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Protein

Lipase 2

Gene

LIP2

Organism
Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes all ester bonds in triglyceride and displays a high affinity for triolein. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15) GCL I shows higher specific activity than GCL II, whereas GCL II shows higher specific activity against saturated substrates having short fatty acid chains (C8, C10, C12 and C14).

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei236 – 2361Acyl-ester intermediate
Active sitei373 – 3731Charge relay system
Active sitei482 – 4821Charge relay system

GO - Molecular functioni

  1. triglyceride lipase activity Source: UniProtKB-EC

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase 2 (EC:3.1.1.3)
Alternative name(s):
GCL II
Lipase II
Gene namesi
Name:LIP2
OrganismiGeotrichum candidum (Oospora lactis) (Dipodascus geotrichum)
Taxonomic identifieri1173061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeGalactomyces

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 563544Lipase 2PRO_0000008625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Pyrrolidone carboxylic acid
Disulfide bondi80 ↔ 124
Disulfide bondi295 ↔ 307
Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi383 – 3831N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
563
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni27 – 293
Beta strandi30 – 334
Beta strandi35 – 373
Beta strandi40 – 478
Helixi54 – 563
Helixi85 – 9612
Helixi98 – 1014
Helixi104 – 11310
Beta strandi126 – 1327
Beta strandi141 – 1477
Helixi156 – 1594
Helixi163 – 1719
Beta strandi177 – 1815
Helixi186 – 1905
Helixi194 – 1996
Helixi204 – 21916
Helixi220 – 2234
Beta strandi225 – 23511
Helixi237 – 24711
Helixi248 – 2503
Beta strandi258 – 2603
Beta strandi262 – 2687
Beta strandi275 – 2773
Beta strandi280 – 2834
Helixi285 – 2939
Helixi301 – 31010
Helixi313 – 32715
Turni329 – 3313
Helixi334 – 3363
Beta strandi344 – 3474
Helixi351 – 3566
Beta strandi365 – 3706
Turni373 – 3775
Helixi378 – 3814
Helixi387 – 39711
Turni398 – 4003
Helixi403 – 41210
Helixi417 – 4193
Beta strandi420 – 4223
Turni426 – 4294
Beta strandi431 – 4344
Helixi435 – 44612
Helixi448 – 45710
Beta strandi463 – 4686
Turni470 – 4745
Turni476 – 4783
Beta strandi479 – 4813
Turni482 – 4854
Helixi486 – 4905
Helixi497 – 51014
Turni527 – 5293
Beta strandi531 – 5355
Beta strandi540 – 5456
Helixi549 – 5579
Helixi559 – 5613

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1THGX-ray1.80A26-563[»]
ProteinModelPortaliP22394.
SMRiP22394. Positions 20-563.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22394.

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.

