FITM1_PIG
ID FITM1_PIG Reviewed; 290 AA.
AC B2MVP8;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Fat storage-inducing transmembrane protein 1 {ECO:0000250|UniProtKB:A5D6W6, ECO:0000255|HAMAP-Rule:MF_03229};
DE AltName: Full=Fat-inducing protein 1 {ECO:0000255|HAMAP-Rule:MF_03229};
GN Name=FITM1 {ECO:0000255|HAMAP-Rule:MF_03229};
GN Synonyms=FIT1 {ECO:0000255|HAMAP-Rule:MF_03229};
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.,
RA Zhang Z.-Q., Tai Y.-L., Wu Y.-X., Zang M.;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the formation of lipid droplets
CC (LDs) which are storage organelles at the center of lipid and energy
CC homeostasis (By similarity). Directly binds to diacylglycerol (DAGs)
CC and triacylglycerol (By similarity). {ECO:0000255|HAMAP-Rule:MF_03229}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03229}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03229}.
CC -!- SIMILARITY: Belongs to the FIT family. FIT1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03229}.
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DR EMBL; EU625275; ACC85691.1; -; mRNA.
DR RefSeq; NP_001121942.1; NM_001128470.1.
DR AlphaFoldDB; B2MVP8; -.
DR STRING; 9823.ENSSSCP00000002194; -.
DR PaxDb; B2MVP8; -.
DR PRIDE; B2MVP8; -.
DR GeneID; 100147706; -.
DR KEGG; ssc:100147706; -.
DR CTD; 161247; -.
DR eggNOG; KOG3750; Eukaryota.
DR InParanoid; B2MVP8; -.
DR OrthoDB; 1621925at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0019992; F:diacylglycerol binding; ISS:UniProtKB.
DR GO; GO:0017129; F:triglyceride binding; ISS:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_03229; FITM1; 1.
DR HAMAP; MF_03230; FITM2; 1.
DR InterPro; IPR019388; FIT.
DR InterPro; IPR046402; FIT1.
DR InterPro; IPR046401; FITM1/2.
DR PANTHER; PTHR23129; PTHR23129; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..290
FT /note="Fat storage-inducing transmembrane protein 1"
FT /id="PRO_0000350630"
FT TOPO_DOM 1..18
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..94
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..187
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..249
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 186
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03229"
FT ACT_SITE 244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03229"
FT SITE 248
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03229"
SQ SEQUENCE 290 AA; 32164 MW; B5514CCA1E9AD36E CRC64;
MERGPVVGAG LGARARIRTL LGCLVKVLLW VASALLYFGS EQAARLLGSP CLRRLYHAWL
AAVVIFGPLL QFHVNPRTIF ASHGNFFNIK FVNSAWGWTC TFLGGFVLLV VFLATRRVAV
TARHLSRLVV GAAVWRGAGR AFLLIEDLTG SCFEPLPQGL LLHELPDRRS RLAAGHQWRG
YTVSSHTFLL TFCCLLMAEE AAVFAKYLAH GLPAGAPLRL VFLLNVLLLG LWNFLLLCTV
IYFHQYTHKV VGAAVGTFAW YLTYGSWYHQ PWSPGSPGHG LFTHPSRKHN
