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P32947 (LIP3_CANRU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lipase 3
EC=3.1.1.3
Alternative name(s):
Cholesterol esterase
Gene names
Name:LIP3
OrganismCandida rugosa (Yeast) (Candida cylindracea)
Taxonomic identifier5481 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length549 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subunit structure

Monomer and homodimer. Ref.2

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Ref.2
Chain16 – 549534Lipase 3
PRO_0000008621

Sites

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

Amino acid modifications

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P32947 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: C5F95C31422975DA

FASTA54958,755
        10         20         30         40         50         60 
MKLALALSLI ASVAAAPTAK LANGDTITGL NAIINEAFLG IPFAEPPVGN LRFKDPVPYS 

        70         80         90        100        110        120 
GSLNGQKFTS YGPSCMQQNP EGTFEENLGK TALDLVMQSK VFQAVLPQSE DCLTINVVRP 

       130        140        150        160        170        180 
PGTKAGANLP VMLWIFGGGF EIGSPTIFPP AQMVTKSVLM GKPIIHVAVN YRVASWGFLA 

       190        200        210        220        230        240 
GDDIKAEGSG NAGLKDQRLG MQWVADNIAG FGGDPSKVTI FGESAGSMSV LCHLIWNDGD 

       250        260        270        280        290        300 
NTYKGKPLFR AGIMQSGAMV PSDPVDGTYG NEIYDLFVSS AGCGSASDKL ACLRSASSDT 

       310        320        330        340        350        360 
LLDATNNTPG FLAYSSLRLS YLPRPDGKNI TDDMYKLVRD GKYASVPVII GDQNDEGTIF 

       370        380        390        400        410        420 
GLSSLNVTTN AQARAYFKQS FIHASDAEID TLMAAYPQDI TQGSPFDTGI FNAITPQFKR 

       430        440        450        460        470        480 
ISAVLGDLAF IHARRYFLNH FQGGTKYSFL SKQLSGLPIM GTFHANDIVW QDYLLGSGSV 

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


MTNPSSFFV

« Hide

References

[1]"Cloning and analysis of Candida cylindracea lipase sequences."
Lotti M., Grandori R., Fusetti F., Longhi S., Brocca S., Tramontano A., Alberghina L.
Gene 124:45-55(1993) [PubMed: 8440480] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506.
[2]"Monomeric and dimeric forms of cholesterol esterase from Candida cylindracea. Primary structure, identity in peptide patterns, and additional microheterogeneity."
Kaiser R., Erman M., Duax W.L., Ghosh D., Joernvall H.
FEBS Lett. 337:123-127(1994) [PubMed: 8287964] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-549, SUBUNIT STRUCTURE.
[3]"Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase."
Ghosh D., Wawrzak Z., Pletnev V.Z., Li N., Kaiser R., Pangborn W., Joernvall H., Erman M., Duax W.L.
Structure 3:279-288(1995) [PubMed: 7788294] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[4]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X66006 Genomic DNA. Translation: CAA46805.1.
PIRJN0551.
S41735.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CLEX-ray2.00A/B16-549[»]
1LLFX-ray1.40A/B16-549[»]
ProteinModelPortalP32947.
SMRP32947. Positions 16-549.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.1.1.3. 1139.

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...

Entry information

Entry nameLIP3_CANRU
AccessionPrimary (citable) accession number: P32947
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 31, 2011
This is version 71 of the entry and version 1 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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