O59952 (LIP_THELA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipase
EC=3.1.1.3

Alternative name(s):
Triacylglycerol lipase

Gene names

Name:

LIP

Organism

Thermomyces lanuginosus (Humicola lanuginosa)

Taxonomic identifier

5541 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › mitosporic Ascomycota › Thermomyces

Protein attributes

Sequence length	291 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Lipid degradation Lipid metabolism
Domain	Signal
Molecular function	Hydrolase
PTM	Cleavage on pair of basic residues Zymogen
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	carboxylesterase activity Inferred from electronic annotation. Source: InterPro retinyl-palmitate esterase activity Inferred from electronic annotation. Source: EC triglyceride lipase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Potential

Propeptide

18 – 22

5

PRO_0000017737

Chain

23 – 291

269

Lipase

PRO_0000017738

Sites

Active site

168

1

Nucleophile

Active site

223

1

Charge relay system By similarity

Active site

280

1

Charge relay system By similarity

Experimental info

Mutagenesis

109

1

E → A: 35-70% of wild-type activity. Ref.4

Mutagenesis

111

1

W → E, F, G or L: Altered chain length specificity. Ref.2 Ref.4

Mutagenesis

168

1

S → A: Decrease in liposome binding. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

291

Helix Strand Turn

Details...

Helix

26 – 41

16

Helix

45 – 47

3

Beta strand

52 – 55

4

Helix

59 – 61

3

Helix

64 – 68

5

Beta strand

72 – 80

9

Turn

81 – 84

4

Beta strand

85 – 92

8

Turn

93 – 96

4

Beta strand

97 – 102

6

Helix

109 – 112

4

Beta strand

119 – 121

3

Turn

123 – 125

3

Beta strand

130 – 132

3

Helix

133 – 156

24

Beta strand

160 – 167

8

Helix

169 – 181

13

Beta strand

184 – 186

3

Beta strand

188 – 194

7

Helix

201 – 209

9

Beta strand

211 – 213

3

Beta strand

215 – 220

6

Helix

225 – 227

3

Helix

231 – 233

3

Beta strand

241 – 244

4

Helix

254 – 256

3

Beta strand

257 – 260

4

Beta strand

266 – 269

4

Beta strand

271 – 273

3

Helix

278 – 281

4

Beta strand

282 – 286

5

Sequences

	Sequence		Length	Mass (Da)
	O59952 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 170ACEDF791DB07B	FASTA	291	31,807
	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

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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DT3	X-ray	2.60	A/B	23-291	[»]
1DT5	X-ray	2.40	A/B/C/D/E/F/G/H	23-291	[»]
1DTE	X-ray	2.35	A/B	23-291	[»]
1DU4	X-ray	2.50	A/B/C/D	23-291	[»]
1EIN	X-ray	3.00	A/B/C	23-291	[»]
1GT6	X-ray	2.20	A/B	23-291	[»]
1TIB	X-ray	1.84	A	23-291	[»]
4DYH	X-ray	2.00	A/B	23-291	[»]
4EA6	X-ray	2.30	A/B	23-291	[»]
4FLF	X-ray	2.15	A/B	23-291	[»]
4GBG	X-ray	2.90	A/B	23-291	[»]
4GHW	X-ray	2.60	A/B	23-291	[»]
4GI1	X-ray	2.43	A/B	23-291	[»]
4GLB	X-ray	2.69	A/B	23-291	[»]
4GWL	X-ray	2.55	A/B	23-291	[»]

ProteinModelPortal

O59952.

SMR

O59952. Positions 23-291.

ModBase

Search...

Protein family/group databases

Allergome

904. The l Lipase.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002921. Lipase_3.
IPR005592. Mono/diacylglycerol_lipase_N.
[Graphical view]

Pfam

PF03893. Lipase3_N. 1 hit.
PF01764. Lipase_3. 1 hit.
[Graphical view]

PROSITE

PS00120. LIPASE_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O59952.

Entry information

Entry name

LIP_THELA

Accession

Primary (citable) accession number: O59952

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 4, 2001
Last sequence update:	August 1, 1998
Last modified:	April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program