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Protein

Lipase

Gene
N/A
Organism
Rhizopus niveus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes ester bonds of triglycerides as well as of their derived partial glycerides with a strong 1,3-positional specificity.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Enzyme regulationi

Lipase activity is maximal at a lipid-water interface (interfacial activation), probably by an induced conformational change that results in an increased accessibility of the active site to the substrate.

pH dependencei

Optimum pH is 6.0-6.5.2 Publications

Temperature dependencei

Optimum temperature is 35 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei268Nucleophile1 Publication1
Active sitei327Charge relay system1 Publication1
Metal bindingi379CalciumBy similarity1
Active sitei380Charge relay system1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

ESTHERirhidl-lipas. Lipase_3.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase (EC:3.1.1.3)
Alternative name(s):
Lipase II
RNL
Triacylglycerol lipase
OrganismiRhizopus niveus
Taxonomic identifieri4844 [NCBI]
Taxonomic lineageiEukaryotaFungiFungi incertae sedisMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi313E → V: Increases the optimum temperature to 50 degrees Celsius. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
PropeptideiPRO_000001773327 – 951 PublicationAdd BLAST69
ChainiPRO_000001773496 – 392LipaseAdd BLAST297

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi152 ↔ 3911 Publication
Disulfide bondi163 ↔ 1661 Publication
Disulfide bondi358 ↔ 3671 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Structurei

Secondary structure

1392
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi129 – 131Combined sources3
Helixi134 – 149Combined sources16
Turni153 – 158Combined sources6
Helixi164 – 169Combined sources6
Beta strandi174 – 181Combined sources8
Turni182 – 185Combined sources4
Beta strandi186 – 193Combined sources8
Turni194 – 197Combined sources4
Beta strandi198 – 204Combined sources7
Helixi210 – 214Combined sources5
Beta strandi220 – 222Combined sources3
Beta strandi230 – 232Combined sources3
Helixi233 – 256Combined sources24
Beta strandi261 – 267Combined sources7
Helixi269 – 284Combined sources16
Turni290 – 292Combined sources3
Beta strandi293 – 299Combined sources7
Helixi306 – 315Combined sources10
Beta strandi319 – 324Combined sources6
Helixi329 – 331Combined sources3
Helixi335 – 337Combined sources3
Beta strandi342 – 350Combined sources9
Turni351 – 353Combined sources3
Beta strandi354 – 358Combined sources5
Beta strandi360 – 362Combined sources3
Beta strandi365 – 367Combined sources3
Helixi368 – 370Combined sources3
Helixi378 – 381Combined sources4
Beta strandi386 – 390Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LGYX-ray2.20A/B/C124-392[»]
ProteinModelPortaliP61871.
SMRiP61871.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61871.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
[Graphical view]
PfamiPF01764. Lipase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P61871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFISISQG VSLCLLVSSM MLGSSAVPVS GKSGSSNTAV SASDNAALPP
60 70 80 90 100
LISSRCAPPS NKGSKSDLQA EPYNMQKNTE WYESHGGNLT SIGKRDDNLV
110 120 130 140 150
GGMTLDLPSD APPISLSSST NSASDGGKVV AATTAQIQEF TKYAGIAATA
160 170 180 190 200
YCRSVVPGNK WDCVQCQKWV PDGKIITTFT SLLSDTNGYV LRSDKQKTIY
210 220 230 240 250
LVFRGTNSFR SAITDIVFNF SDYKPVKGAK VHAGFLSSYE QVVNDYFPVV
260 270 280 290 300
QEQLTAHPTY KVIVTGHSLG GAQALLAGMD LYQREPRLSP KNLSIFTVGG
310 320 330 340 350
PRVGNPTFAY YVESTGIPFQ RTVHKRDIVP HVPPQSFGFL HPGVESWIKS
360 370 380 390
GTSNVQICTS EIETKDCSNS IVPFTSILDH LSYFDINEGS CL
Length:392
Mass (Da):42,139
Last modified:June 7, 2004 - v1
Checksum:iD08F651EE77AA5A3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti348I → M in AAC60540 (PubMed:1368341).Curated1
Sequence conflicti348I → M in BAA02181 (PubMed:1368341).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013496 Genomic DNA. Translation: BAA31548.1.
D13206 Genomic DNA. Translation: BAA02493.1.
S39525 mRNA. Translation: AAC60540.2.
D12680 mRNA. Translation: BAA02181.1.
PIRiJT0604.
PC2171.
PC2172.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013496 Genomic DNA. Translation: BAA31548.1.
D13206 Genomic DNA. Translation: BAA02493.1.
S39525 mRNA. Translation: AAC60540.2.
D12680 mRNA. Translation: BAA02181.1.
PIRiJT0604.
PC2171.
PC2172.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LGYX-ray2.20A/B/C124-392[»]
ProteinModelPortaliP61871.
SMRiP61871.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERirhidl-lipas. Lipase_3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP61871.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
[Graphical view]
PfamiPF01764. Lipase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIP_RHINI
AccessioniPrimary (citable) accession number: P61871
Secondary accession number(s): O74166, P21811, Q12237
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: November 2, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Limited proteolysis produces a smaller peptide starting at residue Ser-124, that has altered substrate specificity and biophysicochemical properties.

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.