ID LIP3_DIURU Reviewed; 549 AA. AC P32947; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 106. DE RecName: Full=Lipase 3; DE EC=3.1.1.3; DE AltName: Full=Cholesterol esterase; DE Flags: Precursor; GN Name=LIP3; OS Diutina rugosa (Yeast) (Candida rugosa). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes; OC Debaryomycetaceae; Diutina. OX NCBI_TaxID=5481; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506; RX PubMed=8440480; DOI=10.1016/0378-1119(93)90760-z; RA Lotti M., Grandori R., Fusetti F., Longhi S., Brocca S., Tramontano A., RA Alberghina L.; RT "Cloning and analysis of Candida cylindracea lipase sequences."; RL Gene 124:45-55(1993). RN [2] RP PROTEIN SEQUENCE OF 16-549, AND SUBUNIT STRUCTURE. RX PubMed=8287964; DOI=10.1016/0014-5793(94)80257-2; RA Kaiser R., Erman M., Duax W.L., Ghosh D., Joernvall H.; RT "Monomeric and dimeric forms of cholesterol esterase from Candida RT cylindracea. Primary structure, identity in peptide patterns, and RT additional microheterogeneity."; RL FEBS Lett. 337:123-127(1994). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=7788294; DOI=10.1016/s0969-2126(01)00158-7; RA Ghosh D., Wawrzak Z., Pletnev V.Z., Li N., Kaiser R., Pangborn W., RA Joernvall H., Erman M., Duax W.L.; RT "Structure of uncomplexed and linoleate-bound Candida cylindracea RT cholesterol esterase."; RL Structure 3:279-288(1995). RN [4] RP REVIEW. RX PubMed=9778794; RX DOI=10.1002/(sici)1097-0061(19980915)14:12<1069::aid-yea303>3.0.co;2-k; RA Benjamin S., Pandey A.; RT "Candida rugosa lipases: molecular biology and versatility in RT biotechnology."; RL Yeast 14:1069-1087(1998). 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 and homodimer. {ECO:0000269|PubMed:8287964}. 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; X66006; CAA46805.1; -; Genomic_DNA. DR PIR; JN0551; JN0551. DR PIR; S41735; S41735. DR PDB; 1CLE; X-ray; 2.00 A; A/B=16-549. DR PDB; 1LLF; X-ray; 1.40 A; A/B=16-549. DR AlphaFoldDB; P32947; -. DR MDRepo; P32947; -. DR SMR; P32947; -. DR DrugBank; DB02092; Cholesteryl Linoleate. DR DrugBank; DB03500; Tricosanoic acid. DR ESTHER; canru-3lipa; Fungal_carboxylesterase_lipase. DR GlyCosmos; P32947; 2 sites, No reported glycans. DR BRENDA; 3.1.1.3; 1139. DR EvolutionaryTrace; P32947; -. DR GO; GO:0004806; F:triacylglycerol lipase activity; IEA:UniProtKB-EC. DR CDD; cd00312; Esterase_lipase; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase_fold. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR019826; Carboxylesterase_B_AS. DR InterPro; IPR019819; Carboxylesterase_B_CS. DR InterPro; IPR050309; Type-B_Carboxylest/Lipase. DR PANTHER; PTHR11559; CARBOXYLESTERASE; 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. DR PDBsum; 1CLE; -. DR PDBsum; 1LLF; -. PE 1: Evidence at protein level; KW 3D-structure; Cholesterol metabolism; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation; KW Lipid metabolism; Signal; Steroid metabolism; Sterol metabolism. FT SIGNAL 1..15 FT /evidence="ECO:0000269|PubMed:8287964" FT CHAIN 16..549 FT /note="Lipase 3" FT /id="PRO_0000008621" FT ACT_SITE 224 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039" FT ACT_SITE 356 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 464 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT CARBOHYD 329 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 366 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 75..112 FT /evidence="ECO:0000250" FT DISULFID 283..292 FT /evidence="ECO:0000250" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 36..42 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 88..98 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 100..105 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 114..119 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 129..135 FT /evidence="ECO:0007829|PDB:1LLF" FT TURN 139..141 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 151..159 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 165..169 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 174..178 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 182..187 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 192..207 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 208..211 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 213..223 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 225..235 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 236..239 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 250..256 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 268..280 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 289..295 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 298..306 FT /evidence="ECO:0007829|PDB:1LLF" FT TURN 314..317 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 327..330 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 334..339 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 348..353 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 358..361 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 362..364 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 370..380 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 386..395 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 400..402 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 403..405 FT /evidence="ECO:0007829|PDB:1LLF" FT TURN 409..412 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 413..417 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 418..426 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 427..431 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 432..440 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 446..451 FT /evidence="ECO:0007829|PDB:1LLF" FT TURN 453..456 FT /evidence="ECO:0007829|PDB:1LLF" FT TURN 458..460 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 469..473 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 480..485 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 486..492 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 495..498 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 517..521 FT /evidence="ECO:0007829|PDB:1LLF" FT STRAND 524..528 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 534..541 FT /evidence="ECO:0007829|PDB:1LLF" FT HELIX 544..547 FT /evidence="ECO:0007829|PDB:1LLF" SQ SEQUENCE 549 AA; 58755 MW; C5F95C31422975DA CRC64; MKLALALSLI ASVAAAPTAK LANGDTITGL NAIINEAFLG IPFAEPPVGN LRFKDPVPYS GSLNGQKFTS YGPSCMQQNP EGTFEENLGK TALDLVMQSK VFQAVLPQSE DCLTINVVRP PGTKAGANLP VMLWIFGGGF EIGSPTIFPP AQMVTKSVLM GKPIIHVAVN YRVASWGFLA GDDIKAEGSG NAGLKDQRLG MQWVADNIAG FGGDPSKVTI FGESAGSMSV LCHLIWNDGD NTYKGKPLFR AGIMQSGAMV PSDPVDGTYG NEIYDLFVSS AGCGSASDKL ACLRSASSDT LLDATNNTPG FLAYSSLRLS YLPRPDGKNI TDDMYKLVRD GKYASVPVII GDQNDEGTIF GLSSLNVTTN AQARAYFKQS FIHASDAEID TLMAAYPQDI TQGSPFDTGI FNAITPQFKR ISAVLGDLAF IHARRYFLNH FQGGTKYSFL SKQLSGLPIM GTFHANDIVW QDYLLGSGSV IYNNAFIAFA TDLDPNTAGL LVNWPKYTSS SQSGNNLMMI NALGLYTGKD NFRTAGYDAL MTNPSSFFV //