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P22394

- LIP2_GEOCN

UniProt

P22394 - LIP2_GEOCN

Protein

Lipase 2

Gene

LIP2

Organism
Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    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

    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 identifieri27317 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaemitosporic DipodascaceaeGeotrichum

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    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:
    PDBe
    RCSB PDB
    PDBj
    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

    MVSKSLFLAA AVNLAGVLAQ APRPSLNGNE VISGVLEGKV DTFKGIPFAD    50
    PPLNDLRFKH PQPFTGSYQG LKANDFSPAC MQLDPGNSLT LLDKALGLAK 100
    VIPEEFRGPL YDMAKGTVSM NEDCLYLNVF RPAGTKPDAK LPVMVWIYGG 150
    AFVYGSSAAY PGNSYVKESI NMGQPVVFVS INYRTGPFGF LGGDAITAEG 200
    NTNAGLHDQR KGLEWVSDNI ANFGGDPDKV MIFGESAGAM SVAHQLIAYG 250
    GDNTYNGKKL FHSAILQSGG PLPYHDSSSV GPDISYNRFA QYAGCDTSAS 300
    ANDTLECLRS KSSSVLHDAQ NSYDLKDLFG LLPQFLGFGP RPDGNIIPDA 350
    AYELFRSGRY AKVPYISGNQ EDEGTAFAPV ALNATTTPHV KKWLQYIFYD 400
    ASEASIDRVL SLYPQTLSVG SPFRTGILNA LTPQFKRVAA ILSDMLFQSP 450
    RRVMLSATKD VNRWTYLSTH LHNLVPFLGT FHGNELIFQF NVNIGPANSY 500
    LRYFISFANH HDPNVGTNLL QWDQYTDEGK EMLEIHMTDN VMRTDDYRIE 550
    GISNFETDVN LYG 563
    Length:563
    Mass (Da):61,617
    Last modified:June 1, 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi PN0493.
    PX0030.
    S41094.
    S41095.
    S41096.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1THG X-ray 1.80 A 26-563 [» ]
    ProteinModelPortali P22394.
    SMRi P22394. Positions 20-563.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P22394.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    [Graphical view ]
    Pfami PF00135. COesterase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
    PS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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(1993) [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(1990) [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(1994) [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(1990) [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(1995) [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(1991) [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(1993) [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: August 1, 1991
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 91 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