LIP1_GEOCN
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 25-MAY-2022, entry version 102.
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; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061;
RN [1]
RP NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 34614;
RX PubMed=2481674; DOI=10.1093/oxfordjournals.jbchem.a122862;
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., 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, AND PYROGLUTAMATE FORMATION AT
RP GLN-20.
RC STRAIN=ATCC 34614;
RX PubMed=8370674; DOI=10.1093/oxfordjournals.jbchem.a124117;
RA Nagao T., Shimada Y., Sugihara A., Tominaga Y.;
RT "Cloning and sequencing of two chromosomal lipase genes from Geotrichum
RT candidum.";
RL J. Biochem. 113:776-780(1993).
RN [4]
RP SIMILARITY TO CARBOXYLESTERASES.
RX PubMed=2115773; DOI=10.1042/bj2690279;
RA Slabas A.R., Windust J., Sidebottom C.M.;
RT "Does sequence similarity of human choline esterase, Torpedo acetylcholine
RT esterase and Geotrichum candidum lipase reveal the active site serine
RT 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., 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 a
CC high affinity for triolein. For unsaturated substrates having long
CC fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15)
CC GCL I shows higher specific activity than GCL II, whereas GCL II shows
CC higher specific activity against saturated substrates having short
CC fatty acid chains (C8, C10, C12 and C14).
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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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 AlphaFoldDB; P17573; -.
DR SMR; P17573; -.
DR ESTHER; geoca-1lipa; Fungal_carboxylesterase_lipase.
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 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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Pyrrolidone carboxylic acid; Secreted;
KW Signal.
FT SIGNAL 1..19
FT CHAIN 20..563
FT /note="Lipase 1"
FT /id="PRO_0000008624"
FT ACT_SITE 236
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 373
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 482
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2481674"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..124
FT DISULFID 295..307
FT VARIANT 37
FT /note="E -> G (in strain: NRRL Y-553)"
FT VARIANT 91
FT /note="L -> W (in strain: NRRL Y-553)"
FT VARIANT 102
FT /note="I -> L (in strain: NRCC 205002 and NRRL Y-553)"
FT VARIANT 201
FT /note="N -> S (in strain: NRCC 205002)"
FT VARIANT 259
FT /note="Q -> K (in strain: NRRL Y-553)"
FT VARIANT 297
FT /note="A -> T (in strain: NRCC 205002)"
FT VARIANT 300
FT /note="G -> S (in strain: NRCC 205002 and NRRL Y-553)"
FT VARIANT 303
FT /note="E -> D (in strain: NRCC 205002)"
FT VARIANT 400
FT /note="E -> Q (in strain: NRCC 205002)"
FT VARIANT 405
FT /note="S -> P (in strain: NRRL Y-552)"
FT VARIANT 421
FT /note="A -> S (in strain: NRCC 205002)"
FT VARIANT 520
FT /note="K -> Q (in strain: NRCC 205002)"
FT VARIANT 528
FT /note="S -> A (in strain: NRCC 205002, NRRL Y-552 and NRRL
FT Y-553)"
FT VARIANT 538
FT /note="I -> V (in strain: NRRL Y-553)"
FT CONFLICT 170
FT /note="V -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 492..496
FT /note="VDLGP -> AGPWS (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
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