P22394-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSKSLFLAA AVNLAGVLAQ APRPSLNGNE VISGVLEGKV DTFKGIPFAD
60 70 80 90 100
PPLNDLRFKH PQPFTGSYQG LKANDFSPAC MQLDPGNSLT LLDKALGLAK
110 120 130 140 150
VIPEEFRGPL YDMAKGTVSM NEDCLYLNVF RPAGTKPDAK LPVMVWIYGG
160 170 180 190 200
AFVYGSSAAY PGNSYVKESI NMGQPVVFVS INYRTGPFGF LGGDAITAEG
210 220 230 240 250
NTNAGLHDQR KGLEWVSDNI ANFGGDPDKV MIFGESAGAM SVAHQLIAYG
260 270 280 290 300
GDNTYNGKKL FHSAILQSGG PLPYHDSSSV GPDISYNRFA QYAGCDTSAS
310 320 330 340 350
ANDTLECLRS KSSSVLHDAQ NSYDLKDLFG LLPQFLGFGP RPDGNIIPDA
360 370 380 390 400
AYELFRSGRY AKVPYISGNQ EDEGTAFAPV ALNATTTPHV KKWLQYIFYD
410 420 430 440 450
ASEASIDRVL SLYPQTLSVG SPFRTGILNA LTPQFKRVAA ILSDMLFQSP
460 470 480 490 500
RRVMLSATKD VNRWTYLSTH LHNLVPFLGT FHGNELIFQF NVNIGPANSY
510 520 530 540 550
LRYFISFANH HDPNVGTNLL QWDQYTDEGK EMLEIHMTDN VMRTDDYRIE
560
GISNFETDVN LYG
Length:563
Mass (Da):61,617
Last modified:May 31, 1994 - v2
Checksum:i12AA134A258C652F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 253RPS → TAV in AAA03430 (PubMed:8306978).Curated
Sequence conflicti23 – 253RPS → TAV in AAA03436 (PubMed:8306978).Curated
Sequence conflicti36 – 361L → V in AAA03430 (PubMed:8306978).Curated
Sequence conflicti36 – 361L → V in AAA03437 (PubMed:8306978).Curated
Sequence conflicti138 – 1392DA → ED in AAA03430 (PubMed:8306978).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461I → V in strain: NRRL Y-552.
Natural varianti247 – 2471I → V in strain: NRRL Y-553.
Natural varianti355 – 3551F → Y in strain: NRRL Y-553.
Natural varianti391 – 3911K → R in strain: NRRL Y-553.
Natural varianti439 – 4391A → S in strain: NRRL Y-553.
Natural varianti484 – 4841N → D in strain: NRRL Y-552.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S65090 Genomic DNA. Translation: AAB28108.1.
S65092 Genomic DNA. Translation: AAB28109.1.
D00697 mRNA. Translation: BAA00603.1.
U02541 Genomic DNA. Translation: AAA03430.1.
U02623 Genomic DNA. Translation: AAA03436.1.
U02625 Genomic DNA. Translation: AAA03437.1.
PIRiPN0493.
PX0030.
S41094.
S41095.
S41096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S65090 Genomic DNA. Translation: AAB28108.1.
S65092 Genomic DNA. Translation: AAB28109.1.
D00697 mRNA. Translation: BAA00603.1.
U02541 Genomic DNA. Translation: AAA03430.1.
U02623 Genomic DNA. Translation: AAA03436.1.
U02625 Genomic DNA. Translation: AAA03437.1.
PIRiPN0493.
PX0030.
S41094.
S41095.
S41096.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1THGX-ray1.80A26-563[»]
ProteinModelPortaliP22394.
SMRiP22394. Positions 20-563.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP22394.

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 sequencing of two chromosomal lipase genes from Geotrichum candidum."
    Nagao T., Shimada Y., Sugihara A., Tominaga Y.
    J. Biochem. 113:776-780(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 34614.
  2. "cDNA cloning and characterization of Geotrichum candidum lipase II."
    Shimada Y., Sugihara A., Iizumi T., Tominaga Y.
    J. Biochem. 107:703-707(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-563, PARTIAL PROTEIN SEQUENCE.
  3. "Polymorphism in the lipase genes of Geotrichum candidum strains."
    Bertolini M.C., Laramee L., Thomas D.Y., Cygler M., Schrag J.D., Vernet T.
    Eur. J. Biochem. 219:119-125(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-563.
    Strain: ATCC 34614, ATCC 74169 / NRRL Y-552 / ED00652 and ATCC 90287 / NRRL Y-553.
  4. "Separation and characterization of two molecular forms of Geotrichum candidum lipase."
    Sugihara A., Shimada Y., Tominaga Y.
    J. Biochem. 107:426-430(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-26 AND 561-563.
  5. "Expression and characterization of Geotrichum candidum lipase I gene. Comparison of specificity profile with lipase II."
    Bertolini M.C., Schrag J.D., Cygler M., Ziomek E., Thomas D.Y., Vernet T.
    Eur. J. Biochem. 228:863-869(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum."
    Schrag J.D., Li Y., Wu S., Cygler M.
    Nature 351:761-764(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  7. "1.8 A refined structure of the lipase from Geotrichum candidum."
    Schrag J.D., Cygler M.
    J. Mol. Biol. 230:575-591(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiLIP2_GEOCN
AccessioniPrimary (citable) accession number: P22394
Secondary accession number(s): Q00885
, Q00890, Q00892, Q02213, Q96VH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1991
Last sequence update: May 31, 1994
Last modified: January 6, 2015
This is version 93 of the entry and version 2 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

External Data

Dasty 3

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 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.