ID IFM1_HUMAN Reviewed; 125 AA. AC P13164; Q15322; Q53XZ0; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 3. DT 24-JAN-2024, entry version 187. DE RecName: Full=Interferon-induced transmembrane protein 1 {ECO:0000305}; DE AltName: Full=Dispanin subfamily A member 2a; DE Short=DSPA2a; DE AltName: Full=Interferon-induced protein 17; DE AltName: Full=Interferon-inducible protein 9-27; DE AltName: Full=Leu-13 antigen; DE AltName: CD_antigen=CD225; GN Name=IFITM1 {ECO:0000312|HGNC:HGNC:5412}; Synonyms=CD225, IFI17; 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 [MRNA], AND VARIANT ALA-13. RX PubMed=2492664; DOI=10.1073/pnas.86.3.840; RA Reid L.E., Brasnett A.H., Gilbert C.S., Porter A.C.G., Gewert D.R., RA Stark G.R., Kerr I.M.; RT "A single DNA response element can confer inducibility by both alpha- and RT gamma-interferons."; RL Proc. Natl. Acad. Sci. U.S.A. 86:840-844(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-13. RX PubMed=7559564; DOI=10.1074/jbc.270.40.23860; RA Deblandre G.A., Marinx O.P., Evans S.S., Majjaj S., Leo O., Caput D., RA Huez G.A., Wathelet M.G.; RT "Expression cloning of an interferon-inducible 17-kDa membrane protein RT implicated in the control of cell growth."; RL J. Biol. Chem. 270:23860-23866(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-13. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-13. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-13. RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-13. RC TISSUE=Cervix; 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 [8] RP INTERACTION WITH CD81. RX PubMed=2398277; RA Takahashi S., Doss C., Levy S., Levy R.; RT "TAPA-1, the target of an antiproliferative antibody, is associated on the RT cell surface with the Leu-13 antigen."; RL J. Immunol. 145:2207-2213(1990). RN [9] RP IDENTIFICATION IN A COMPLEX WITH CR2; CD81 AND CD19, AND SUBCELLULAR RP LOCATION. RX PubMed=1383329; RA Bradbury L.E., Kansas G.S., Levy S., Evans R.L., Tedder T.F.; RT "The CD19/CD21 signal transducing complex of human B lymphocytes includes RT the target of antiproliferative antibody-1 and Leu-13 molecules."; RL J. Immunol. 149:2841-2850(1992). RN [10] RP FUNCTION. RX PubMed=16847454; DOI=10.1038/sj.onc.1209807; RA Yang G., Xu Y., Chen X., Hu G.; RT "IFITM1 plays an essential role in the antiproliferative action of RT interferon-gamma."; RL Oncogene 26:594-603(2007). RN [11] RP SUBCELLULAR LOCATION, AND INTERACTION WITH CAV1. RX PubMed=19499152; DOI=10.1093/abbs/gmp034; RA Xu Y., Yang G., Hu G.; RT "Binding of IFITM1 enhances the inhibiting effect of caveolin-1 on ERK RT activation."; RL Acta Biochim. Biophys. Sin. 41:488-494(2009). RN [12] RP FUNCTION IN VIRAL RESISTANCE. RX PubMed=20064371; DOI=10.1016/j.cell.2009.12.017; RA Brass A.L., Huang I.C., Benita Y., John S.P., Krishnan M.N., Feeley E.M., RA Ryan B.J., Weyer J.L., van der Weyden L., Fikrig E., Adams D.J., RA Xavier R.J., Farzan M., Elledge S.J.; RT "The IFITM proteins mediate cellular resistance to influenza A H1N1 virus, RT West Nile virus, and dengue virus."; RL Cell 139:1243-1254(2009). RN [13] 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 [14] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=20838853; DOI=10.1007/s11060-010-0377-4; RA Yu F., Ng S.S., Chow B.K., Sze J., Lu G., Poon W.S., Kung H.F., Lin M.C.; RT "Knockdown of interferon-induced transmembrane protein 1 (IFITM1) inhibits RT proliferation, migration, and invasion of glioma cells."; RL J. Neurooncol. 103:187-195(2011). RN [15] RP FUNCTION. RX PubMed=21177806; DOI=10.1128/jvi.01531-10; RA Lu J., Pan Q., Rong L., He W., Liu S.L., Liang C.; RT "The IFITM proteins inhibit HIV-1 infection."; RL J. Virol. 85:2126-2137(2011). RN [16] RP ERRATUM OF PUBMED:21177806. RA Lu J., Pan Q., Rong L., He W., Liu S.L., Liang C.; RL J. Virol. 85:4043-4043(2011). RN [17] RP FUNCTION. RX PubMed=21976647; DOI=10.1128/jvi.05633-11; RA Raychoudhuri A., Shrivastava S., Steele R., Kim H., Ray R., Ray R.B.; RT "ISG56 and IFITM1 proteins inhibit hepatitis C virus replication."; RL J. Virol. 