FITM2_CAEEL
ID FITM2_CAEEL Reviewed; 283 AA.
AC Q5CZ37;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Acyl-coenzyme A diphosphatase FITM2 {ECO:0000255|HAMAP-Rule:MF_03230};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_03230};
DE AltName: Full=FIT family protein fitm-2 {ECO:0000312|WormBase:ZK265.9};
DE AltName: Full=Fat storage-inducing transmembrane homolog 2 {ECO:0000312|WormBase:ZK265.9};
DE AltName: Full=Fat storage-inducing transmembrane protein 2 {ECO:0000255|HAMAP-Rule:MF_03230};
DE AltName: Full=Fat-inducing protein 2 {ECO:0000255|HAMAP-Rule:MF_03230};
GN Name=fitm-2 {ECO:0000312|WormBase:ZK265.9};
GN Synonyms=fit2 {ECO:0000255|HAMAP-Rule:MF_03230},
GN fitm2 {ECO:0000255|HAMAP-Rule:MF_03230};
GN ORFNames=ZK265.9 {ECO:0000312|WormBase:ZK265.9};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
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).
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 (By
CC similarity). May play a role in the regulation of cell morphology, ER
CC morphology and cytoskeletal organization (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_03230, ECO:0000269|PubMed:26504167}.
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_03230};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50045;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03230};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03230}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03230}.
CC -!- SIMILARITY: Belongs to the FIT family. FIT2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03230}.
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DR EMBL; Z81143; CAI58649.1; -; Genomic_DNA.
DR RefSeq; NP_001021865.1; NM_001026694.3.
DR AlphaFoldDB; Q5CZ37; -.
DR STRING; 6239.ZK265.9; -.
DR EPD; Q5CZ37; -.
DR PaxDb; Q5CZ37; -.
DR PeptideAtlas; Q5CZ37; -.
DR EnsemblMetazoa; ZK265.9.1; ZK265.9.1; WBGene00044094.
DR GeneID; 3565961; -.
DR KEGG; cel:CELE_ZK265.9; -.
DR UCSC; ZK265.9; c. elegans.
DR CTD; 3565961; -.
DR WormBase; ZK265.9; CE38132; WBGene00044094; fitm-2.
DR eggNOG; KOG3750; Eukaryota.
DR GeneTree; ENSGT00530000063693; -.
DR HOGENOM; CLU_049499_0_0_1; -.
DR InParanoid; Q5CZ37; -.
DR OMA; ERCAWFL; -.
DR OrthoDB; 1621925at2759; -.
DR PhylomeDB; Q5CZ37; -.
DR Reactome; R-CEL-8964572; Lipid particle organization.
DR PRO; PR:Q5CZ37; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00044094; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0010945; F:CoA pyrophosphatase activity; ISS:UniProtKB.
DR GO; GO:0036115; P:fatty-acyl-CoA catabolic process; 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:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_03230; FITM2; 1.
DR InterPro; IPR019388; FIT.
DR InterPro; IPR046401; FITM1/2.
DR PANTHER; PTHR23129; PTHR23129; 1.
DR Pfam; PF10261; Scs3p; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..283
FT /note="Acyl-coenzyme A diphosphatase FITM2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000350635"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..81
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..168
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03230"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03230"
SQ SEQUENCE 283 AA; 32680 MW; 31ED12DB48B87EBF CRC64;
MSTRRSSTRA DSTTKRPASP NSTPNAALGI FVAIARQILF IDARKVALFY LAFVTVLSFI
ESRIELDSTY YLVQKHSVLN QYGVKMGWFW TLVIVGPFIW FSSKAHNRRD RDQPIVDVCR
LGVGTACWYF SVQFFHKVLA LTSMCDKGRT LTRAQCSEKE GVWTPGYDIS GHCFLMIYSI
LIITEEAIAY RHYQQVTDAV HQMDGDREEH DRLTRCIQYF FVAMLFLHAF WFKQIIISVL
YYHIFIEEIL GAVAAVVCWF VTYRMLYPAG FLASPIRRTV GRK
