ID LIP2_DIURU Reviewed; 548 AA. AC P32946; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 99. DE RecName: Full=Lipase 2; DE EC=3.1.1.3; DE Flags: Precursor; GN Name=LIP2; 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=1610906; DOI=10.1016/0167-4781(92)90085-e; RA Longhi S., Fusetti F., Grandori R., Lotti M., Vanoni M., Alberghina L.; RT "Cloning and nucleotide sequences of two lipase genes from Candida RT cylindracea."; RL Biochim. Biophys. Acta 1131:227-232(1992). 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). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 15-548, DISULFIDE BONDS, AND RP GLYCOSYLATION AT ASN-365. RX PubMed=14499609; DOI=10.1016/j.jmb.2003.08.005; RA Mancheno J.M., Pernas M.A., Martinez M.J., Ochoa B., Rua M.L., RA Hermoso J.A.; RT "Structural insights into the lipase/esterase behavior in the Candida RT rugosa lipases family: crystal structure of the lipase 2 isoenzyme at 1.97A RT resolution."; RL J. Mol. Biol. 332:1059-1069(2003). 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; X64704; CAA45958.1; -; Genomic_DNA. DR PIR; S32615; S32615. DR PDB; 1GZ7; X-ray; 1.97 A; A/B/C/D=15-548. DR AlphaFoldDB; P32946; -. DR SMR; P32946; -. DR ESTHER; canru-2lipa; Fungal_carboxylesterase_lipase. DR GlyCosmos; P32946; 1 site, No reported glycans. DR iPTMnet; P32946; -. DR EvolutionaryTrace; P32946; -. 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; 1GZ7; -. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation; KW Lipid metabolism; Signal. FT SIGNAL 1..14 FT CHAIN 15..548 FT /note="Lipase 2" FT /id="PRO_0000008620" FT ACT_SITE 223 FT /note="Acyl-ester intermediate" FT ACT_SITE 355 FT /note="Charge relay system" FT ACT_SITE 463 FT /note="Charge relay system" FT CARBOHYD 365 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:14499609" FT DISULFID 74..111 FT /evidence="ECO:0000269|PubMed:14499609" FT DISULFID 282..291 FT /evidence="ECO:0000269|PubMed:14499609" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 32..41 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 76..78 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 89..98 FT /evidence="ECO:0007829|PDB:1GZ7" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 128..134 FT /evidence="ECO:0007829|PDB:1GZ7" FT TURN 138..140 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 150..158 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 164..168 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 173..177 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 181..186 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 191..206 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 207..210 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 212..222 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 224..234 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 235..238 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 249..255 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 267..279 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 288..293 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 297..304 FT /evidence="ECO:0007829|PDB:1GZ7" FT TURN 313..316 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 326..329 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 333..338 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 347..352 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 357..360 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 361..363 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 369..379 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 385..394 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 399..401 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 402..404 FT /evidence="ECO:0007829|PDB:1GZ7" FT TURN 408..411 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 417..425 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 426..430 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 431..439 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 445..450 FT /evidence="ECO:0007829|PDB:1GZ7" FT TURN 452..455 FT /evidence="ECO:0007829|PDB:1GZ7" FT TURN 457..459 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 460..462 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 468..472 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 479..484 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 485..491 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 494..497 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 511..513 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 516..519 FT /evidence="ECO:0007829|PDB:1GZ7" FT STRAND 524..527 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 533..540 FT /evidence="ECO:0007829|PDB:1GZ7" FT HELIX 543..546 FT /evidence="ECO:0007829|PDB:1GZ7" SQ SEQUENCE 548 AA; 58865 MW; E0DBCFF2501E7614 CRC64; MKLCLLALGA AVAAAPTATL ANGDTITGLN AIVNEKFLGI PFAEPPVGTL RFKPPVPYSA SLNGQQFTSY GPSCMQMNPM GSFEDTLPKN ARHLVLQSKI FQVVLPNDED CLTINVIRPP GTRASAGLPV MLWIFGGGFE LGGSSLFPGD QMVAKSVLMG KPVIHVSMNY RVASWGFLAG PDIQNEGSGN AGLHDQRLAM QWVADNIAGF GGDPSKVTIY GESAGSMSTF VHLVWNDGDN TYNGKPLFRA AIMQSGCMVP SDPVDGTYGT EIYNQVVASA GCGSASDKLA CLRGLSQDTL YQATSDTPGV LAYPSLRLSY LPRPDGTFIT DDMYALVRDG KYAHVPVIIG DQNDEGTLFG LSSLNVTTDA QARAYFKQSF IHASDAEIDT LMAAYTSDIT QGSPFDTGIF NAITPQFKRI SALLGDLAFT LARRYFLNYY QGGTKYSFLS KQLSGLPVLG TFHGNDIIWQ DYLVGSGSVI YNNAFIAFAN DLDPNKAGLW TNWPTYTSSS QSGNNLMQIN GLGLYTGKDN FRPDAYSALF SNPPSFFV //