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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)DescriptionActionsGraphical viewLength
Active sitei236Acyl-ester intermediate1
Active sitei373Charge relay system1
Active sitei482Charge relay system1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Protein family/group databases

ESTHERigeoca-2lipa. Fungal_carboxylesterase_lipase.

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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeGeotrichum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000000862520 – 563Lipase 2Add BLAST544

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei20Pyrrolidone carboxylic acid1
Disulfide bondi80 ↔ 124
Disulfide bondi295 ↔ 307
Glycosylationi302N-linked (GlcNAc...)Sequence analysis1
Glycosylationi383N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1563
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni27 – 29Combined sources3
Beta strandi30 – 33Combined sources4
Beta strandi35 – 37Combined sources3
Beta strandi40 – 47Combined sources8
Helixi54 – 56Combined sources3
Helixi85 – 96Combined sources12
Helixi98 – 101Combined sources4
Helixi104 – 113Combined sources10
Beta strandi126 – 132Combined sources7
Beta strandi141 – 147Combined sources7
Helixi156 – 159Combined sources4
Helixi163 – 171Combined sources9
Beta strandi177 – 181Combined sources5
Helixi186 – 190Combined sources5
Helixi194 – 199Combined sources6
Helixi204 – 219Combined sources16
Helixi220 – 223Combined sources4
Beta strandi225 – 235Combined sources11
Helixi237 – 247Combined sources11
Helixi248 – 250Combined sources3
Beta strandi258 – 260Combined sources3
Beta strandi262 – 268Combined sources7
Beta strandi275 – 277Combined sources3
Beta strandi280 – 283Combined sources4
Helixi285 – 293Combined sources9
Helixi301 – 310Combined sources10
Helixi313 – 327Combined sources15
Turni329 – 331Combined sources3
Helixi334 – 336Combined sources3
Beta strandi344 – 347Combined sources4
Helixi351 – 356Combined sources6
Beta strandi365 – 370Combined sources6
Turni373 – 377Combined sources5
Helixi378 – 381Combined sources4
Helixi387 – 397Combined sources11
Turni398 – 400Combined sources3
Helixi403 – 412Combined sources10
Helixi417 – 419Combined sources3
Beta strandi420 – 422Combined sources3
Turni426 – 429Combined sources4
Beta strandi431 – 434Combined sources4
Helixi435 – 446Combined sources12
Helixi448 – 457Combined sources10
Beta strandi463 – 468Combined sources6
Turni470 – 474Combined sources5
Turni476 – 478Combined sources3
Beta strandi479 – 481Combined sources3
Turni482 – 485Combined sources4
Helixi486 – 490Combined sources5
Helixi497 – 510Combined sources14
Turni527 – 529Combined sources3
Beta strandi531 – 535Combined sources5
Beta strandi540 – 545Combined sources6
Helixi549 – 557Combined sources9
Helixi559 – 561Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1THGX-ray1.80A26-563[»]
ProteinModelPortaliP22394.
SMRiP22394.
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:June 1, 1994 - v2
Checksum:i12AA134A258C652F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23 – 25RPS → TAV in AAA03430 (PubMed:8306978).Curated3
Sequence conflicti23 – 25RPS → TAV in AAA03436 (PubMed:8306978).Curated3
Sequence conflicti36L → V in AAA03430 (PubMed:8306978).Curated1
Sequence conflicti36L → V in AAA03437 (PubMed:8306978).Curated1
Sequence conflicti138 – 139DA → ED in AAA03430 (PubMed:8306978).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti46I → V in strain: NRRL Y-552. 1
Natural varianti247I → V in strain: NRRL Y-553. 1
Natural varianti355F → Y in strain: NRRL Y-553. 1
Natural varianti391K → R in strain: NRRL Y-553. 1
Natural varianti439A → S in strain: NRRL Y-553. 1
Natural varianti484N → D in strain: NRRL Y-552. 1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1THGX-ray1.80A26-563[»]
ProteinModelPortaliP22394.
SMRiP22394.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERigeoca-2lipa. Fungal_carboxylesterase_lipase.

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...

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: August 1, 1991
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 100 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

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.