FITM2_PIG
ID FITM2_PIG Reviewed; 262 AA.
AC B2LYG4;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang J., Yang G.-Y., Li H.-J., Wang Y.-L., Zhao W.-D., Wang W.-J.;
RL Submitted (MAR-2008) 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 such as oleoyl-CoA/(9Z)-octadecenoyl-CoA
CC and arachidonoyl-CoA/(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA in the
CC endoplasmic reticulum (ER) lumen (By similarity). 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 (By similarity). Directly
CC binds to diacylglycerol (DAGs) and triacylglycerol, which is also
CC important for LD biogenesis (By similarity). May support directional
CC budding of nacent LDs from the ER into the cytosol by reducing DAG
CC levels at sites of LD formation (By similarity). Plays a role in the
CC regulation of cell morphology and cytoskeletal organization (By
CC similarity). {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 -!- 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 Evidence={ECO:0000255|HAMAP-Rule:MF_03230};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65565;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03230};
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; Evidence={ECO:0000255|HAMAP-Rule:MF_03230};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65569;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03230};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03230};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50033;
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; EU596460; ACC59091.1; -; mRNA.
DR RefSeq; NP_001121932.1; NM_001128460.1.
DR AlphaFoldDB; B2LYG4; -.
DR STRING; 9823.ENSSSCP00000007854; -.
DR PaxDb; B2LYG4; -.
DR Ensembl; ENSSSCT00015104822; ENSSSCP00015043865; ENSSSCG00015077492.
DR Ensembl; ENSSSCT00025082983; ENSSSCP00025036066; ENSSSCG00025060557.
DR Ensembl; ENSSSCT00030040070; ENSSSCP00030018405; ENSSSCG00030028631.
DR Ensembl; ENSSSCT00035105881; ENSSSCP00035045538; ENSSSCG00035077582.
DR Ensembl; ENSSSCT00045067506; ENSSSCP00045047944; ENSSSCG00045038859.
DR Ensembl; ENSSSCT00050002210; ENSSSCP00050000666; ENSSSCG00050001772.
DR Ensembl; ENSSSCT00055016045; ENSSSCP00055012618; ENSSSCG00055008224.
DR Ensembl; ENSSSCT00060010789; ENSSSCP00060003967; ENSSSCG00060008430.
DR Ensembl; ENSSSCT00065098993; ENSSSCP00065043426; ENSSSCG00065072019.
DR GeneID; 100158013; -.
DR KEGG; ssc:100158013; -.
DR CTD; 128486; -.
DR eggNOG; KOG3750; Eukaryota.
DR HOGENOM; CLU_049499_1_1_1; -.
DR InParanoid; B2LYG4; -.
DR OrthoDB; 1621925at2759; -.
DR Reactome; R-SSC-8964572; Lipid particle organization.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
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:0035356; P:cellular triglyceride homeostasis; 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:0034389; P:lipid droplet organization; ISS:UniProtKB.
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 GO; GO:0010890; P:positive regulation of sequestering of triglyceride; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0010866; P:regulation of triglyceride biosynthetic process; 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..262
FT /note="Acyl-coenzyme A diphosphatase FITM2"
FT /id="PRO_0000350633"
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..145
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..218
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 155
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03230"
FT ACT_SITE 214
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03230"
SQ SEQUENCE 262 AA; 29633 MW; 08D26B5227213DAA CRC64;
MEHLERCAWV LRGTLVRAAV RRYLPWALAA SMLAGSLLKE LSPLPESYLS NKRNVLNVYF
VKVAWAWTFC LLLPFIALTN YHLTGKAGLV LRRLSTLLVG TAIWYVCTAI FSNVEHYTGS
CYQSPALEGV RNEPLSKQQC HGQGGFWHGF DISGHSFLLT FCALMIVEEM AVLHEVKTDR
SHCLHVAITA LVVALGFLTF IWVWMFLCTA VYFHNLSQKV FGTLFGLLGW YGTYGFWYLK
SFSPGLPPQS CSSNLKQDSY KR
