FITM1_HUMAN
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 03-AUG-2022, entry version 99.
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, 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; A5D6W6; -.
DR PeptideAtlas; A5D6W6; -.
DR PRIDE; A5D6W6; -.
DR ProteomicsDB; 707; -. [A5D6W6-1]
DR Antibodypedia; 8923; 40 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 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; 1621925at2759; -.
DR PhylomeDB; A5D6W6; -.
DR PathwayCommons; A5D6W6; -.
DR Reactome; R-HSA-8964572; Lipid particle organization.
DR BioGRID-ORCS; 161247; 15 hits in 1068 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 tissues.
DR Genevisible; A5D6W6; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:BHF-UCL.
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; 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; PTHR23129; 1.
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
