FITM2_DANRE
ID FITM2_DANRE Reviewed; 252 AA.
AC Q52KL1; A8KBW3;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=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=fitm2 {ECO:0000255|HAMAP-Rule:MF_03230};
GN Synonyms=fit2 {ECO:0000255|HAMAP-Rule:MF_03230}; ORFNames=zgc:110840;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18160536; DOI=10.1073/pnas.0708579105;
RA Kadereit B., Kumar P., Wang W.-J., Miranda D., Snapp E.L., Severina N.,
RA Torregroza I., Evans T., Silver D.L.;
RT "Evolutionarily conserved gene family important for fat storage.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:94-99(2008).
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:18160536) (By similarity). Required for lipid droplet
CC accumulation in liver and intestine during embryogenesis
CC (PubMed:18160536). May directly bind to diacylglycerol (DAGs) and
CC triacylglycerol, which is also important for LD biogenesis (By
CC similarity). May support directional budding of nacent LDs from the ER
CC 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:18160536}.
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 -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18160536}.
CC -!- SIMILARITY: Belongs to the FIT family. FIT2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03230}.
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DR EMBL; BC094293; AAH94293.1; -; mRNA.
DR EMBL; BC154267; AAI54268.1; -; mRNA.
DR RefSeq; NP_001018334.1; NM_001020498.1.
DR AlphaFoldDB; Q52KL1; -.
DR STRING; 7955.ENSDARP00000041832; -.
DR PaxDb; Q52KL1; -.
DR GeneID; 552928; -.
DR KEGG; dre:552928; -.
DR CTD; 128486; -.
DR ZFIN; ZDB-GENE-050508-5; fitm2.
DR eggNOG; KOG3750; Eukaryota.
DR InParanoid; Q52KL1; -.
DR OrthoDB; 1621925at2759; -.
DR PhylomeDB; Q52KL1; -.
DR Reactome; R-DRE-8964572; Lipid particle organization.
DR PRO; PR:Q52KL1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0019992; F:diacylglycerol binding; ISS:UniProtKB.
DR GO; GO:0017129; F:triglyceride binding; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0031018; P:endocrine pancreas development; IMP:ZFIN.
DR GO; GO:0036115; P:fatty-acyl-CoA catabolic process; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IMP:ZFIN.
DR GO; GO:0140042; P:lipid droplet formation; ISS: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; IMP:ZFIN.
DR GO; GO:1990798; P:pancreas regeneration; IMP:ZFIN.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0003323; P:type B pancreatic cell development; IMP:ZFIN.
DR HAMAP; MF_03230; FITM2; 1.
DR InterPro; IPR019388; FIT.
DR InterPro; IPR046401; FITM1/2.
DR PANTHER; PTHR23129; PTHR23129; 1.
DR Pfam; PF10261; Scs3p; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..252
FT /note="Acyl-coenzyme A diphosphatase FITM2"
FT /id="PRO_0000350634"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..59
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..156
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..223
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 156
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03230"
FT ACT_SITE 212
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03230"
FT CONFLICT 237
FT /note="V -> L (in Ref. 1; AAI54268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 252 AA; 28972 MW; B9269BAA1596C5A5 CRC64;
MAAAVAGSLV DKLVCLWRQP YTRIYLPHLF FCISLVGSVL KNAELVPESY FSSSRNVLNL
YFVKVSWGWT IVLLLPFIAY SNFYIKSHMF ALRRLTSLLV ATLVWYICTE TFFYIEDITG
SCYESNTMVV IRGEFDTKAA CRKAGFFWDG FDISGHSFIL SYSSLVIMEE MVPMLHIQPA
YRNPPLDCLY LALNVIVAIW IWMFGCTSVY FHDIIDKILG TSCGILGWYM TYKVWYVKLF
SPGLPPQPKQ HT
