LIP2_GEOCN
ID LIP2_GEOCN Reviewed; 563 AA.
AC P22394; Q00885; Q00890; Q00892; Q02213; Q96VH7;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Lipase 2;
DE EC=3.1.1.3;
DE AltName: Full=GCL II;
DE AltName: Full=Lipase II;
DE Flags: Precursor;
GN Name=LIP2;
OS Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 34614;
RX PubMed=8370674; DOI=10.1093/oxfordjournals.jbchem.a124117;
RA Nagao T., Shimada Y., Sugihara A., Tominaga Y.;
RT "Cloning and sequencing of two chromosomal lipase genes from Geotrichum
RT candidum.";
RL J. Biochem. 113:776-780(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-563, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2398037; DOI=10.1093/oxfordjournals.jbchem.a123112;
RA Shimada Y., Sugihara A., Iizumi T., Tominaga Y.;
RT "cDNA cloning and characterization of Geotrichum candidum lipase II.";
RL J. Biochem. 107:703-707(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-563.
RC STRAIN=ATCC 34614, ATCC 74169 / NRRL Y-552 / ED00652, and
RC ATCC 90287 / NRRL Y-553;
RX PubMed=8306978; DOI=10.1111/j.1432-1033.1994.tb19921.x;
RA Bertolini M.C., Laramee L., Thomas D.Y., Cygler M., Schrag J.D., Vernet T.;
RT "Polymorphism in the lipase genes of Geotrichum candidum strains.";
RL Eur. J. Biochem. 219:119-125(1994).
RN [4]
RP PROTEIN SEQUENCE OF 20-26 AND 561-563, AND PYROGLUTAMATE FORMATION AT
RP GLN-20.
RX PubMed=2341377; DOI=10.1093/oxfordjournals.jbchem.a123061;
RA Sugihara A., Shimada Y., Tominaga Y.;
RT "Separation and characterization of two molecular forms of Geotrichum
RT candidum lipase.";
RL J. Biochem. 107:426-430(1990).
RN [5]
RP CHARACTERIZATION.
RX PubMed=7737187; DOI=10.1111/j.1432-1033.1995.0863m.x;
RA Bertolini M.C., Schrag J.D., Cygler M., Ziomek E., Thomas D.Y., Vernet T.;
RT "Expression and characterization of Geotrichum candidum lipase I gene.
RT Comparison of specificity profile with lipase II.";
RL Eur. J. Biochem. 228:863-869(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=2062369; DOI=10.1038/351761a0;
RA Schrag J.D., Li Y., Wu S., Cygler M.;
RT "Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum
RT candidum.";
RL Nature 351:761-764(1991).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8464065; DOI=10.1006/jmbi.1993.1171;
RA Schrag J.D., Cygler M.;
RT "1.8 A refined structure of the lipase from Geotrichum candidum.";
RL J. Mol. Biol. 230:575-591(1993).
CC -!- FUNCTION: Hydrolyzes all ester bonds in triglyceride and displays a
CC high affinity for triolein. For unsaturated substrates having long
CC fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15)
CC GCL I shows higher specific activity than GCL II, whereas GCL II shows
CC higher specific activity against saturated substrates having short
CC fatty acid chains (C8, C10, C12 and C14).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; S65090; AAB28108.1; -; Genomic_DNA.
DR EMBL; S65092; AAB28109.1; -; Genomic_DNA.
DR EMBL; D00697; BAA00603.1; -; mRNA.
DR EMBL; U02541; AAA03430.1; -; Genomic_DNA.
DR EMBL; U02623; AAA03436.1; -; Genomic_DNA.
DR EMBL; U02625; AAA03437.1; -; Genomic_DNA.
DR PIR; PN0493; PN0493.
DR PIR; PX0030; PX0030.
DR PIR; S41094; S41094.
DR PIR; S41095; S41095.
DR PIR; S41096; S41096.
DR PDB; 1THG; X-ray; 1.80 A; A=26-563.
DR PDBsum; 1THG; -.
DR AlphaFoldDB; P22394; -.
DR SMR; P22394; -.
DR ESTHER; geoca-2lipa; Fungal_carboxylesterase_lipase.
DR EvolutionaryTrace; P22394; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism;
KW Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2341377"
FT CHAIN 20..563
FT /note="Lipase 2"
FT /id="PRO_0000008625"
FT ACT_SITE 236
FT /note="Acyl-ester intermediate"
FT ACT_SITE 373
FT /note="Charge relay system"
FT ACT_SITE 482
FT /note="Charge relay system"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2341377"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..124
FT DISULFID 295..307
FT VARIANT 46
FT /note="I -> V (in strain: NRRL Y-552)"
FT VARIANT 247
FT /note="I -> V (in strain: NRRL Y-553)"
FT VARIANT 355
FT /note="F -> Y (in strain: NRRL Y-553)"
FT VARIANT 391
FT /note="K -> R (in strain: NRRL Y-553)"
FT VARIANT 439
FT /note="A -> S (in strain: NRRL Y-553)"
FT VARIANT 484
FT /note="N -> D (in strain: NRRL Y-552)"
FT CONFLICT 23..25
FT /note="RPS -> TAV (in Ref. 3; AAA03430/AAA03436)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="L -> V (in Ref. 3; AAA03430/AAA03437)"
FT /evidence="ECO:0000305"
FT CONFLICT 138..139
FT /note="DA -> ED (in Ref. 3; AAA03430)"
FT /evidence="ECO:0000305"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 204..219
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 225..235
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 313..327
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 373..377
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 403..412
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 426..429
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 435..446
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 448..457
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 470..474
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 482..485
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 486..490
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 497..510
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:1THG"
SQ SEQUENCE 563 AA; 61617 MW; 12AA134A258C652F CRC64;
MVSKSLFLAA AVNLAGVLAQ APRPSLNGNE VISGVLEGKV DTFKGIPFAD PPLNDLRFKH
PQPFTGSYQG LKANDFSPAC MQLDPGNSLT LLDKALGLAK VIPEEFRGPL YDMAKGTVSM
NEDCLYLNVF RPAGTKPDAK LPVMVWIYGG AFVYGSSAAY PGNSYVKESI NMGQPVVFVS
INYRTGPFGF LGGDAITAEG NTNAGLHDQR KGLEWVSDNI ANFGGDPDKV MIFGESAGAM
SVAHQLIAYG GDNTYNGKKL FHSAILQSGG PLPYHDSSSV GPDISYNRFA QYAGCDTSAS
ANDTLECLRS KSSSVLHDAQ NSYDLKDLFG LLPQFLGFGP RPDGNIIPDA AYELFRSGRY
AKVPYISGNQ EDEGTAFAPV ALNATTTPHV KKWLQYIFYD ASEASIDRVL SLYPQTLSVG
SPFRTGILNA LTPQFKRVAA ILSDMLFQSP RRVMLSATKD VNRWTYLSTH LHNLVPFLGT
FHGNELIFQF NVNIGPANSY LRYFISFANH HDPNVGTNLL QWDQYTDEGK EMLEIHMTDN
VMRTDDYRIE GISNFETDVN LYG
