GenomeNet

Database: UniProt
Entry: P17573
LinkDB: P17573
Original site: P17573 
ID   LIP1_GEOCN              Reviewed;         563 AA.
AC   P17573; Q00882; Q00883; Q00884; Q00886; Q02176; Q96WW8;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   19-FEB-2014, entry version 82.
DE   RecName: Full=Lipase 1;
DE            EC=3.1.1.3;
DE   AltName: Full=GCL I;
DE   AltName: Full=Lipase I;
DE   Flags: Precursor;
GN   Name=LIP1;
OS   Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae;
OC   mitosporic Dipodascaceae; Geotrichum.
OX   NCBI_TaxID=27317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 34614;
RX   PubMed=2481674;
RA   Shimada Y., Sugihara A., Tominaga Y., Iizumi T., Tsunasawa S.;
RT   "cDNA molecular cloning of Geotrichum candidum lipase.";
RL   J. Biochem. 106:383-388(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 20-563.
RC   STRAIN=ATCC 34614, ATCC 74169 / NRRL Y-552 / ED00652,
RC   ATCC 90287 / NRRL Y-553, and NRCC 205002;
RX   PubMed=8306978; DOI=10.1111/j.1432-1033.1994.tb19921.x;
RA   Bertolini M.C., Laramee L., Thomas D.Y., Cygler M., Schrag J.D.,
RA   Vernet T.;
RT   "Polymorphism in the lipase genes of Geotrichum candidum strains.";
RL   Eur. J. Biochem. 219:119-125(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 1-30 AND 551-563.
RC   STRAIN=ATCC 34614;
RX   PubMed=8370674;
RA   Nagao T., Shimada Y., Sugihara A., Tominaga Y.;
RT   "Cloning and sequencing of two chromosomal lipase genes from
RT   Geotrichum candidum.";
RL   J. Biochem. 113:776-780(1993).
RN   [4]
RP   SIMILARITY TO CARBOXYLESTERASES.
RX   PubMed=2115773;
RA   Slabas A.R., Windust J., Sidebottom C.M.;
RT   "Does sequence similarity of human choline esterase, Torpedo
RT   acetylcholine esterase and Geotrichum candidum lipase reveal the
RT   active site serine residue?";
RL   Biochem. J. 269:279-280(1990).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=7737187; DOI=10.1111/j.1432-1033.1995.0863m.x;
RA   Bertolini M.C., Schrag J.D., Cygler M., Ziomek E., Thomas D.Y.,
RA   Vernet T.;
RT   "Expression and characterization of Geotrichum candidum lipase I gene.
RT   Comparison of specificity profile with lipase II.";
RL   Eur. J. Biochem. 228:863-869(1995).
CC   -!- FUNCTION: Hydrolyzes all ester bonds in triglyceride and displays
CC       a high affinity for triolein. For unsaturated substrates having
CC       long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-
CC       12, cis-15) GCL I shows higher specific activity than GCL II,
CC       whereas GCL II shows higher specific activity against saturated
CC       substrates having short fatty acid chains (C8, C10, C12 and C14).
CC   -!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
CC       carboxylate.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U02622; AAA03435.1; -; Unassigned_DNA.
DR   EMBL; U02387; AAA03425.1; -; Unassigned_DNA.
DR   EMBL; U02524; AAA03428.1; -; Unassigned_DNA.
DR   EMBL; U02525; AAA03429.1; -; Unassigned_DNA.
DR   EMBL; S65081; AAB28106.1; -; Genomic_DNA.
DR   EMBL; S65082; AAB28107.1; -; Genomic_DNA.
DR   PIR; PN0492; ACGUGC.
DR   PIR; S41090; S41090.
DR   PIR; S41091; S41091.
DR   PIR; S41092; S41092.
DR   PIR; S41093; S41093.
DR   ProteinModelPortal; P17573; -.
DR   SMR; P17573; 20-563.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   Pfam; PF00135; COesterase; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Pyrrolidone carboxylic acid;
KW   Secreted; Signal.
FT   SIGNAL        1     19
FT   CHAIN        20    563       Lipase 1.
FT                                /FTId=PRO_0000008624.
FT   ACT_SITE    236    236       Acyl-ester intermediate (By similarity).
FT   ACT_SITE    373    373       Charge relay system (By similarity).
FT   ACT_SITE    482    482       Charge relay system (By similarity).
FT   MOD_RES      20     20       Pyrrolidone carboxylic acid.
FT   CARBOHYD    302    302       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    383    383       N-linked (GlcNAc...) (Potential).
FT   DISULFID     80    124
FT   DISULFID    295    307
FT   VARIANT      37     37       E -> G (in strain: NRRL Y-553).
FT   VARIANT      91     91       L -> W (in strain: NRRL Y-553).
FT   VARIANT     102    102       I -> L (in strain: NRCC 205002 and NRRL
FT                                Y-553).
FT   VARIANT     201    201       N -> S (in strain: NRCC 205002).
FT   VARIANT     259    259       Q -> K (in strain: NRRL Y-553).
FT   VARIANT     297    297       A -> T (in strain: NRCC 205002).
FT   VARIANT     300    300       G -> S (in strain: NRCC 205002 and NRRL
FT                                Y-553).
FT   VARIANT     303    303       E -> D (in strain: NRCC 205002).
FT   VARIANT     400    400       E -> Q (in strain: NRCC 205002).
FT   VARIANT     405    405       S -> P (in strain: NRRL Y-552).
FT   VARIANT     421    421       A -> S (in strain: NRCC 205002).
FT   VARIANT     520    520       K -> Q (in strain: NRCC 205002).
FT   VARIANT     528    528       S -> A (in strain: NRCC 205002, NRRL Y-
FT                                552 and NRRL Y-553).
FT   VARIANT     538    538       I -> V (in strain: NRRL Y-553).
FT   CONFLICT    170    170       V -> L (in Ref. 1; AA sequence).
FT   CONFLICT    492    496       VDLGP -> AGPWS (in Ref. 1; AA sequence).
SQ   SEQUENCE   563 AA;  61199 MW;  732E43AE060BB95F CRC64;
     MVSKTFFLAA ALNVVGTLAQ APTAVLNGNE VISGVLEGKV DTFKGIPFAD PPVGDLRFKH
     PQPFTGSYQG LKANDFSSAC MQLDPGNAIS LLDKVVGLGK IIPDNLRGPL YDMAQGSVSM
     NEDCLYLNVF RPAGTKPDAK LPVMVWIYGG AFVFGSSASY PGNGYVKESV EMGQPVVFVS
     INYRTGPYGF LGGDAITAEG NTNAGLHDQR KGLEWVSDNI ANFGGDPDKV MIFGESAGAM
     SVAHQLVAYG GDNTYNGKQL FHSAILQSGG PLPYFDSTSV GPESAYSRFA QYAGCDASAG
     DNETLACLRS KSSDVLHSAQ NSYDLKDLFG LLPQFLGFGP RPDGNIIPDA AYELYRSGRY
     AKVPYITGNQ EDEGTILAPV AINATTTPHV KKWLKYICSE ASDASLDRVL SLYPGSWSEG
     APFRTGILNA LTPQFKRIAA IFTDLLFQSP RRVMLNATKD VNRWTYLATQ LHNLVPFLGT
     FHGSDLLFQY YVDLGPSSAY RRYFISFANH HDPNVGTNLK QWDMYTDSGK EMLQIHMIGN
     SMRTDDFRIE GISNFESDVT LFG
//
DBGET integrated database retrieval system