandi119 – 1213Combined sources
Turni123 – 1253Combined sources
Beta strandi130 – 1323Combined sources
Helixi133 – 15624Combined sources
Beta strandi160 – 1678Combined sources
Helixi169 – 18113Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi188 – 1947Combined sources
Helixi201 – 2099Combined sources
Beta strandi211 – 2133Combined sources
Beta strandi215 – 2206Combined sources
Helixi225 – 2273Combined sources
Helixi231 – 2333Combined sources
Beta strandi241 – 2444Combined sources
Helixi254 – 2563Combined sources
Beta strandi257 – 2604Combined sources
Beta strandi266 – 2694Combined sources
Beta strandi271 – 2733Combined sources
Helixi278 – 2814Combined sources
Beta strandi282 – 2865Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliO59952.
SMRiO59952. Positions 23-291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59952.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
IPR005592. Mono/diacylglycerol_lipase_N.
[Graphical view]
PfamiPF03893. Lipase3_N. 1 hit.
PF01764. Lipase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O59952-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRSSLVLFFV SAWTALASPI RREVSQDLFN QFNLFAQYSA AAYCGKNNDA
60 70 80 90 100
PAGTNITCTG NACPEVEKAD ATFLYSFEDS GVGDVTGFLA LDNTNKLIVL
110 120 130 140 150
SFRGSRSIEN WIGNLNFDLK EINDICSGCR GHDGFTSSWR SVADTLRQKV
160 170 180 190 200
EDAVREHPDY RVVFTGHSLG GALATVAGAD LRGNGYDIDV FSYGAPRVGN
210 220 230 240 250
RAFAEFLTVQ TGGTLYRITH TNDIVPRLPP REFGYSHSSP EYWIKSGTLV
260 270 280 290
PVTRNDIVKI EGIDATGGNN QPNIPDIPAH LWYFGLIGTC L
Length:291
Mass (Da):31,807
Last modified:August 1, 1998 - v1
Checksum:i170ACEDF791DB07B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054513 mRNA. Translation: AAC08588.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054513 mRNA. Translation: AAC08588.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliO59952.
SMRiO59952. Positions 23-291.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL2021756.

Protein family/group databases

Allergomei904. The l Lipase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKO59952.

Miscellaneous databases

EvolutionaryTraceiO59952.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
IPR005592. Mono/diacylglycerol_lipase_N.
[Graphical view]
PfamiPF03893. Lipase3_N. 1 hit.
PF01764. Lipase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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), ACTIVE SITE.
  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.

Entry informationi

Entry nameiLIP_THELA
AccessioniPrimary (citable) accession number: O59952
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: August 1, 1998
Last modified: November 26, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.