ID LIP1_CANRU Reviewed; 549 AA. AC P20261; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 3. DT 28-NOV-2006, entry version 52. DE Lipase 1 precursor (EC 3.1.1.3). GN Name=LIP1; OS Candida rugosa (Yeast) (Candida cylindracea). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. 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 MEDLINE=92305068; PubMed=1610906; DOI=10.1016/0167-4781(92)90085-E; RA Longhi S., Fusetti F., Grandori R., Lotti M., Vanoni M., RA 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 NUCLEOTIDE SEQUENCE [MRNA] OF 12-549, AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506; RX MEDLINE=89384874; PubMed=2506450; DOI=10.1038/341164a0; RA Kawaguchi Y., Honda H., Taniguchi-Morimura J., Iwasaki S.; RT "The codon CUG is read as serine in an asporogenic yeast Candida RT cylindracea."; RL Nature 341:164-166(1989). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS). RX MEDLINE=93286131; PubMed=8509417; RA Grochulski P., Li Y., Schrag J.D., Bouthillier F., Smith P., RA Harrison D., Rubin B., Cygler M.; RT "Insights into interfacial activation from an open structure of RT Candida rugosa lipase."; RL J. Biol. Chem. 268:12843-12847(1993). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). RX MEDLINE=94190867; PubMed=8142346; DOI=10.1021/bi00178a005; RA Grochulski P., Bouthillier F., Kazlauskas R.J., Serreqi A.N., RA Schrag J.D., Ziomek E., Cygler M.; RT "Analogs of reaction intermediates identify a unique substrate binding RT site in Candida rugosa lipase."; RL Biochemistry 33:3494-3500(1994). RN [5] RP REVIEW. RX MEDLINE=98451816; PubMed=9778794; RX DOI=10.1002/(SICI)1097-0061(19980915)14:12<1069::AID-YEA303>3.3.CO;2-B; 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: Triacylglycerol + H(2)O = diacylglycerol + a CC carboxylate. CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family. 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; X64703; CAA45957.1; -; Genomic_DNA. DR EMBL; X16712; CAA34684.1; -; mRNA. DR PIR; S05684; S05684. DR PIR; S23448; S23448. DR PDB; 1CRL; X-ray; @=16-549. DR PDB; 1LPM; X-ray; @=1-549. DR PDB; 1LPN; X-ray; @=1-549. DR PDB; 1LPO; X-ray; @=1-549. DR PDB; 1LPP; X-ray; @=1-549. DR PDB; 1LPS; X-ray; @=1-549. DR PDB; 1TRH; X-ray; @=16-549. DR LinkHub; P20261; -. DR GO; GO:0004806; F:triacylglycerol lipase activity; IEA:EC. DR InterPro; IPR002018; CarbesteraseB. DR Pfam; PF00135; COesterase; 1. DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. KW 3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; KW Lipid degradation; Signal. FT SIGNAL 1 15 FT CHAIN 16 549 Lipase 1. FT /FTId=PRO_0000008619. FT ACT_SITE 224 224 Acyl-ester intermediate. FT ACT_SITE 356 356 Charge relay system. FT ACT_SITE 464 464 Charge relay system. FT CARBOHYD 329 329 N-linked (GlcNAc...). FT CARBOHYD 366 366 N-linked (GlcNAc...). FT DISULFID 75 112 FT DISULFID 283 292 FT VARIANT 398 398 G -> Q. FT STRAND 18 20 FT TURN 22 23 FT STRAND 26 28 FT STRAND 33 42 FT HELIX 49 51 FT TURN 52 53 FT TURN 64 65 FT TURN 80 81 FT HELIX 88 97 FT TURN 98 98 FT HELIX 100 105 FT STRAND 114 119 FT TURN 121 122 FT TURN 125 126 FT STRAND 129 135 FT TURN 139 141 FT TURN 146 147 FT HELIX 151 159 FT TURN 160 161 FT STRAND 165 169 FT HELIX 174 178 FT HELIX 182 187 FT TURN 188 188 FT TURN 190 191 FT HELIX 192 207 FT HELIX 208 211 FT TURN 212 212 FT STRAND 213 223 FT TURN 224 224 FT HELIX 225 235 FT HELIX 236 239 FT TURN 244 245 FT STRAND 246 248 FT STRAND 250 256 FT TURN 265 266 FT HELIX 268 281 FT TURN 282 282 FT TURN 284 285 FT HELIX 289 295 FT HELIX 298 306 FT TURN 307 307 FT TURN 311 312 FT TURN 314 317 FT STRAND 327 330 FT HELIX 334 339 FT TURN 340 341 FT STRAND 348 353 FT TURN 354 354 FT TURN 356 357 FT HELIX 358 361 FT HELIX 362 364 FT TURN 365 366 FT HELIX 370 380 FT TURN 382 383 FT HELIX 386 395 FT HELIX 400 402 FT STRAND 403 405 FT TURN 406 407 FT TURN 409 412 FT STRAND 414 417 FT HELIX 418 429 FT TURN 430 430 FT HELIX 431 440 FT STRAND 446 451 FT TURN 453 456 FT TURN 458 460 FT STRAND 461 463 FT TURN 464 465 FT HELIX 466 472 FT TURN 473 473 FT TURN 477 478 FT HELIX 479 482 FT TURN 483 483 FT HELIX 484 492 FT HELIX 495 498 FT TURN 510 511 FT STRAND 517 520 FT STRAND 525 528 FT HELIX 534 541 FT HELIX 544 547 SQ SEQUENCE 549 AA; 58550 MW; 27A40BD318757CE0 CRC64; MELALALSLI ASVAAAPTAT LANGDTITGL NAIINEAFLG IPFAEPPVGN LRFKDPVPYS GSLDGQKFTS YGPSCMQQNP EGTYEENLPK AALDLVMQSK VFEAVSPSSE DCLTINVVRP PGTKAGANLP VMLWIFGGGF EVGGTSTFPP AQMITKSIAM GKPIIHVSVN YRVSSWGFLA GDEIKAEGSA NAGLKDQRLG MQWVADNIAA FGGDPTKVTI FGESAGSMSV MCHILWNDGD NTYKGKPLFR AGIMQSGAMV PSDAVDGIYG NEIFDLLASN AGCGSASDKL ACLRGVSSDT LEDATNNTPG FLAYSSLRLS YLPRPDGVNI TDDMYALVRE GKYANIPVII GDQNDEGTFF GTSSLNVTTD AQAREYFKQS FVHASDAEID TLMTAYPGDI TQGSPFDTGI LNALTPQFKR ISAVLGDLGF TLARRYFLNH YTGGTKYSFL SKQLSGLPVL GTFHSNDIVF QDYLLGSGSL IYNNAFIAFA TDLDPNTAGL LVKWPEYTSS SQSGNNLMMI NALGLYTGKD NFRTAGYDAL FSNPPSFFV //