ID   FITM1_HUMAN             Reviewed;         292 AA.
AC   A5D6W6; Q8IUQ7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   RecName: Full=Fat storage-inducing transmembrane protein 1 {ECO:0000255|HAMAP-Rule:MF_03229, ECO:0000303|PubMed:18160536};
DE   AltName: Full=Fat-inducing protein 1 {ECO:0000255|HAMAP-Rule:MF_03229};
GN   Name=FITM1 {ECO:0000255|HAMAP-Rule:MF_03229,
GN   ECO:0000312|HGNC:HGNC:33714};
GN   Synonyms=FIT1 {ECO:0000255|HAMAP-Rule:MF_03229};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, 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: 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 (PubMed:18160536) (By similarity). Directly binds to
CC       diacylglycerol (DAGs) and triacylglycerol (By similarity).
CC       {ECO:0000255|HAMAP-Rule:MF_03229, ECO:0000269|PubMed:18160536}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03229, ECO:0000269|PubMed:18160536}; Multi-
CC       pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03229}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A5D6W6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A5D6W6-2; Sequence=VSP_031493;
CC   -!- TISSUE SPECIFICITY: Primarily expressed in heart and skeletal muscle.
CC       {ECO:0000269|PubMed:18160536}.
CC   -!- SIMILARITY: Belongs to the FIT family. FIT1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03229}.
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DR   EMBL; CH471078; EAW66107.1; -; Genomic_DNA.
DR   EMBL; BC042179; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC139911; AAI39912.1; -; mRNA.
DR   CCDS; CCDS9611.1; -. [A5D6W6-1]
DR   RefSeq; NP_981947.1; NM_203402.2. [A5D6W6-1]
DR   AlphaFoldDB; A5D6W6; -.
DR   BioGRID; 127777; 1.
DR   STRING; 9606.ENSP00000267426; -.
DR   iPTMnet; A5D6W6; -.
DR   PhosphoSitePlus; A5D6W6; -.
DR   BioMuta; FITM1; -.
DR   jPOST; A5D6W6; -.
DR   MassIVE; A5D6W6; -.
DR   PaxDb; 9606-ENSP00000267426; -.
DR   PeptideAtlas; A5D6W6; -.
DR   ProteomicsDB; 707; -. [A5D6W6-1]
DR   Antibodypedia; 8923; 44 antibodies from 15 providers.
DR   DNASU; 161247; -.
DR   Ensembl; ENST00000267426.6; ENSP00000267426.5; ENSG00000139914.7. [A5D6W6-1]
DR   Ensembl; ENST00000559294.1; ENSP00000453741.1; ENSG00000139914.7. [A5D6W6-2]
DR   Ensembl; ENST00000642380.1; ENSP00000493481.1; ENSG00000285321.1. [A5D6W6-2]
DR   Ensembl; ENST00000644407.1; ENSP00000493961.1; ENSG00000285321.1. [A5D6W6-1]
DR   GeneID; 161247; -.
DR   KEGG; hsa:161247; -.
DR   MANE-Select; ENST00000267426.6; ENSP00000267426.5; NM_203402.3; NP_981947.1.
DR   UCSC; uc001wmf.3; human. [A5D6W6-1]
DR   AGR; HGNC:33714; -.
DR   CTD; 161247; -.
DR   DisGeNET; 161247; -.
DR   GeneCards; FITM1; -.
DR   HGNC; HGNC:33714; FITM1.
DR   HPA; ENSG00000139914; Group enriched (heart muscle, skeletal muscle).
DR   MIM; 612028; gene.
DR   neXtProt; NX_A5D6W6; -.
DR   OpenTargets; ENSG00000139914; -.
DR   PharmGKB; PA165478932; -.
DR   VEuPathDB; HostDB:ENSG00000139914; -.
DR   eggNOG; KOG3750; Eukaryota.
DR   GeneTree; ENSGT00530000063693; -.
DR   HOGENOM; CLU_049499_2_0_1; -.
DR   InParanoid; A5D6W6; -.
DR   OMA; GWTCIFT; -.
DR   OrthoDB; 4210222at2759; -.
DR   PhylomeDB; A5D6W6; -.
DR   PathwayCommons; A5D6W6; -.
DR   Reactome; R-HSA-8964572; Lipid particle organization.
DR   BioGRID-ORCS; 161247; 16 hits in 1144 CRISPR screens.
DR   ChiTaRS; FITM1; human.
DR   GenomeRNAi; 161247; -.
DR   Pharos; A5D6W6; Tdark.
DR   PRO; PR:A5D6W6; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; A5D6W6; Protein.
DR   Bgee; ENSG00000139914; Expressed in hindlimb stylopod muscle and 92 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:BHF-UCL.
DR   GO; GO:0106399; F:acyl-coenzyme A diphosphatase activity; IEA:InterPro.
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; ISS:BHF-UCL.
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:BHF-UCL.
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:SF3; FAT STORAGE-INDUCING TRANSMEMBRANE PROTEIN 1; 1.
DR   PANTHER; PTHR23129; UNCHARACTERIZED; 1.
DR   Genevisible; A5D6W6; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..292
FT                   /note="Fat storage-inducing transmembrane protein 1"
FT                   /id="PRO_0000319575"
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"
FT   VAR_SEQ         1..196
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031493"
SQ   SEQUENCE   292 AA;  32207 MW;  5722083EB85EEDC8 CRC64;
     MERGPVVGAG LGAGARIQAL LGCLLKVLLW 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 LFPRPHSSRK HN
//