GUP1_YEAST
ID GUP1_YEAST Reviewed; 560 AA.
AC P53154; D6VU60;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Membrane-bound O-acyltransferase GUP1 {ECO:0000305};
DE AltName: Full=Glycerol uptake protein 1;
GN Name=GUP1; OrderedLocusNames=YGL084C;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=10747858; DOI=10.1074/jbc.c000144200;
RA Oelkers P., Tinkelenberg A., Erdeniz N., Cromley D., Billheimer J.T.,
RA Sturley S.L.;
RT "A lecithin cholesterol acyltransferase-like gene mediates diacylglycerol
RT esterification in yeast.";
RL J. Biol. Chem. 275:15609-15612(2000).
RN [5]
RP FUNCTION.
RX PubMed=10931309; DOI=10.1046/j.1365-2958.2000.01968.x;
RA Holst B., Lunde C., Lages F., Oliveira R., Lucas C., Kielland-Brandt M.C.;
RT "GUP1 and its close homologue GUP2, encoding multimembrane-spanning
RT proteins involved in active glycerol uptake in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 37:108-124(2000).
RN [6]
RP FUNCTION.
RX PubMed=10694878; DOI=10.1016/s0968-0004(99)01539-x;
RA Hofmann K.;
RT "A superfamily of membrane-bound O-acyltransferases with implications for
RT wnt signaling.";
RL Trends Biochem. Sci. 25:111-112(2000).
RN [7]
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 [8]
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 [9]
RP INDUCTION.
RX PubMed=15278288; DOI=10.1007/s00294-004-0519-3;
RA Oliveira R., Lucas C.;
RT "Expression studies of GUP1 and GUP2, genes involved in glycerol active
RT transport in Saccharomyces cerevisiae, using semi-quantitative RT-PCR.";
RL Curr. Genet. 46:140-146(2004).
RN [10]
RP FUNCTION.
RX PubMed=15381122; DOI=10.1016/j.femsyr.2004.06.012;
RA Neves L., Oliveira R., Lucas C.;
RT "Yeast orthologues associated with glycerol transport and metabolism.";
RL FEMS Yeast Res. 5:51-62(2004).
RN [11]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=15813700; DOI=10.1042/bj20042045;
RA Bleve G., Zacheo G., Cappello M.S., Dellaglio F., Grieco F.;
RT "Subcellular localization and functional expression of the glycerol uptake
RT protein 1 (GUP1) of Saccharomyces cerevisiae tagged with green fluorescent
RT protein.";
RL Biochem. J. 390:145-155(2005).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=17042752; DOI=10.1111/j.1567-1364.2006.00110.x;
RA Ferreira C., Silva S., van Voorst F., Aguiar C., Kielland-Brandt M.C.,
RA Brandt A., Lucas C.;
RT "Absence of Gup1p in Saccharomyces cerevisiae results in defective cell
RT wall composition, assembly, stability and morphology.";
RL FEMS Yeast Res. 6:1027-1038(2006).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF HIS-447.
RX PubMed=16597698; DOI=10.1091/mbc.e06-02-0104;
RA Bosson R., Jaquenoud M., Conzelmann A.;
RT "GUP1 of Saccharomyces cerevisiae encodes an O-acyltransferase involved in
RT remodeling of the GPI anchor.";
RL Mol. Biol. Cell 17:2636-2645(2006).
RN [14]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18786505; DOI=10.1016/j.bbamem.2008.08.011;
RA Ferreira C., Lucas C.;
RT "The yeast O-acyltransferase Gup1p interferes in lipid metabolism with
RT direct consequences on the sphingolipid-sterol-ordered domains
RT integrity/assembly.";
RL Biochim. Biophys. Acta 1778:2648-2653(2008).
RN [16]
RP FUNCTION.
RX PubMed=18036137; DOI=10.1111/j.1365-2958.2007.06043.x;
RA Jaquenoud M., Pagac M., Signorell A., Benghezal M., Jelk J., Buetikofer P.,
RA Conzelmann A.;
RT "The Gup1 homologue of Trypanosoma brucei is a GPI
RT glycosylphosphatidylinositol remodelase.";
RL Mol. Microbiol. 67:202-212(2008).
RN [17]
RP TOPOLOGY.
