AC   MF_03232;
DC   Protein; auto
TR   HAMAP; MF_03232; -; 1; level=0
XX
Names: YFT2
XX
ID   YFT2
case <FTGroup:1>
DE   RecName: Full=Acyl-coenzyme A diphosphatase YFT2;
DE            EC=3.6.1.-;
DE   AltName: Full=FIT family protein YFT2;
else
ID   YFT2
DE   RecName: Full=Acyl-coenzyme A diphosphatase YFT2 homolog;
DE   AltName: Full=FIT family protein YFT2 homolog;
end case
GN   Name=YFT2; Synonyms=FIT2A;
XX
case <FTGroup:1>
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. Preferentially hydrolyzes unsaturated long-chain acyl-CoA
CC       substrates in the endoplasmic reticulum (ER) lumen. This catalytic
CC       activity is required for maintaining ER structure and for lipid
CC       droplets (LDs) biogenesis, which are lipid storage organelles involved
CC       in maintaining lipid and energy homeostasis. May directly bind to
CC       diacylglycerol (DAGs) and triacylglycerol, which is also important for
CC       LD biogenesis. May support directional budding of nacent LDs from the
CC       ER into the cytosol by reducing DAG levels at sites of LD formation.
CC       May play a role in the regulation of cell morphology and cytoskeletal
CC       organization). Involved in phospholipid biosynthesis.
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;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50045;
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       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65565;
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;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65569;
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;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50033;
else
CC   -!- FUNCTION: May hydrolyze
CC       fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-
CC       bisphosphate. May be required for maintaining ER structure and for lipid
CC       droplets (LDs) biogenesis, which are lipid storage organelles involved
CC       in maintaining lipid and energy homeostasis.
end case
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the FIT family. Yeast FIT2A/YFT2 subfamily.
XX
DR   Pfam; PF10261; Scs3p; 1; trigger=no
DR   General; Transmembrane; -; 4-6; trigger=no
XX
case <FTGroup:1>
KW   Hydrolase
KW   Lipid biosynthesis
KW   Phospholipid biosynthesis
KW   Phospholipid metabolism
end case
KW   Endoplasmic reticulum
KW   Membrane
KW   Transmembrane
KW   Transmembrane helix
XX
case <FTGroup:1>
GO   GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
end case
GO   GO:0005789; C:endoplasmic reticulum membrane
GO   GO:0140042; P:lipid droplet formation
XX
FT   From: YFT2_YEAST (Q06676)
FT   ACT_SITE        178
FT   Group: 1; Condition: H
FT   ACT_SITE        239
FT   Group: 1; Condition: H
XX
Size: 255-330;
Related: None;
Template: Q06676;
Scope:
 Eukaryota; Saccharomycetales
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.3 2021/05/20
//