CST26_YEAST
ID CST26_YEAST Reviewed; 397 AA.
AC P38226; D6VQ42;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=2-acyl-1-lysophosphatidylinositol acyltransferase {ECO:0000303|PubMed:19796168};
DE EC=2.3.-.-;
DE AltName: Full=Acyl-CoA:lyso-PI acyltransferase {ECO:0000303|PubMed:27462707};
DE AltName: Full=Chromosome stability protein 26 {ECO:0000303|PubMed:10454593};
DE AltName: Full=Phosphatidylinositol stearoyl incorporating protein 1 {ECO:0000303|PubMed:19796168};
GN Name=CST26 {ECO:0000303|PubMed:10454593};
GN Synonyms=PSI1 {ECO:0000303|PubMed:19796168}; OrderedLocusNames=YBR042C;
GN ORFNames=YBR0412;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
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 IDENTIFICATION, AND FUNCTION.
RX PubMed=10454593; DOI=10.1093/nar/27.15.3001;
RA Ouspenski I.I., Elledge S.J., Brinkley B.R.;
RT "New yeast genes important for chromosome integrity and segregation
RT identified by dosage effects on genome stability.";
RL Nucleic Acids Res. 27:3001-3008(1999).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15716577; DOI=10.1074/mcp.m400123-mcp200;
RA Natter K., Leitner P., Faschinger A., Wolinski H., McCraith S., Fields S.,
RA Kohlwein S.D.;
RT "The spatial organization of lipid synthesis in the yeast Saccharomyces
RT cerevisiae derived from large scale green fluorescent protein tagging and
RT high resolution microscopy.";
RL Mol. Cell. Proteomics 4:662-672(2005).
RN [7]
RP FUNCTION.
RX PubMed=19796168; DOI=10.1111/j.1742-4658.2009.07355.x;
RA Le Guedard M., Bessoule J.J., Boyer V., Ayciriex S., Velours G., Kulik W.,
RA Ejsing C.S., Shevchenko A., Coulon D., Lessire R., Testet E.;
RT "PSI1 is responsible for the stearic acid enrichment that is characteristic
RT of phosphatidylinositol in yeast.";
RL FEBS J. 276:6412-6424(2009).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=20694142; DOI=10.1371/journal.pone.0011956;
RA Shui G., Guan X.L., Gopalakrishnan P., Xue Y., Goh J.S., Yang H.,
RA Wenk M.R.;
RT "Characterization of substrate preference for Slc1p and Cst26p in
RT Saccharomyces cerevisiae using lipidomic approaches and an LPAAT activity
RT assay.";
RL PLoS ONE 5:e11956-e11956(2010).
RN [9]
RP FUNCTION.
RX PubMed=22323296; DOI=10.1091/mbc.e11-07-0624;
RA De Smet C.H., Vittone E., Scherer M., Houweling M., Liebisch G.,
RA Brouwers J.F., de Kroon A.I.;
RT "The yeast acyltransferase Sct1p regulates fatty acid desaturation by
RT competing with the desaturase Ole1p.";
RL Mol. Biol. Cell 23:1146-1156(2012).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26711260; DOI=10.1128/mcb.00843-15;
RA Doignon F., Laquel P., Testet E., Tuphile K., Fouillen L., Bessoule J.J.;
RT "Requirement of phosphoinositides containing stearic acid to control cell
RT polarity.";
RL Mol. Cell. Biol. 36:765-780(2016).
RN [11]
RP FUNCTION.
RX PubMed=27462707; DOI=10.1371/journal.pgen.1006160;
RA Vazquez H.M., Vionnet C., Roubaty C., Mallela S.K., Schneiter R.,
RA Conzelmann A.;
RT "Chemogenetic E-MAP in Saccharomyces cerevisiae for identification of
RT membrane transporters operating lipid flip flop.";
RL PLoS Genet. 12:e1006160-e1006160(2016).
CC -!- FUNCTION: Acyltransferase with lysophosphatidic acid acyltransferase
CC (LPAAT) activity. Fatty acyl substrates include 18:0-acyl-CoA, 16:0-
CC acyl-CoA, 17:0-acyl-CoA and 14:0-acyl-CoA (PubMed:20694142).
