YFT2_YEAST
ID YFT2_YEAST Reviewed; 274 AA.
AC Q06676; D6VSV0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Acyl-coenzyme A diphosphatase YFT2 {ECO:0000255|HAMAP-Rule:MF_03232};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_03232};
DE AltName: Full=FIT family protein YFT2 {ECO:0000255|HAMAP-Rule:MF_03232, ECO:0000303|PubMed:26504167};
GN Name=YFT2 {ECO:0000255|HAMAP-Rule:MF_03232, ECO:0000312|SGD:S000002727};
GN Synonyms=FIT2A {ECO:0000255|HAMAP-Rule:MF_03232,
GN ECO:0000312|EMBL:DAA12160.1};
GN OrderedLocusNames=YDR319C {ECO:0000312|EMBL:DAA12160.1};
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26504167; DOI=10.1083/jcb.201505067;
RA Choudhary V., Ojha N., Golden A., Prinz W.A.;
RT "A conserved family of proteins facilitates nascent lipid droplet budding
RT from the ER.";
RL J. Cell Biol. 211:261-271(2015).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-178 AND GLU-243.
RX PubMed=29417057; DOI=10.15698/mic2018.02.614;
RA Hayes M., Choudhary V., Ojha N., Shin J.J., Han G.S., Carman G.M.,
RA Loewen C.J., Prinz W.A., Levine T.;
RT "Fat storage-inducing transmembrane (FIT or FITM) proteins are related to
RT lipid phosphatase/phosphotransferase enzymes.";
RL Microb. Cell 5:88-103(2017).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29526591; DOI=10.1016/j.cub.2018.02.020;
RA Choudhary V., Golani G., Joshi A.S., Cottier S., Schneiter R., Prinz W.A.,
RA Kozlov M.M.;
RT "Architecture of lipid droplets in endoplasmic reticulum is determined by
RT phospholipid intrinsic curvature.";
RL Curr. Biol. 28:915-926(2018).
CC -!- FUNCTION: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes
CC fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-
CC bisphosphate (By similarity). Preferentially hydrolyzes unsaturated
CC long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen
CC (By similarity). This catalytic activity is required for maintaining ER
CC structure and for lipid droplets (LDs) biogenesis, which are lipid
CC storage organelles involved in maintaining lipid and energy homeostasis
CC (PubMed:26504167) (By similarity). May directly bind to diacylglycerol
CC (DAGs) and triacylglycerol, which is also important for LD biogenesis
CC (By similarity). May support directional budding of nacent LDs from the
CC ER into the cytosol by reducing DAG levels at sites of LD formation
CC (PubMed:29526591) (By similarity). May play a role in the regulation of
CC cell morphology and cytoskeletal organization (By similarity). Involved
CC in phospholipid biosynthesis (PubMed:29417057) (By similarity).
CC {ECO:0000250|UniProtKB:P59266, ECO:0000250|UniProtKB:Q8N6M3,
CC ECO:0000255|HAMAP-Rule:MF_03232, ECO:0000269|PubMed:26504167,
CC ECO:0000269|PubMed:29417057, ECO:0000269|PubMed:29526591}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + H2O = adenosine 3',5'-bisphosphate + an acyl-4'-
CC phosphopantetheine + 2 H(+); Xref=Rhea:RHEA:50044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58342, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:132023; Evidence={ECO:0000255|HAMAP-Rule:MF_03232};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50045;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03232};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2
CC H(+) + S-(9Z-octadecenoyl)-4'-phosphopantetheine;
CC Xref=Rhea:RHEA:65564, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:58343, ChEBI:CHEBI:156553;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03232};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65565;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03232};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = adenosine 3',5'-
CC bisphosphate + 2 H(+) + S-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-4'-
CC phosphopantetheine; Xref=Rhea:RHEA:65568, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57368, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:156554; Evidence={ECO:0000255|HAMAP-Rule:MF_03232};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65569;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03232};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+)
CC + S-hexadecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50032,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132018; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03232};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03232};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03232, ECO:0000269|PubMed:26504167,
CC ECO:0000269|PubMed:29526591}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03232}. Vacuole
CC {ECO:0000269|PubMed:29417057}. Note=Enriched at sites of lipid droplet
CC (LD) biogenesis. {ECO:0000269|PubMed:29526591}.
CC -!- SIMILARITY: Belongs to the FIT family. Yeast FIT2A/YFT2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03232}.
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DR EMBL; U32517; AAB64755.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12160.1; -; Genomic_DNA.
DR PIR; S59785; S59785.
DR RefSeq; NP_010605.1; NM_001180627.1.
DR AlphaFoldDB; Q06676; -.
DR SMR; Q06676; -.
DR BioGRID; 32375; 57.
DR DIP; DIP-4731N; -.
DR IntAct; Q06676; 1.
DR STRING; 4932.YDR319C; -.
DR PaxDb; Q06676; -.
DR PRIDE; Q06676; -.
DR EnsemblFungi; YDR319C_mRNA; YDR319C; YDR319C.
DR GeneID; 851917; -.
DR KEGG; sce:YDR319C; -.
DR SGD; S000002727; YFT2.
DR VEuPathDB; FungiDB:YDR319C; -.
DR eggNOG; KOG3750; Eukaryota.
DR GeneTree; ENSGT00530000063693; -.
DR HOGENOM; CLU_086757_0_0_1; -.
DR InParanoid; Q06676; -.
DR OMA; LILWCEL; -.
DR BioCyc; YEAST:G3O-29877-MON; -.
DR Reactome; R-SCE-8964572; Lipid particle organization.
DR PRO; PR:Q06676; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06676; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IMP:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; ISS:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR GO; GO:1900481; P:negative regulation of diacylglycerol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:SGD.
DR GO; GO:1900480; P:regulation of diacylglycerol biosynthetic process; IMP:UniProtKB.
DR HAMAP; MF_03232; YFT2; 1.
DR InterPro; IPR019388; FIT.
DR InterPro; IPR046398; YFT2.
DR PANTHER; PTHR23129; PTHR23129; 1.
DR Pfam; PF10261; Scs3p; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..274
FT /note="Acyl-coenzyme A diphosphatase YFT2"
FT /id="PRO_0000252273"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..60
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..170
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..247
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 178
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03232"
FT ACT_SITE 239
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03232"
FT MUTAGEN 178
FT /note="H->A: Inositol auxotrophy. Impaired ER morphology
FT and aberrant lipid droplet (LD) budding."
FT /evidence="ECO:0000269|PubMed:29417057"
FT MUTAGEN 243
FT /note="E->A: Inositol auxotrophy. Impaired ER morphology
FT and aberrant lipid droplet (LD) budding."
FT /evidence="ECO:0000269|PubMed:29417057"
FT MUTAGEN 243
FT /note="E->D: No defect in inositol biosynthesis."
FT /evidence="ECO:0000269|PubMed:29417057"
SQ SEQUENCE 274 AA; 32011 MW; 8E63022F4DCC5530 CRC64;
MIRQLNYWSR KAYLIYPFQV FVGALLSIVV SSETLNHQKE TCALLKSSNI FNVIFAYKAN
QLWPFLFFSL AFLQIYFHYL ARMDILPLPI SSTETSSSYL TYTNHWPLLK NRIISIMITQ
YACKFVLKYL LLFLNFQFID HVFIWTGGEC SSGSKTTSAE KCRLENGKWD GGFDISGHFC
FLVSISMILW MELHLFSRFV QAEDMFWVVN KWVRACLAIV CAVLVIWICI LWVTAIYYHT
ILEKVLGCLM GFICPVFIYH ILPKIGILHN YLYL