85:12881-12889(2011). RN [18] 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 [19] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=22634173; DOI=10.1016/j.bone.2012.05.012; RA Kim B.S., Kim H.J., Kim J.S., You Y.O., Zadeh H., Shin H.I., Lee S.J., RA Park Y.J., Takata T., Pi S.H., Lee J., You H.K.; RT "IFITM1 increases osteogenesis through Runx2 in human alveolar-derived bone RT marrow stromal cells."; RL Bone 51:506-514(2012). RN [20] RP FUNCTION. RX PubMed=22479637; DOI=10.1371/journal.pone.0034508; RA Chan Y.K., Huang I.C., Farzan M.; RT "IFITM proteins restrict antibody-dependent enhancement of dengue virus RT infection."; RL PLoS ONE 7:E34508-E34508(2012). RN [21] 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). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, VARIANT [LARGE SCALE RP ANALYSIS] ALA-13, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=25105503; DOI=10.1371/journal.pone.0104341; RA Weston S., Czieso S., White I.J., Smith S.E., Kellam P., Marsh M.; RT "A membrane topology model for human interferon inducible transmembrane RT protein 1."; RL PLoS ONE 9:E104341-E104341(2014). RN [24] RP FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-50; CYS-51 AND RP CYS-84, AND MUTAGENESIS OF 50-CYS-CYS-51 AND CYS-84. RX PubMed=26354436; DOI=10.1074/jbc.m115.657346; RA Narayana S.K., Helbig K.J., McCartney E.M., Eyre N.S., Bull R.A., RA Eltahla A., Lloyd A.R., Beard M.R.; RT "The Interferon-induced Transmembrane Proteins, IFITM1, IFITM2, and IFITM3 RT Inhibit Hepatitis C Virus Entry."; RL J. Biol. Chem. 290:25946-25959(2015). RN [25] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=33051876; DOI=10.15252/embj.2020106267; RA Buchrieser J., Dufloo J., Hubert M., Monel B., Planas D., Rajah M.M., RA Planchais C., Porrot F., Guivel-Benhassine F., Van der Werf S., RA Casartelli N., Mouquet H., Bruel T., Schwartz O.; RT "Syncytia formation by SARS-CoV-2-infected cells."; RL EMBO J. 39:e106267-e106267(2020). RN [26] RP ERRATUM OF PUBMED:33051876. RX PubMed=33522642; DOI=10.15252/embj.2020107405; RA Buchrieser J., Dufloo J., Hubert M., Monel B., Planas D., Rajah M.M., RA Planchais C., Porrot F., Guivel-Benhassine F., Van der Werf S., RA Casartelli N., Mouquet H., Bruel T., Schwartz O.; RT "Syncytia formation by SARS-CoV-2-infected cells."; RL EMBO J. 40:e107405-e107405(2021). RN [27] RP FUNCTION. RX PubMed=33270927; DOI=10.15252/embj.2020106501; RA Shi G., Kenney A.D., Kudryashova E., Zani A., Zhang L., Lai K.K., RA Hall-Stoodley L., Robinson R.T., Kudryashov D.S., Compton A.A., Yount J.S.; RT "Opposing activities of IFITM proteins in SARS-CoV-2 infection."; RL EMBO J. 40:e106501-e106501(2021). RN [28] RP VARIANT [LARGE SCALE ANALYSIS] ALA-13, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). 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 coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus CC (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), CC human immunodeficiency virus type 1 (HIV-1) and hepatitis C virus (HCV) CC (PubMed:26354436, PubMed:33270927). Can inhibit: influenza virus CC hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2- CC mediated viral entry and SARS-CoV and SARS-CoV-2 S protein-mediated CC viral entry. Also implicated in cell adhesion and control of cell CC growth and migration (PubMed:33270927). Inhibits SARS-CoV-2 S protein- CC mediated syncytia formation (PubMed:33051876). Plays a key role in the CC antiproliferative action of IFN-gamma either by inhibiting the ERK CC activation or by arresting cell growth in G1 phase in a p53-dependent CC manner. Acts as a positive regulator of osteoblast differentiation. In CC hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV CC infection by targeting the endocytosed HCV virion for lysosomal CC degradation (PubMed:26354436). IFITM2 and IFITM3 display anti-HCV CC activity that may complement the anti-HCV activity of IFITM1 by CC inhibiting the late stages of HCV entry, possibly in a coordinated CC manner by trapping the virion in the endosomal pathway and targeting it CC for degradation at the lysosome (PubMed:26354436). CC {ECO:0000269|PubMed:16847454, ECO:0000269|PubMed:20064371, CC ECO:0000269|PubMed:20838853, ECO:0000269|PubMed:21177806, CC ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:21976647, CC ECO:0000269|PubMed:22479637, ECO:0000269|PubMed:22634173, CC ECO:0000269|PubMed:26354436, ECO:0000269|PubMed:33051876, CC ECO:0000269|PubMed:33270927}. CC -!