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 22-FEB-2023, entry version 114. 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 ATCC 90287 / RC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P22394; 2 sites, No reported glycans. 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 CDD; cd00312; Esterase_lipase; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR019826; Carboxylesterase_B_AS. DR InterPro; IPR019819; Carboxylesterase_B_CS. DR PANTHER; PTHR11559; CARBOXYLESTERASE; 1. DR PANTHER; PTHR11559:SF162; CARBOXYLIC ESTER HYDROLASE; 1. DR Pfam; PF00135; COesterase; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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: NRRLY-552)" FT VARIANT 247 FT /note="I -> V (in strain: NRRLY-553)" FT VARIANT 355 FT /note="F -> Y (in strain: NRRLY-553)" FT VARIANT 391 FT /note="K -> R (in strain: NRRLY-553)" FT VARIANT 439 FT /note="A -> S (in strain: NRRLY-553)" FT VARIANT 484 FT /note="N -> D (in strain: NRRLY-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 //