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Reviewed, UniProtKB/Swiss-Prot P79066 (LIP1_GEOFE)

Last modified July 28, 2009. Version 61. 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 1
    EC=3.1.1.3
Alternative name(s):
    Lipase I
    TFL I
Gene names
Name: LIP1
OrganismGeotrichum fermentans (Trichosporon fermentans)
Taxonomic identifier44066 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › mitosporic Dipodascaceae › Geotrichum

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Protein attributes

Sequence length563 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.

Subunit structure

Homotrimer. Ref.1

Subcellular location

Secreted.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

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Ontologies

Keywords
   Biological processLipid degradation
   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 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 – 1919 Potential
Chain20 – 563544Lipase 1
PRO_0000008626

Sites

Active site2361Acyl-ester intermediate Ref.2
Active site3731Charge relay system Ref.2
Active site4821Charge relay system Ref.2

Amino acid modifications

Modified residue201Pyrrolidone carboxylic acid
Glycosylation3021N-linked (GlcNAc...) Ref.2
Glycosylation3831N-linked (GlcNAc...) Ref.2
Disulfide bond80 ↔ 124 Ref.2
Disulfide bond295 ↔ 307 Ref.2

Secondary structure

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

Details...

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Sequences

Sequence LengthMass (Da)Tools
P79066-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 210A12C206F33881

FASTA56361,548
        10         20         30         40         50         60 
MVSKSLFLAA AVNLAGVLAQ APTAVLNGNE 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

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References

[1]"Cloning and sequencing of the cDNA encoding lipase I from Trichosporon fermentans WU-C12."
Arai T., Yusa S., Kirimura K., Usami S.
FEMS Microbiol. Lett. 152:183-188(1997) [PubMed: 9228786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBUNIT.
Strain: WU-C12.
[2]"1.8 A refined structure of the lipase from Geotrichum candidum."
Schrag J.D., Cygler M.
J. Mol. Biol. 230:575-591(1993) [PubMed: 8464065] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-563, DISULFIDE BONDS, ACTIVE SITE, PYROGLUTAMATE FORMATION AT GLN-20, GLYCOSYLATION AT ASN-302 AND ASN-383.

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Cross-references

Sequence databases

AB000260 mRNA. Translation: BAA19072.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1THGX-ray1.80A21-563[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.1.3. 291569.

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 nameLIP1_GEOFE
AccessionPrimary (citable) accession number: P79066
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 1997
Last modified: July 28, 2009
This is version 61 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