LIH1_YEAST
ID LIH1_YEAST Reviewed; 328 AA.
AC P47145; D6VWS6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Putative lipase LIH1 {ECO:0000303|PubMed:26580812};
DE EC=3.1.1.3 {ECO:0000305|PubMed:26580812};
DE AltName: Full=Lipase homolog 1 {ECO:0000303|PubMed:26580812};
GN Name=LIH1 {ECO:0000303|PubMed:26580812}; OrderedLocusNames=YJR107W;
GN ORFNames=J1983;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 14 AND 66.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=26580812; DOI=10.1371/journal.pone.0143096;
RA Meunchan M., Michely S., Devillers H., Nicaud J.M., Marty A.,
RA Neuveglise C.;
RT "Comprehensive analysis of a yeast lipase family in the Yarrowia clade.";
RL PLoS ONE 10:e0143096-e0143096(2015).
CC -!- FUNCTION: Lipases catalyze the hydrolysis of the ester bond of tri-,
CC di- and monoglycerides of long-chain fatty acids into fatty acids and
CC glycerol. {ECO:0000305|PubMed:26580812}.
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 Evidence={ECO:0000305|PubMed:26580812};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:26580812};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; Z49607; CAA89637.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08892.2; -; Genomic_DNA.
DR PIR; S57128; S57128.
DR RefSeq; NP_012641.2; NM_001181765.2.
DR AlphaFoldDB; P47145; -.
DR SMR; P47145; -.
DR BioGRID; 33863; 73.
DR STRING; 4932.YJR107W; -.
DR ESTHER; yeast-yj77; Lipase_3.
DR PaxDb; P47145; -.
DR PRIDE; P47145; -.
DR EnsemblFungi; YJR107W_mRNA; YJR107W; YJR107W.
DR GeneID; 853571; -.
DR KEGG; sce:YJR107W; -.
DR SGD; S000003868; LIH1.
DR VEuPathDB; FungiDB:YJR107W; -.
DR eggNOG; KOG4569; Eukaryota.
DR GeneTree; ENSGT00940000171519; -.
DR HOGENOM; CLU_032957_3_0_1; -.
DR InParanoid; P47145; -.
DR OMA; LHMYEHR; -.
DR PRO; PR:P47145; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47145; protein.
DR GO; GO:0016298; F:lipase activity; ISS:SGD.
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; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome.
FT CHAIN 1..328
FT /note="Putative lipase LIH1"
FT /id="PRO_0000090374"
FT ACT_SITE 181
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O59952"
FT ACT_SITE 253
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O59952"
FT ACT_SITE 315
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O59952"
FT CONFLICT 14
FT /note="P -> L (in Ref. 1; CAA89637)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="G -> P (in Ref. 1; CAA89637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 37205 MW; 56233E0C6DC7F089 CRC64;
MPVVHCSSNL PITPYIYERL VYFIKASSIS SCISDNLLLV NKTFNDGGCP PHINFCNDEI
INPTAGQTVV ELVLNAKKGE LGSGYLAVDH GKKVVILAFR GSTTRQDWFS DFEIYPVNYS
PLCVKEYRKL IEEGKIRECE GCKMHRGFLR FTETLGMDVF KKMESILESF PEYRIVVTGH
SLGAALASLA GIELKIRGFD PLVLTFATPK IFNSEMKQWV DELFETDAIE KESILKDEIQ
FRKGYFRVVH TGDYIPMVPP FYHPAGLEMF INKVGLPQNA EDIEYRGKNN RLTLKDGFRE
GMSGLVEDWL HVYEHRAYFI DVVGCSGL
