AC   MF_03230;
DC   Protein; auto
TR   HAMAP; MF_03230; -; 1; level=0
XX
Names: FITM2
XX
ID   FITM2
case <FTGroup:1>
DE   RecName: Full=Acyl-coenzyme A diphosphatase FITM2;
DE            EC=3.6.1.-;
DE   AltName: Full=Fat storage-inducing transmembrane protein 2;
DE   AltName: Full=Fat-inducing protein 2;
else
DE   RecName: Full=Acyl-coenzyme A diphosphatase FITM2 homolog;
DE   AltName: Full=Fat storage-inducing transmembrane protein 2 homolog;
DE   AltName: Full=FITM2-like protein;
end case
GN   Name=FITM2; Synonyms=FIT2;
XX
case <FTGroup:1> and <OC:Mammalia>
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 such as oleoyl-CoA/(9Z)-octadecenoyl-CoA and arachidonoyl-
CC       CoA/(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA in the endoplasmic reticulum
CC       (ER) lumen. 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
CC       homeostasis. Directly binds to diacylglycerol (DAGs) and
CC       triacylglycerol, which is also important for LD biogenesis. May support
CC       directional budding of nacent LDs from the ER into the cytosol by
CC       reducing DAG levels at sites of LD formation. Plays a role in the
CC       regulation of cell morphology and cytoskeletal organization.
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 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, ER morphology and
CC       cytoskeletal organization.
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;
else
CC   -!- FUNCTION: May hydrolyze fatty acyl-CoA to yield acyl-4'-
CC       phosphopantetheine and adenosine 3',5'-bisphosphate. May be required
CC       for maintaining ER structure and for lipid droplets (LDs) biogenesis,
CC       which are lipid storage organelles involved in maintaining lipid and
CC       energy homeostasis.
end case
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the FIT family. FIT2 subfamily.
XX
DR   Pfam; PF10261; Scs3p; 1-2; trigger=no
DR   General; Transmembrane; -; 0-6; trigger=no
XX
case <FTGroup:1>
KW   Hydrolase
KW   Lipid 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: FITM2_HUMAN (Q8N6M3)
FT   ACT_SITE        155
FT   Group: 1; Condition: H
FT   ACT_SITE        214
FT   Group: 1; Condition: H
XX
Size: 252-448;
Related: None;
Template: Q8N6M3;
Scope:
 Eukaryota; Bilateria
Fusion:
 Nter: None
 Cter: None
Duplicate: in BRAFL
Plasmid: None
Comments: None
XX
# Revision 1.3 2021/05/20
//