LIP1_DIURU
ID LIP1_DIURU Reviewed; 549 AA.
AC P20261;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 3.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Lipase 1;
DE EC=3.1.1.3;
DE Flags: Precursor;
GN Name=LIP1;
OS Diutina rugosa (Yeast) (Candida rugosa).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 12-549, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506;
RX 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 PubMed=8509417; DOI=10.1016/s0021-9258(18)31464-9;
RA Grochulski P., Li Y., Schrag J.D., Bouthillier F., Smith P., Harrison D.,
RA Rubin B., Cygler M.;
RT "Insights into interfacial activation from an open structure of Candida
RT rugosa lipase.";
RL J. Biol. Chem. 268:12843-12847(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RX PubMed=8142346; DOI=10.1021/bi00178a005;
RA Grochulski P., Bouthillier F., Kazlauskas R.J., Serreqi A.N., Schrag J.D.,
RA Ziomek E., Cygler M.;
RT "Analogs of reaction intermediates identify a unique substrate binding site
RT in Candida rugosa lipase.";
RL Biochemistry 33:3494-3500(1994).
RN [5]
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}.
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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; 2.06 A; A=16-549.
DR PDB; 1LPM; X-ray; 2.18 A; A=1-549.
DR PDB; 1LPN; X-ray; 2.18 A; A=1-549.
DR PDB; 1LPO; X-ray; 2.18 A; A=1-549.
DR PDB; 1LPP; X-ray; 2.18 A; A=1-549.
DR PDB; 1LPS; X-ray; 2.18 A; A=1-549.
DR PDB; 1TRH; X-ray; 2.10 A; A=16-549.
DR PDB; 3RAR; X-ray; 2.19 A; A=16-549.
DR PDBsum; 1CRL; -.
DR PDBsum; 1LPM; -.
DR PDBsum; 1LPN; -.
DR PDBsum; 1LPO; -.
DR PDBsum; 1LPP; -.
DR PDBsum; 1LPS; -.
DR PDBsum; 1TRH; -.
DR PDBsum; 3RAR; -.
DR AlphaFoldDB; P20261; -.
DR SMR; P20261; -.
DR DrugBank; DB02776; 1-Hexadecanosulfonic Acid.
DR ESTHER; canru-1lipa; Fungal_carboxylesterase_lipase.
DR BRENDA; 3.1.1.3; 1139.
DR EvolutionaryTrace; P20261; -.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 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; Signal.
FT SIGNAL 1..15
FT CHAIN 16..549
FT /note="Lipase 1"
FT /id="PRO_0000008619"
FT ACT_SITE 224
FT /note="Acyl-ester intermediate"
FT ACT_SITE 356
FT /note="Charge relay system"
FT ACT_SITE 464
FT /note="Charge relay system"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 75..112
FT DISULFID 283..292
FT VARIANT 398
FT /note="G -> Q"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1TRH"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1TRH"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1CRL"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1LPM"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 213..223
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:1CRL"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 370..380
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1CRL"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 418..429
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 431..440
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:1CRL"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:1CRL"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 466..472
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 484..492
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:1TRH"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:1CRL"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 534..541
FT /evidence="ECO:0007829|PDB:1CRL"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:1CRL"
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
