IFM1_MOUSE
ID IFM1_MOUSE Reviewed; 106 AA.
AC Q9D103; Q8R2S7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Interferon-induced transmembrane protein 1 {ECO:0000305};
DE AltName: Full=Dispanin subfamily A member 2a;
DE Short=DSPA2a;
DE AltName: Full=Fragilis protein 2;
DE AltName: Full=Mouse ifitm-like protein 2;
DE Short=Mil-2;
GN Name=Ifitm1 {ECO:0000312|MGI:MGI:1915963};
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 [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=14516695; DOI=10.1016/s0925-4773(03)00126-6;
RA Tanaka S.S., Matsui Y.;
RT "Developmentally regulated expression of mil-1 and mil-2, mouse interferon-
RT induced transmembrane protein like genes, during formation and
RT differentiation of primordial germ cells.";
RL Mech. Dev. 119:S261-S267(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, Heart, Lung, 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 [5]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=12659663; DOI=10.1186/1471-213x-3-1;
RA Lange U.C., Saitou M., Western P.S., Barton S.C., Surani M.A.;
RT "The fragilis interferon-inducible gene family of transmembrane proteins is
RT associated with germ cell specification in mice.";
RL BMC Dev. Biol. 3:1-1(2003).
RN [6]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16326387; DOI=10.1016/j.devcel.2005.10.010;
RA Tanaka S.S., Yamaguchi Y.L., Tsoi B., Lickert H., Tam P.P.;
RT "IFITM/Mil/fragilis family proteins IFITM1 and IFITM3 play distinct roles
RT in mouse primordial germ cell homing and repulsion.";
RL Dev. Cell 9:745-756(2005).
RN [7]
RP FUNCTION.
RX PubMed=18505827; DOI=10.1128/mcb.00272-08;
RA Lange U.C., Adams D.J., Lee C., Barton S., Schneider R., Bradley A.,
RA Surani M.A.;
RT "Normal germ line establishment in mice carrying a deletion of the
RT Ifitm/Fragilis gene family cluster.";
RL Mol. Cell. Biol. 28:4688-4696(2008).
RN [8]
RP REVIEW.
RX PubMed=21166591; DOI=10.1089/jir.2010.0112;
RA Siegrist F., Ebeling M., Certa U.;
RT "The small interferon-induced transmembrane genes and proteins.";
RL J. Interferon Cytokine Res. 31:183-197(2011).
RN [9]
RP FUNCTION.
RX PubMed=21253575; DOI=10.1371/journal.ppat.1001258;
RA Huang I.C., Bailey C.C., Weyer J.L., Radoshitzky S.R., Becker M.M.,
RA Chiang J.J., Brass A.L., Ahmed A.A., Chi X., Dong L., Longobardi L.E.,
RA Boltz D., Kuhn J.H., Elledge S.J., Bavari S., Denison M.R., Choe H.,
RA Farzan M.;
RT "Distinct patterns of IFITM-mediated restriction of filoviruses, SARS
RT coronavirus, and influenza A virus.";
RL PLoS Pathog. 7:E1001258-E1001258(2011).
RN [10]
RP GENE FAMILY.
RX PubMed=22363774; DOI=10.1371/journal.pone.0031961;
RA Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.;
RT "The dispanins: a novel gene family of ancient origin that contains 14
RT human members.";
RL PLoS ONE 7:E31961-E31961(2012).
CC -!- FUNCTION: IFN-induced antiviral protein which inhibits the entry of
CC viruses to the host cell cytoplasm, permitting endocytosis, but
CC preventing subsequent viral fusion and release of viral contents into
CC the cytosol. Active against multiple viruses, including influenza A
CC virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus
CC (EBOV), Dengue virus (DNV) and West Nile virus (WNV). Can inhibit:
CC influenza virus hemagglutinin protein-mediated viral entry, MARV and
CC EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral
CC entry. Also implicated in cell adhesion and control of cell growth and
CC migration. Plays a key role in the antiproliferative action of IFN-
CC gamma either by inhibiting the ERK activation or by arresting cell
CC growth in G1 phase in a p53-dependent manner. Acts as a positive
CC regulator of osteoblast differentiation. {ECO:0000269|PubMed:18505827,
CC ECO:0000269|PubMed:21253575}.
CC -!- SUBUNIT: Interacts with CD81. Part of a complex composed of CD19,
CC CR2/CD21, CD81 and IFITM1/CD225 in the membrane of mature B-cells.
CC Interacts with CAV1; this interaction enhances the ability of CAV1 in
CC inhibiting ERK activation. {ECO:0000250|UniProtKB:P13164}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16326387};
CC Single-pass membrane protein {ECO:0000269|PubMed:16326387}. Lysosome
CC membrane {ECO:0000250|UniProtKB:P13164}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in nascent primordial germ
CC cells, as well as in gonadal germ cells. {ECO:0000269|PubMed:12659663}.
