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Protein

Lipase 1

Gene

LIP1

Organism
Candida rugosa (Yeast) (Candida cylindracea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei224 – 2241Acyl-ester intermediate
Active sitei356 – 3561Charge relay system
Active sitei464 – 4641Charge relay system

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.3. 1139.

Protein family/group databases

ESTHERicanru-1lipa. Fungal_carboxylesterase_lipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase 1 (EC:3.1.1.3)
Gene namesi
Name:LIP1
OrganismiCandida rugosa (Yeast) (Candida cylindracea)
Taxonomic identifieri5481 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Add
BLAST
Chaini16 – 549534Lipase 1PRO_0000008619Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi75 ↔ 112
Disulfide bondi283 ↔ 292
Glycosylationi329 – 3291N-linked (GlcNAc...)
Glycosylationi366 – 3661N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1
549
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 203Combined sources
Beta strandi26 – 283Combined sources
Beta strandi33 – 4210Combined sources
Helixi49 – 513Combined sources
Helixi84 – 863Combined sources
Helixi88 – 9710Combined sources
Helixi100 – 1056Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi114 – 1196Combined sources
Beta strandi129 – 1357Combined sources
Turni139 – 1413Combined sources
Helixi145 – 1473Combined sources
Helixi151 – 1599Combined sources
Beta strandi165 – 1695Combined sources
Helixi174 – 1785Combined sources
Helixi182 – 1876Combined sources
Helixi192 – 20716Combined sources
Helixi208 – 2114Combined sources
Beta strandi213 – 22311Combined sources
Helixi225 – 23511Combined sources
Helixi236 – 2394Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi250 – 2567Combined sources
Helixi268 – 28114Combined sources
Helixi289 – 2957Combined sources
Helixi298 – 3069Combined sources
Turni314 – 3174Combined sources
Beta strandi327 – 3304Combined sources
Helixi334 – 3396Combined sources
Beta strandi348 – 3536Combined sources
Helixi358 – 3614Combined sources
Helixi362 – 3643Combined sources
Helixi370 – 38011Combined sources
Helixi386 – 39510Combined sources
Helixi400 – 4023Combined sources
Beta strandi403 – 4053Combined sources
Turni409 – 4124Combined sources
Beta strandi414 – 4174Combined sources
Helixi418 – 42912Combined sources
Helixi431 – 44010Combined sources
Beta strandi446 – 4516Combined sources
Turni453 – 4564Combined sources
Turni458 – 4603Combined sources
Beta strandi461 – 4633Combined sources
Helixi466 – 4727Combined sources
Helixi479 – 4824Combined sources
Helixi484 – 4929Combined sources
Helixi495 – 4984Combined sources
Beta strandi512 – 5143Combined sources
Beta strandi517 – 5204Combined sources
Beta strandi525 – 5284Combined sources
Helixi534 – 5418Combined sources
Helixi544 – 5474Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
3RARX-ray2.19A16-549[»]
ProteinModelPortaliP20261.
SMRiP20261. Positions 16-549.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20261.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20261-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELALALSLI ASVAAAPTAT LANGDTITGL NAIINEAFLG IPFAEPPVGN
60 70 80 90 100
LRFKDPVPYS GSLDGQKFTS YGPSCMQQNP EGTYEENLPK AALDLVMQSK
110 120 130 140 150
VFEAVSPSSE DCLTINVVRP PGTKAGANLP VMLWIFGGGF EVGGTSTFPP
160 170 180 190 200
AQMITKSIAM GKPIIHVSVN YRVSSWGFLA GDEIKAEGSA NAGLKDQRLG
210 220 230 240 250
MQWVADNIAA FGGDPTKVTI FGESAGSMSV MCHILWNDGD NTYKGKPLFR
260 270 280 290 300
AGIMQSGAMV PSDAVDGIYG NEIFDLLASN AGCGSASDKL ACLRGVSSDT
310 320 330 340 350
LEDATNNTPG FLAYSSLRLS YLPRPDGVNI TDDMYALVRE GKYANIPVII
360 370 380 390 400
GDQNDEGTFF GTSSLNVTTD AQAREYFKQS FVHASDAEID TLMTAYPGDI
410 420 430 440 450
TQGSPFDTGI LNALTPQFKR ISAVLGDLGF TLARRYFLNH YTGGTKYSFL
460 470 480 490 500
SKQLSGLPVL GTFHSNDIVF QDYLLGSGSL IYNNAFIAFA TDLDPNTAGL
510 520 530 540
LVKWPEYTSS SQSGNNLMMI NALGLYTGKD NFRTAGYDAL FSNPPSFFV
Length:549
Mass (Da):58,550
Last modified:October 1, 1993 - v3
Checksum:i27A40BD318757CE0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti398 – 3981G → Q.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64703 Genomic DNA. Translation: CAA45957.1.
X16712 mRNA. Translation: CAA34684.1.
PIRiS05684.
S23448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64703 Genomic DNA. Translation: CAA45957.1.
X16712 mRNA. Translation: CAA34684.1.
PIRiS05684.
S23448.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
3RARX-ray2.19A16-549[»]
ProteinModelPortaliP20261.
SMRiP20261. Positions 16-549.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERicanru-1lipa. Fungal_carboxylesterase_lipase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.1.3. 1139.

Miscellaneous databases

EvolutionaryTraceiP20261.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiLIP1_CANRU
AccessioniPrimary (citable) accession number: P20261
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1993
Last modified: October 14, 2015
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.