FITM2_XENLA
ID FITM2_XENLA Reviewed; 260 AA.
AC Q6AX73;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 54.
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};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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}.
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; BC079727; AAH79727.1; -; mRNA.
DR RefSeq; NP_001087401.1; NM_001093932.1.
DR AlphaFoldDB; Q6AX73; -.
DR SMR; Q6AX73; -.
DR GeneID; 447225; -.
DR CTD; 447225; -.
DR Xenbase; XB-GENE-950537; fitm2.L.
DR OrthoDB; 1621925at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 447225; Expressed in muscle tissue and 18 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0036115; P:fatty-acyl-CoA catabolic process; ISS:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..260
FT /note="Acyl-coenzyme A diphosphatase FITM2"
FT /id="PRO_0000319572"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..57
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..144
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 154
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03230"
FT ACT_SITE 212
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03230"
SQ SEQUENCE 260 AA; 30565 MW; 1C00505E69CEE144 CRC64;
MERLENCAQM FQRKFLNEAF RRHCPVLLAC IALGGSLLKE LSPLPDSYWN NKRNVLNVYF
VKFCWGWTLW LLLPFITLTN YKLTGSITKV LRRLSSLLVG TLFWYLCTNL FLYIEHITGS
CYESEALLDS IEHQDRKECR LHGGFWHGFD ISGHCFLLSY CILIILEETS VIRSIQFERH
WHRMAINAQF TALSILVIIW VWMFLCTAVY FHNIFQKVIG TAFGMLAWYI TYRWWYLQPI
SPGLPPASAS HSEKEPVYKN