CC -!- DEVELOPMENTAL STAGE: In migrating PGCs, expression is first detected
CC during germ cell differentiation. {ECO:0000269|PubMed:14516695,
CC ECO:0000269|PubMed:16326387}.
CC -!- PTM: Palmitoylation on membrane-proximal cysteines controls clustering
CC in membrane compartments and antiviral activity.
CC {ECO:0000250|UniProtKB:P13164}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
CC -!- CAUTION: It has been previously shown that mediates migration of early
CC primordial germ cells (PGCs) (PubMed:16326387). But according to
CC PubMed:16326387, have no detectable effects on development of the germ
CC line or on the generation of live young, hence, is not essential for
CC PGC migration. {ECO:0000305|PubMed:16326387}.
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DR EMBL; AK004121; BAB23181.1; -; mRNA.
DR EMBL; AK169960; BAE41483.1; -; mRNA.
DR EMBL; CH466531; EDL17976.1; -; Genomic_DNA.
DR EMBL; BC027285; AAH27285.1; -; mRNA.
DR EMBL; BC090258; AAH90258.1; -; mRNA.
DR EMBL; BC090972; AAH90972.1; -; mRNA.
DR EMBL; BK001123; DAA01238.1; -; mRNA.
DR CCDS; CCDS21995.1; -.
DR RefSeq; NP_001106186.1; NM_001112715.1.
DR RefSeq; NP_081096.3; NM_026820.3.
DR RefSeq; XP_006536301.1; XM_006536238.1.
DR AlphaFoldDB; Q9D103; -.
DR DIP; DIP-60824N; -.
DR IntAct; Q9D103; 1.
DR STRING; 10090.ENSMUSP00000026564; -.
DR PhosphoSitePlus; Q9D103; -.
DR SwissPalm; Q9D103; -.
DR EPD; Q9D103; -.
DR MaxQB; Q9D103; -.
DR PaxDb; Q9D103; -.
DR PRIDE; Q9D103; -.
DR ProteomicsDB; 267279; -.
DR DNASU; 68713; -.
DR Ensembl; ENSMUST00000026564; ENSMUSP00000026564; ENSMUSG00000025491.
DR Ensembl; ENSMUST00000106040; ENSMUSP00000101655; ENSMUSG00000025491.
DR Ensembl; ENSMUST00000106042; ENSMUSP00000101657; ENSMUSG00000025491.
DR GeneID; 68713; -.
DR KEGG; mmu:68713; -.
DR UCSC; uc009kja.2; mouse.
DR CTD; 8519; -.
DR MGI; MGI:1915963; Ifitm1.
DR VEuPathDB; HostDB:ENSMUSG00000025491; -.
DR eggNOG; ENOG502S9XK; Eukaryota.
DR GeneTree; ENSGT00950000182857; -.
DR HOGENOM; CLU_124511_3_0_1; -.
DR InParanoid; Q9D103; -.
DR OMA; MLKEGHE; -.
DR OrthoDB; 1555189at2759; -.
DR PhylomeDB; Q9D103; -.
DR TreeFam; TF334894; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 68713; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ifitm1; mouse.
DR PRO; PR:Q9D103; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D103; protein.
DR Bgee; ENSMUSG00000025491; Expressed in conjunctival fornix and 234 other tissues.
DR Genevisible; Q9D103; MM.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0051607; P:defense response to virus; IDA:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0035455; P:response to interferon-alpha; ISS:UniProtKB.
DR GO; GO:0035456; P:response to interferon-beta; ISS:UniProtKB.
DR GO; GO:0034341; P:response to interferon-gamma; ISS:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR GO; GO:0060337; P:type I interferon signaling pathway; IBA:GO_Central.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Cell membrane; Immunity; Innate immunity; Lipoprotein;
KW Lysosome; Membrane; Osteogenesis; Palmitate; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..106
FT /note="Interferon-induced transmembrane protein 1"
FT /id="PRO_0000398565"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P13164"
FT TOPO_DOM 57..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT LIPID 49
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P13164"
FT LIPID 50
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P13164"
FT LIPID 83
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P13164"
FT CONFLICT 37
FT /note="V -> I (in Ref. 3; AAH27285)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="V -> I (in Ref. 3; AAH27285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 106 AA; 11524 MW; 7B0E7D8200D36631 CRC64;
MPKEQQEVVV LGSPHISTSA TATTINMPEI STPDHVVWSL FNTLFMNFCC LGFVAYAYSV
KSRDRKMVGD TTGAQAFAST AKCLNISSLF FTILTAIVVI VVCAIR
