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Reviewed, UniProtKB/Swiss-Prot P20261 (LIP1_CANRU)

Last modified November 24, 2009. Version 67. 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
Gene names
Name: LIP1
OrganismCandida rugosa (Yeast) (Candida cylindracea)
Taxonomic identifier5481 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length549 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.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

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Ontologies

Keywords
   Biological processLipid degradation
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 1515
Chain16 – 549534Lipase 1
PRO_0000008619

Sites

Active site2241Acyl-ester intermediate
Active site3561Charge relay system
Active site4641Charge relay system

Amino acid modifications

Glycosylation3291N-linked (GlcNAc...)
Glycosylation3661N-linked (GlcNAc...)
Disulfide bond75 ↔ 112
Disulfide bond283 ↔ 292

Natural variations

Natural variant3981G → Q

Secondary structure

1 ............................................................................................ 549
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P20261-1 [UniParc].

Last modified October 1, 1993. Version 3.
Checksum: 27A40BD318757CE0

FASTA54958,550
        10         20         30         40         50         60 
MELALALSLI ASVAAAPTAT LANGDTITGL NAIINEAFLG IPFAEPPVGN LRFKDPVPYS 

        70         80         90        100        110        120 
GSLDGQKFTS YGPSCMQQNP EGTYEENLPK AALDLVMQSK VFEAVSPSSE DCLTINVVRP 

       130        140        150        160        170        180 
PGTKAGANLP VMLWIFGGGF EVGGTSTFPP AQMITKSIAM GKPIIHVSVN YRVSSWGFLA 

       190        200        210        220        230        240 
GDEIKAEGSA NAGLKDQRLG MQWVADNIAA FGGDPTKVTI FGESAGSMSV MCHILWNDGD 

       250        260        270        280        290        300 
NTYKGKPLFR AGIMQSGAMV PSDAVDGIYG NEIFDLLASN AGCGSASDKL ACLRGVSSDT 

       310        320        330        340        350        360 
LEDATNNTPG FLAYSSLRLS YLPRPDGVNI TDDMYALVRE GKYANIPVII GDQNDEGTFF 

       370        380        390        400        410        420 
GTSSLNVTTD AQAREYFKQS FVHASDAEID TLMTAYPGDI TQGSPFDTGI LNALTPQFKR 

       430        440        450        460        470        480 
ISAVLGDLGF TLARRYFLNH YTGGTKYSFL SKQLSGLPVL GTFHSNDIVF QDYLLGSGSL 

       490        500        510        520        530        540 
IYNNAFIAFA TDLDPNTAGL LVKWPEYTSS SQSGNNLMMI NALGLYTGKD NFRTAGYDAL 


FSNPPSFFV

« Hide

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References

[1]"Cloning and nucleotide sequences of two lipase genes from Candida cylindracea."
Longhi S., Fusetti F., Grandori R., Lotti M., Vanoni M., Alberghina L.
Biochim. Biophys. Acta 1131:227-232(1992) [PubMed: 1610906] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506.
[2]"The codon CUG is read as serine in an asporogenic yeast Candida cylindracea."
Kawaguchi Y., Honda H., Taniguchi-Morimura J., Iwasaki S.
Nature 341:164-166(1989) [PubMed: 2506450] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-549, PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506.
[3]"Insights into interfacial activation from an open structure of Candida rugosa lipase."
Grochulski P., Li Y., Schrag J.D., Bouthillier F., Smith P., Harrison D., Rubin B., Cygler M.
J. Biol. Chem. 268:12843-12847(1993) [PubMed: 8509417] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS).
[4]"Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase."
Grochulski P., Bouthillier F., Kazlauskas R.J., Serreqi A.N., Schrag J.D., Ziomek E., Cygler M.
Biochemistry 33:3494-3500(1994) [PubMed: 8142346] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
[5]"Candida rugosa lipases: molecular biology and versatility in biotechnology."
Benjamin S., Pandey A.
Yeast 14:1069-1087(1998) [PubMed: 9778794] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X64703 Genomic DNA. Translation: CAA45957.1.
X16712 mRNA. Translation: CAA34684.1.
PIRS05684.
S23448.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CRLX-ray2.06A16-549[»]
1LPMX-ray2.18A1-549[»]
1LPNX-ray2.18A1-549[»]
1LPOX-ray2.18A1-549[»]
1LPPX-ray2.18A1-549[»]
1LPSX-ray2.18A1-549[»]
1TRHX-ray2.10A16-549[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.1.3. 3604.

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_CANRU
AccessionPrimary (citable) accession number: P20261
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1993
Last modified: November 24, 2009
This is version 67 of the entry and version 3 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