ID LIP5_DIURU Reviewed; 549 AA. AC P32949; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 85. DE RecName: Full=Lipase 5; DE EC=3.1.1.3; DE Flags: Precursor; GN Name=LIP5; 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 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 -!- 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; X66008; CAA46807.1; -; Genomic_DNA. DR PIR; JN0553; JN0553. DR SMR; P32949; -. DR ESTHER; canru-5lipa; Fungal_carboxylesterase_lipase. DR GlyCosmos; P32949; 2 sites, No reported glycans. 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 GO; GO:0004806; F:triacylglycerol lipase activity; IEA:UniProtKB-EC. DR AlphaFoldDB; P32949; -. PE 3: Inferred from homology; KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation; KW Lipid metabolism; Signal. FT SIGNAL 1..15 FT CHAIN 16..549 FT /note="Lipase 5" FT /id="PRO_0000008623" 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" SQ SEQUENCE 549 AA; 58420 MW; 0F3D04C9716F6F22 CRC64; MKLALALSLI ASVAAAPTAT LANGDTITGL NAIINEAFLG IPFAEPPVGN LRFKDPVPYR GSLNGQSFTA YGPSCMQQNP EGTYEENLPK VALDLVMQSK VFQAVLPNSE DCLTINVVRP PGTKAGANLP VMLWIFGGGF EIGSPTIFPP AQMVSKSVLM GKPIIHVAVN YRLASFGFLA GPDIKAEGSS NAGLKDQRLG MQWVADNIAG FGGDPSKVTI FGESAGSMSV LCHLLWNGGD NTYKGKPLFR AGIMQSGAMV PSDPVDGTYG TQIYDTLVAS TGCSSASNKL ACLRGLSTQA LLDATNDTPG FLSYTSLRLS YLPRPDGANI TDDMYKLVRD GKYASVPVII GDQNDEGFLF GLSSLNTTTE ADAEAYLRKS FIHATDADIT ALKAAYPSDV TQGSPFDTGI LNALTPQLKR INAVLGDLTF TLSRRYFLNH YTGGPKYSFL SKQLSGLPIL GTFHANDIVW QHFLLGSGSV IYNNAFIAFA TDLDPNTAGL SVQWPKSTSS SQAGDNLMQI SALGLYTGKD NFRTAGYNAL FADPSHFFV //