CC Responsible for the acyl-CoA-dependent introduction of saturated very
CC long chain fatty acids (VLCFAs) into phosphatidylinositol, transferring
CC saturated FAs with 18 to 26 carbon atoms (PubMed:27462707). Responsible
CC for the incorporation of stearate into phosphatidylinositol
CC (PubMed:19796168, PubMed:26711260). Overexpression has an effect on
CC chromosome stability (PubMed:10454593). Regulates phosphorylation and
CC expression of glycerol-3-phosphate acyltransferase SCT1
CC (PubMed:22323296). {ECO:0000269|PubMed:10454593,
CC ECO:0000269|PubMed:19796168, ECO:0000269|PubMed:20694142,
CC ECO:0000269|PubMed:22323296, ECO:0000269|PubMed:26711260,
CC ECO:0000269|PubMed:27462707}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-heptadecanoyl-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-
CC heptadecanoyl-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:44392, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:74554, ChEBI:CHEBI:84429;
CC Evidence={ECO:0000269|PubMed:20694142};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44393;
CC Evidence={ECO:0000305|PubMed:20694142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-heptadecanoyl-sn-glycero-3-phosphate + tetradecanoyl-CoA =
CC 1-heptadecanoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:44388, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:74554, ChEBI:CHEBI:84428;
CC Evidence={ECO:0000269|PubMed:20694142};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44389;
CC Evidence={ECO:0000305|PubMed:20694142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-heptadecanoyl-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-
CC heptadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:44396, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74554, ChEBI:CHEBI:84430;
CC Evidence={ECO:0000269|PubMed:20694142};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44397;
CC Evidence={ECO:0000305|PubMed:20694142};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14562106, ECO:0000269|PubMed:20694142}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Phosphoinositides (PIPs) with stearic acyl chains
CC are strongly disturbed. Induces disturbances in intracellular
CC trafficking, alterations in the budding pattern and defects in actin
CC cytoskeleton organization. {ECO:0000269|PubMed:26711260}.
CC -!- MISCELLANEOUS: Present with 2010 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; Z35911; CAA84984.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07162.1; -; Genomic_DNA.
DR PIR; S45900; S45900.
DR RefSeq; NP_009598.1; NM_001178390.1.
DR AlphaFoldDB; P38226; -.
DR BioGRID; 32743; 70.
DR DIP; DIP-5358N; -.
DR IntAct; P38226; 1.
DR MINT; P38226; -.
DR STRING; 4932.YBR042C; -.
DR SwissLipids; SLP:000000080; -.
DR MaxQB; P38226; -.
DR PaxDb; P38226; -.
DR PRIDE; P38226; -.
DR EnsemblFungi; YBR042C_mRNA; YBR042C; YBR042C.
DR GeneID; 852330; -.
DR KEGG; sce:YBR042C; -.
DR SGD; S000000246; CST26.
DR VEuPathDB; FungiDB:YBR042C; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_041844_3_2_1; -.
DR InParanoid; P38226; -.
DR OMA; YGQDFYT; -.
DR BioCyc; YEAST:G3O-29015-MON; -.
DR Reactome; R-SCE-1482798; Acyl chain remodeling of CL.
DR Reactome; R-SCE-1482925; Acyl chain remodelling of PG.
DR Reactome; R-SCE-1483166; Synthesis of PA.
DR PRO; PR:P38226; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38226; protein.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; HDA:SGD.
DR GO; GO:0016746; F:acyltransferase activity; IMP:SGD.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; IMP:SGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..397
FT /note="2-acyl-1-lysophosphatidylinositol acyltransferase"
FT /id="PRO_0000208207"
FT MOTIF 112..117
FT /note="HXXXXD motif"
SQ SEQUENCE 397 AA; 45515 MW; 04CADDD1247D98A8 CRC64;
MLHQKIAHKV RKVVVPGISL LIFFQGCLIL LFLQLTYKTL YCRNDIRKQI GLNKTKRLFI
VLVSSILHVV APSAVRITTE NSSVPKGTFF LDLKKKRILS HLKSNSVAIC NHQIYTDWIF
LWWLAYTSNL GANVFIILKK SLASIPILGF GMRNYNFIFM SRKWAQDKIT LSNSLAGLDS
NARGAGSLAG KSPERITEEG ESIWNPEVID PKQIHWPYNL ILFPEGTNLS ADTRQKSAKY
AAKIGKKPFK NVLLPHSTGL RYSLQKLKPS IESLYDITIG YSGVKQEEYG ELIYGLKSIF
LEGKYPKLVD IHIRAFDVKD IPLEDENEFS EWLYKIWSEK DALMERYYST GSFVSDPETN
HSVTDSFKIN RIELTEVLIL PTLTIIWLVY KLYCFIF
