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Database: UniProt
Entry: P20261
LinkDB: P20261
Original site: P20261 
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   11-JUN-2014, entry version 80.
DE   RecName: Full=Lipase 1;
DE            EC=3.1.1.3;
DE   Flags: Precursor;
GN   Name=LIP1;
OS   Candida rugosa (Yeast) (Candida cylindracea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   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   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   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;
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   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   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.
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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   ProteinModelPortal; P20261; -.
DR   SMR; P20261; 16-549.
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       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   STRAND       26     28
FT   STRAND       33     42
FT   HELIX        49     51
FT   HELIX        84     86
FT   HELIX        88     97
FT   HELIX       100    105
FT   STRAND      106    108
FT   STRAND      114    119
FT   STRAND      129    135
FT   TURN        139    141
FT   HELIX       145    147
FT   HELIX       151    159
FT   STRAND      165    169
FT   HELIX       174    178
FT   HELIX       182    187
FT   HELIX       192    207
FT   HELIX       208    211
FT   STRAND      213    223
FT   HELIX       225    235
FT   HELIX       236    239
FT   STRAND      246    248
FT   STRAND      250    256
FT   HELIX       268    281
FT   HELIX       289    295
FT   HELIX       298    306
FT   TURN        314    317
FT   STRAND      327    330
FT   HELIX       334    339
FT   STRAND      348    353
FT   HELIX       358    361
FT   HELIX       362    364
FT   HELIX       370    380
FT   HELIX       386    395
FT   HELIX       400    402
FT   STRAND      403    405
FT   TURN        409    412
FT   STRAND      414    417
FT   HELIX       418    429
FT   HELIX       431    440
FT   STRAND      446    451
FT   TURN        453    456
FT   TURN        458    460
FT   STRAND      461    463
FT   HELIX       466    472
FT   HELIX       479    482
FT   HELIX       484    492
FT   HELIX       495    498
FT   STRAND      512    514
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
//
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