RX PubMed=21849510; DOI=10.1074/jbc.m111.256511;
RA Pagac M., de la Mora H.V., Duperrex C., Roubaty C., Vionnet C.,
RA Conzelmann A.;
RT "Topology of 1-acyl-sn-glycerol-3-phosphate acyltransferases SLC1 and ALE1
RT and related membrane-bound O-acyltransferases (MBOATs) of Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 286:36438-36447(2011).
RN [18]
RP FUNCTION.
RX PubMed=22617017; DOI=10.1186/1471-2180-12-80;
RA Tulha J., Faria-Oliveira F., Lucas C., Ferreira C.;
RT "Programmed cell death in Saccharomyces cerevisiae is hampered by the
RT deletion of GUP1 gene.";
RL BMC Microbiol. 12:80-80(2012).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP FUNCTION.
RX PubMed=25589358; DOI=10.1002/jobm.201400781;
RA Faria-Oliveira F., Carvalho J., Belmiro C.L., Ramalho G., Pavao M.,
RA Lucas C., Ferreira C.;
RT "Elemental biochemical analysis of the polysaccharides in the extracellular
RT matrix of the yeast Saccharomyces cerevisiae.";
RL J. Basic Microbiol. 55:685-694(2015).
RN [21]
RP INTERACTION WITH POR1, AND SUBCELLULAR LOCATION.
RX PubMed=30184078; DOI=10.1093/femsyr/foy097;
RA Tulha J., Lucas C.;
RT "Saccharomyces cerevisiae mitochondrial Por1/yVDAC1 (voltage-dependent
RT anion channel 1) interacts physically with the MBOAT O-acyltransferase
RT Gup1/HHATL in the control of cell wall integrity and programmed cell
RT death.";
RL FEMS Yeast Res. 18:0-0(2018).
CC -!- FUNCTION: Membrane-bound O-acyltransferase involved in the remodeling
CC of glycosylphosphatidylinositol (GPI) anchors. Acts only on GPI-
CC anchored proteins, but not on free GPI lipids. Acts as an
CC acyltransferase for GPI anchors that adds C26 fatty acids to the sn2
CC position of lyso-PI-containing GPI anchors. PER1 first deacylates, GUP1
CC subsequently reacylates the anchor lipid, thus replacing a shorter
CC fatty acid (C16:0 or C18:0) by C26:0 (PubMed:16597698,
CC PubMed:18036137). Also involved in lipid metabolism, having profound
CC effects on sphingolipid-sterol-ordered domains integrity and assembly
CC (PubMed:18786505). Together with GUP2, has an influence on the chemical
CC composition of the yeast extracellular matrix (yECM) in yeast
CC multicellular aggregates, such as biofilms and colonies
CC (PubMed:25589358). Involved in cell integrity and apoptosis
CC (PubMed:22617017, PubMed:30184078). {ECO:0000269|PubMed:16597698,
CC ECO:0000269|PubMed:18036137, ECO:0000269|PubMed:18786505,
CC ECO:0000269|PubMed:22617017, ECO:0000269|PubMed:25589358,
CC ECO:0000269|PubMed:30184078}.
CC -!- SUBUNIT: Interacts with mitochondrial outer membrane voltage-dependent
CC anion channel (VDAC) POR1. {ECO:0000269|PubMed:30184078}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15813700};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15813700};
CC Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000269|PubMed:30184078}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expressed constitutively. {ECO:0000269|PubMed:15278288}.
CC -!- DISRUPTION PHENOTYPE: Results in an increase in triglyceride (TG)
CC synthesis with a concomitant decrease in phospholipid (PL) synthesis
CC and exhibits an altered plasma membrane lipid composition
CC (PubMed:10747858). Shows defects in cell wall assembly and stability
CC and abnormal cell wall morphology (PubMed:17042752). Deficient in GPI
CC anchor remodeling, mutant cells only contain the primary, unremodeled
CC phosphatidylinositol (PI) and are unable to attach remodeled PI or
CC ceramides to the anchor (PubMed:16597698). Defective in sterol lipid
CC distribution (PubMed:18786505). {ECO:0000269|PubMed:10747858,
CC ECO:0000269|PubMed:16597698, ECO:0000269|PubMed:17042752,
CC ECO:0000269|PubMed:18786505}.
