FITM1_MOUSE
ID FITM1_MOUSE Reviewed; 292 AA.
AC Q91V79; Q80ZL0; Q8CI63; Q9CTD0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Fat storage-inducing transmembrane protein 1 {ECO:0000255|HAMAP-Rule:MF_03229, ECO:0000303|PubMed:30923760};
DE AltName: Full=Fat-inducing protein 1 {ECO:0000255|HAMAP-Rule:MF_03229};
GN Name=Fitm1 {ECO:0000255|HAMAP-Rule:MF_03229, ECO:0000312|MGI:MGI:1915930};
GN Synonyms=Fit1 {ECO:0000255|HAMAP-Rule:MF_03229};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ; TISSUE=Lung;
RX PubMed=11345588; DOI=10.1007/s002510100308;
RA Yawata M., Murata S., Tanaka K., Ishigatsubo Y., Kasahara M.;
RT "Nucleotide sequence analysis of the ~35-kb segment containing interferon-
RT gamma-inducible mouse proteasome activator genes.";
RL Immunogenetics 53:119-129(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Liver, and Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22106267; DOI=10.1073/pnas.1110817108;
RA Gross D.A., Zhan C., Silver D.L.;
RT "Direct binding of triglyceride to fat storage-inducing transmembrane
RT proteins 1 and 2 is important for lipid droplet formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19581-19586(2011).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=30923760; DOI=10.1016/j.heliyon.2019.e01292;
RA Nishihama N., Nagayama T., Makino S., Koishi R.;
RT "Mice lacking fat storage-inducing transmembrane protein 2 show improved
RT profiles upon pressure overload-induced heart failure.";
RL Heliyon 5:e01292-e01292(2019).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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, PubMed:22106267) (By similarity).
CC Directly binds to diacylglycerol (DAGs) and triacylglycerol
CC (PubMed:22106267) (By similarity). {ECO:0000255|HAMAP-Rule:MF_03229,
CC ECO:0000269|PubMed:18160536, ECO:0000269|PubMed:22106267}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03229, ECO:0000269|PubMed:18160536,
CC ECO:0000269|PubMed:22106267}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03229}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and at
CC lower levels in the heart (at protein level). In the heart, mRNA
CC expression levels do not correlate well with protein levels, suggesting
CC post-transcriptional regulation in this organ.
CC {ECO:0000269|PubMed:18160536}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice show no significant differences in
CC heart size or function. {ECO:0000269|PubMed:30923760}.
CC -!- SIMILARITY: Belongs to the FIT family. FIT1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03229}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB053120; BAB47402.1; -; Genomic_DNA.
DR EMBL; AB054000; BAB47400.1; -; mRNA.
DR EMBL; BC037188; AAH37188.1; ALT_INIT; mRNA.
DR EMBL; BC048823; AAH48823.1; -; mRNA.
DR EMBL; BC104408; AAI04409.1; -; mRNA.
DR EMBL; BC104409; AAI04410.1; -; mRNA.
DR EMBL; AK003939; BAB23085.1; -; mRNA.
DR CCDS; CCDS27116.1; -.
DR RefSeq; NP_081084.1; NM_026808.1.
DR AlphaFoldDB; Q91V79; -.
DR IntAct; Q91V79; 1.
DR STRING; 10090.ENSMUSP00000022826; -.
DR iPTMnet; Q91V79; -.
DR PhosphoSitePlus; Q91V79; -.
DR PaxDb; Q91V79; -.
DR PRIDE; Q91V79; -.
DR ProteomicsDB; 266850; -.
DR Antibodypedia; 8923; 40 antibodies from 15 providers.
DR DNASU; 68680; -.
DR Ensembl; ENSMUST00000022826; ENSMUSP00000022826; ENSMUSG00000022215.
DR GeneID; 68680; -.
DR KEGG; mmu:68680; -.
DR UCSC; uc007tzc.1; mouse.
DR CTD; 161247; -.
DR MGI; MGI:1915930; Fitm1.
DR VEuPathDB; HostDB:ENSMUSG00000022215; -.
DR eggNOG; KOG3750; Eukaryota.
DR GeneTree; ENSGT00530000063693; -.
DR HOGENOM; CLU_049499_2_0_1; -.
DR InParanoid; Q91V79; -.
DR OMA; GWTCIFT; -.
DR OrthoDB; 1621925at2759; -.
DR PhylomeDB; Q91V79; -.
DR Reactome; R-MMU-8964572; Lipid particle organization.
DR BioGRID-ORCS; 68680; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Picalm; mouse.
DR PRO; PR:Q91V79; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q91V79; protein.
DR Bgee; ENSMUSG00000022215; Expressed in hindlimb stylopod muscle and 80 other tissues.
DR Genevisible; Q91V79; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:BHF-UCL.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0019992; F:diacylglycerol binding; IDA:UniProtKB.
DR GO; GO:0017129; F:triglyceride binding; IDA:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; IDA:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IDA: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; IDA: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 1: Evidence at protein 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_0000319576"
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; 32280 MW; 786133E48C9B227A CRC64;
MERGPTVGAG LGAGTRVRAL LGCLVKVLLW VASALLYFGS EQAARLLGSP CLRRLYHAWL
AAVVIFGPLL QFHVNSRTIF ASHGNFFNIK FVNSAWGWTC TFLGGFVLLV VFLATRRVAV
TARHLSRLVV GAAVWRGAGR AFLLIEDLTG SCFEPLPQGL LLHELPDRKS CLAAGHQWRG
YTVSSHTFLL TFCCLLMAEE AAVFAKYLAH GLPAGAPLRL VFLLNVLLLG LWNFLLLCTV
IYFHQYTHKV VGAAVGTFAW YLTYGSWYHQ PWSPGIPGHG LFPRSRSMRK HN
