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   24-JAN-2024, entry version 144.
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;
RC   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.ENSMUSP00000101657; -.
DR   PhosphoSitePlus; Q9D103; -.
DR   SwissPalm; Q9D103; -.
DR   EPD; Q9D103; -.
DR   MaxQB; Q9D103; -.
DR   PaxDb; 10090-ENSMUSP00000026564; -.
DR   ProteomicsDB; 267279; -.
DR   DNASU; 68713; -.
DR   Ensembl; ENSMUST00000026564.9; ENSMUSP00000026564.9; ENSMUSG00000025491.15.
DR   Ensembl; ENSMUST00000106040.8; ENSMUSP00000101655.2; ENSMUSG00000025491.15.
DR   Ensembl; ENSMUST00000106042.9; ENSMUSP00000101657.3; ENSMUSG00000025491.15.
DR   GeneID; 68713; -.
DR   KEGG; mmu:68713; -.
DR   UCSC; uc009kja.2; mouse.
DR   AGR; MGI:1915963; -.
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; VINICSE; -.
DR   OrthoDB; 5322528at2759; -.
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 77 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 237 other cell types or tissues.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
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 type II interferon; 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-mediated signaling pathway; IBA:GO_Central.
DR   InterPro; IPR007593; CD225/Dispanin_fam.
DR   PANTHER; PTHR13999; INTERFERON INDUCIBLE TRANSMEMBRANE PROTEIN; 1.
DR   PANTHER; PTHR13999:SF13; INTERFERON-INDUCED TRANSMEMBRANE PROTEIN 1-RELATED; 1.
DR   Pfam; PF04505; CD225; 1.
DR   Genevisible; Q9D103; MM.
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
//