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P22394 (LIP2_GEOCN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 2
EC=3.1.1.3
Alternative name(s):
GCL II
Lipase II
Gene names
Name:LIP2
OrganismGeotrichum candidum (Oospora lactis) (Dipodascus geotrichum)
Taxonomic identifier27317 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Galactomyces

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes all ester bonds in triglyceride and displays a high affinity for triolein. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15) GCL I shows higher specific activity than GCL II, whereas GCL II shows higher specific activity against saturated substrates having short fatty acid chains (C8, C10, C12 and C14).

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subunit structure

Monomer.

Subcellular location

Secreted.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionretinyl-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.4
Chain20 – 563544Lipase 2
PRO_0000008625

Sites

Active site2361Acyl-ester intermediate
Active site3731Charge relay system
Active site4821Charge relay system

Amino acid modifications

Modified residue201Pyrrolidone carboxylic acid
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation3831N-linked (GlcNAc...) Potential
Disulfide bond80 ↔ 124
Disulfide bond295 ↔ 307

Natural variations

Natural variant461I → V in strain: NRRL Y-552.
Natural variant2471I → V in strain: NRRL Y-553.
Natural variant3551F → Y in strain: NRRL Y-553.
Natural variant3911K → R in strain: NRRL Y-553.
Natural variant4391A → S in strain: NRRL Y-553.
Natural variant4841N → D in strain: NRRL Y-552.

Experimental info

Sequence conflict23 – 253RPS → TAV in AAA03430. Ref.3
Sequence conflict23 – 253RPS → TAV in AAA03436. Ref.3
Sequence conflict361L → V in AAA03430. Ref.3
Sequence conflict361L → V in AAA03437. Ref.3
Sequence conflict138 – 1392DA → ED in AAA03430. Ref.3

Secondary structure

1 ..................................................................................................... 563
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22394 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 12AA134A258C652F

FASTA56361,617
        10         20         30         40         50         60 
MVSKSLFLAA AVNLAGVLAQ APRPSLNGNE VISGVLEGKV DTFKGIPFAD PPLNDLRFKH 

        70         80         90        100        110        120 
PQPFTGSYQG LKANDFSPAC MQLDPGNSLT LLDKALGLAK VIPEEFRGPL YDMAKGTVSM 

       130        140        150        160        170        180 
NEDCLYLNVF RPAGTKPDAK LPVMVWIYGG AFVYGSSAAY PGNSYVKESI NMGQPVVFVS 

       190        200        210        220        230        240 
INYRTGPFGF LGGDAITAEG NTNAGLHDQR KGLEWVSDNI ANFGGDPDKV MIFGESAGAM 

       250        260        270        280        290        300 
SVAHQLIAYG GDNTYNGKKL FHSAILQSGG PLPYHDSSSV GPDISYNRFA QYAGCDTSAS 

       310        320        330        340        350        360 
ANDTLECLRS KSSSVLHDAQ NSYDLKDLFG LLPQFLGFGP RPDGNIIPDA AYELFRSGRY 

       370        380        390        400        410        420 
AKVPYISGNQ EDEGTAFAPV ALNATTTPHV KKWLQYIFYD ASEASIDRVL SLYPQTLSVG 

       430        440        450        460        470        480 
SPFRTGILNA LTPQFKRVAA ILSDMLFQSP RRVMLSATKD VNRWTYLSTH LHNLVPFLGT 

       490        500        510        520        530        540 
FHGNELIFQF NVNIGPANSY LRYFISFANH HDPNVGTNLL QWDQYTDEGK EMLEIHMTDN 

       550        560 
VMRTDDYRIE GISNFETDVN LYG

« Hide

References

[1]"Cloning and sequencing of two chromosomal lipase genes from Geotrichum candidum."
Nagao T., Shimada Y., Sugihara A., Tominaga Y.
J. Biochem. 113:776-780(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 34614.
[2]"cDNA cloning and characterization of Geotrichum candidum lipase II."
Shimada Y., Sugihara A., Iizumi T., Tominaga Y.
J. Biochem. 107:703-707(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-563, PARTIAL PROTEIN SEQUENCE.
[3]"Polymorphism in the lipase genes of Geotrichum candidum strains."
Bertolini M.C., Laramee L., Thomas D.Y., Cygler M., Schrag J.D., Vernet T.
Eur. J. Biochem. 219:119-125(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-563.
Strain: ATCC 34614, ATCC 74169 / NRRL Y-552 / ED00652 and ATCC 90287 / NRRL Y-553.
[4]"Separation and characterization of two molecular forms of Geotrichum candidum lipase."
Sugihara A., Shimada Y., Tominaga Y.
J. Biochem. 107:426-430(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-26 AND 561-563.
[5]"Expression and characterization of Geotrichum candidum lipase I gene. Comparison of specificity profile with lipase II."
Bertolini M.C., Schrag J.D., Cygler M., Ziomek E., Thomas D.Y., Vernet T.
Eur. J. Biochem. 228:863-869(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum."
Schrag J.D., Li Y., Wu S., Cygler M.
Nature 351:761-764(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[7]"1.8 A refined structure of the lipase from Geotrichum candidum."
Schrag J.D., Cygler M.
J. Mol. Biol. 230:575-591(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S65090 Genomic DNA. Translation: AAB28108.1.
S65092 Genomic DNA. Translation: AAB28109.1.
D00697 mRNA. Translation: BAA00603.1.
U02541 Genomic DNA. Translation: AAA03430.1.
U02623 Genomic DNA. Translation: AAA03436.1.
U02625 Genomic DNA. Translation: AAA03437.1.
PIRPN0493.
PX0030.
S41094.
S41095.
S41096.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1THGX-ray1.80A26-563[»]
ProteinModelPortalP22394.
SMRP22394. Positions 20-563.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Other

EvolutionaryTraceP22394.

Entry information

Entry nameLIP2_GEOCN
AccessionPrimary (citable) accession number: P22394
Secondary accession number(s): Q00885 expand/collapse secondary AC list , Q00890, Q00892, Q02213, Q96VH7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 1, 1994
Last modified: April 3, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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