ID   FITM1_BOVIN             Reviewed;         292 AA.
AC   A7YWN2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Fat storage-inducing transmembrane protein 1 {ECO:0000250|UniProtKB:A5D6W6};
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) 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; BC134663; AAI34664.1; -; mRNA.
DR   RefSeq; NP_001098821.1; NM_001105351.2.
DR   AlphaFoldDB; A7YWN2; -.
DR   STRING; 9913.ENSBTAP00000028518; -.
DR   PaxDb; A7YWN2; -.
DR   PRIDE; A7YWN2; -.
DR   GeneID; 510040; -.
DR   KEGG; bta:510040; -.
DR   CTD; 161247; -.
DR   eggNOG; KOG3750; Eukaryota.
DR   HOGENOM; CLU_049499_2_0_1; -.
DR   InParanoid; A7YWN2; -.
DR   OrthoDB; 1621925at2759; -.
DR   Proteomes; UP000009136; 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..292
FT                   /note="Fat storage-inducing transmembrane protein 1"
FT                   /id="PRO_0000319574"
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..292
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   292 AA;  32253 MW;  2F2CBA8DAED84788 CRC64;
     MERGPVVGAG RGAGARIRAL LGGLVRVLLW VASALLYFGS EQAARLLGSP CLRRLYHAWL
     AAVVIFGPLL QFHVNPRTIF ASHGNFFNIK FVNSAWGWTC TFLGGFVLLV VFLATRRVAV
     TARHLSRLVV GAAVWRGAGR AFLLIEDLTG SCFEPLPQGL LLHELPDRRS CLAAGHQWRG
     YTVSSHTFLL TFCCLLMAEE AAVFAKYLAH GLPAGAPLRL VFLLNVLLLG LWNFLLLCTV
     IYFHQYTHKV VGAAVGTFAW YLTYGSWYHQ PWSPGSPGHG LFPRPHSIHK HN