CC -!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originaly thought to be involved in active uptake of
CC glycerol driven by electrogenic proton symport (PubMed:10931309), but
CC has later been shown to be an acyltransferase and that effects on
CC glycerol transport may be indirect (PubMed:10694878, PubMed:15381122).
CC {ECO:0000305|PubMed:10694878, ECO:0000305|PubMed:10931309,
CC ECO:0000305|PubMed:15381122}.
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DR EMBL; Z72606; CAA96789.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08021.1; -; Genomic_DNA.
DR PIR; S64091; S64091.
DR RefSeq; NP_011431.1; NM_001180949.1.
DR AlphaFoldDB; P53154; -.
DR SMR; P53154; -.
DR BioGRID; 33166; 504.
DR DIP; DIP-4367N; -.
DR IntAct; P53154; 1.
DR MINT; P53154; -.
DR STRING; 4932.YGL084C; -.
DR TCDB; 2.A.50.1.1; the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family.
DR iPTMnet; P53154; -.
DR MaxQB; P53154; -.
DR PaxDb; P53154; -.
DR PRIDE; P53154; -.
DR EnsemblFungi; YGL084C_mRNA; YGL084C; YGL084C.
DR GeneID; 852796; -.
DR KEGG; sce:YGL084C; -.
DR SGD; S000003052; GUP1.
DR VEuPathDB; FungiDB:YGL084C; -.
DR eggNOG; KOG3860; Eukaryota.
DR GeneTree; ENSGT00530000063629; -.
DR HOGENOM; CLU_021430_1_1_1; -.
DR InParanoid; P53154; -.
DR OMA; ATWIFNI; -.
DR BioCyc; YEAST:G3O-30585-MON; -.
DR PRO; PR:P53154; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53154; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008374; F:O-acyltransferase activity; IMP:SGD.
DR GO; GO:0019563; P:glycerol catabolic process; IMP:SGD.
DR GO; GO:0015793; P:glycerol transmembrane transport; IMP:SGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Membrane; Mitochondrion;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..560
FT /note="Membrane-bound O-acyltransferase GUP1"
FT /id="PRO_0000213132"
FT TOPO_DOM 1..43
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:21849510,
FT ECO:0000305|PubMed:15813700, ECO:0000305|PubMed:16847258"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..131
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..276
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..352
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..526
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258,
FT ECO:0000269|PubMed:21849510, ECO:0000305|PubMed:15813700"
FT ACT_SITE 447
FT /evidence="ECO:0000305|PubMed:16597698"
FT MUTAGEN 447
FT /note="H->A: Deficient in GPI anchor remodeling."
FT /evidence="ECO:0000269|PubMed:16597698"
SQ SEQUENCE 560 AA; 65340 MW; F8E9017D3E856A35 CRC64;
MSLISILSPL ITSEGLDSRI KPSPKKDAST TTKPSLWKTT EFKFYYIAFL VVVPLMFYAG
LQASSPENPN YARYERLLSQ GWLFGRKVDN SDSQYRFFRD NFALLSVLML VHTSIKRIVL
YSTNITKLRF DLIFGLIFLV AAHGVNSIRI LAHMLILYAI AHVLKNFRRI ATISIWIYGI
STLFINDNFR AYPFGNICSF LSPLDHWYRG IIPRWDVFFN FTLLRVLSYN LDFLERWENL
QKKKSPSYES KEAKSAILLN ERARLTAAHP IQDYSLMNYI AYVTYTPLFI AGPIITFNDY
VYQSKHTLPS INFKFIFYYA VRFVIALLSM EFILHFLHVV AISKTKAWEN DTPFQISMIG
LFNLNIIWLK LLIPWRLFRL WALLDGIDTP ENMIRCVDNN YSSLAFWRAW HRSYNKWVVR
YIYIPLGGSK NRVLTSLAVF SFVAIWHDIE LKLLLWGWLI VLFLLPEIFA TQIFSHYTDA
VWYRHVCAVG AVFNIWVMMI ANLFGFCLGS DGTKKLLSDM FCTVSGFKFV ILASVSLFIA
VQIMFEIREE EKRHGIYLKC