- SUBUNIT: Interacts with CD81 (PubMed:2398277, PubMed:26354436). Part of CC a complex composed of CD19, CR2/CD21, CD81 and IFITM1/CD225 in the CC membrane of mature B-cells (PubMed:1383329). Interacts with CAV1; this CC interaction enhances the ability of CAV1 in inhibiting ERK activation CC (PubMed:19499152). {ECO:0000269|PubMed:1383329, CC ECO:0000269|PubMed:19499152, ECO:0000269|PubMed:2398277, CC ECO:0000269|PubMed:26354436}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1383329, CC ECO:0000269|PubMed:19499152, ECO:0000269|PubMed:25105503, CC ECO:0000269|PubMed:26354436}; Single-pass membrane protein CC {ECO:0000269|PubMed:19499152}. Lysosome membrane CC {ECO:0000269|PubMed:26354436}. CC -!- TISSUE SPECIFICITY: Bone (at protein level). Levels greatly elevated in CC colon cancer, cervical cancer, esophageal cancer and ovarian cancer. CC Expressed in glioma cell lines. {ECO:0000269|PubMed:20838853, CC ECO:0000269|PubMed:22634173}. CC -!- INDUCTION: By IFN-alpha and IFNG/IFN-gamma. CC -!- PTM: Palmitoylation on membrane-proximal cysteines controls clustering CC in membrane compartments and antiviral activity. CC {ECO:0000305|PubMed:26354436}. CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04164; AAA35494.1; -; mRNA. DR EMBL; X84958; CAA59337.1; -; mRNA. DR EMBL; BT007173; AAP35837.1; -; mRNA. DR EMBL; AK290480; BAF83169.1; -; mRNA. DR EMBL; AC136475; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471278; EAW61218.1; -; Genomic_DNA. DR EMBL; BC000897; AAH00897.1; -; mRNA. DR CCDS; CCDS41584.1; -. DR PIR; A31454; A31454. DR RefSeq; NP_003632.3; NM_003641.3. DR AlphaFoldDB; P13164; -. DR BioGRID; 114091; 361. DR DIP; DIP-32672N; -. DR IntAct; P13164; 9. DR MINT; P13164; -. DR STRING; 9606.ENSP00000330825; -. DR TCDB; 8.A.58.1.1; the dispanin (dispanin) family. DR iPTMnet; P13164; -. DR PhosphoSitePlus; P13164; -. DR SwissPalm; P13164; -. DR BioMuta; IFITM1; -. DR DMDM; 215274118; -. DR EPD; P13164; -. DR jPOST; P13164; -. DR MassIVE; P13164; -. DR MaxQB; P13164; -. DR PaxDb; 9606-ENSP00000386187; -. DR PeptideAtlas; P13164; -. DR ProteomicsDB; 52897; -. DR Pumba; P13164; -. DR TopDownProteomics; P13164; -. DR Antibodypedia; 1282; 426 antibodies from 38 providers. DR DNASU; 8519; -. DR Ensembl; ENST00000328221.5; ENSP00000330825.5; ENSG00000185885.17. DR Ensembl; ENST00000408968.4; ENSP00000386187.3; ENSG00000185885.17. DR Ensembl; ENST00000528780.5; ENSP00000437057.1; ENSG00000185885.17. DR Ensembl; ENST00000680588.1; ENSP00000505380.1; ENSG00000185885.17. DR GeneID; 8519; -. DR KEGG; hsa:8519; -. DR MANE-Select; ENST00000408968.4; ENSP00000386187.3; NM_003641.5; NP_003632.4. DR UCSC; uc001loy.5; human. DR AGR; HGNC:5412; -. DR CTD; 8519; -. DR DisGeNET; 8519; -. DR GeneCards; IFITM1; -. DR HGNC; HGNC:5412; IFITM1. DR HPA; ENSG00000185885; Low tissue specificity. DR MIM; 604456; gene. DR neXtProt; NX_P13164; -. DR OpenTargets; ENSG00000185885; -. DR PharmGKB; PA29653; -. DR VEuPathDB; HostDB:ENSG00000185885; -. DR eggNOG; ENOG502S9XK; Eukaryota. DR GeneTree; ENSGT00950000182857; -. DR HOGENOM; CLU_124511_3_0_1; -. DR InParanoid; P13164; -. DR OMA; LYANVCC; -. DR OrthoDB; 5322528at2759; -. DR PhylomeDB; P13164; -. DR TreeFam; TF334894; -. DR PathwayCommons; P13164; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR SignaLink; P13164; -. DR BioGRID-ORCS; 8519; 13 hits in 1151 CRISPR screens. DR ChiTaRS; IFITM1; human. DR GeneWiki; IFITM1; -. DR GenomeRNAi; 8519; -. DR Pharos; P13164; Tbio. DR PRO; PR:P13164; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P13164; Protein. DR Bgee; ENSG00000185885; Expressed in right ovary and 199 other cell types or tissues. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central. DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP: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; IDA:UniProtKB. DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:UniProtKB. DR GO; GO:0035455; P:response to interferon-alpha; IDA:UniProtKB. DR GO; GO:0035456; P:response to interferon-beta; IDA:UniProtKB. DR GO; GO:0034341; P:response to type II interferon; IDA:UniProtKB. DR GO; GO:0009615; P:response to virus; IDA:UniProtKB. 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:SF6; INTERFERON-INDUCED TRANSMEMBRANE PROTEIN 1; 1. DR Pfam; PF04505; CD225; 1. DR Genevisible; P13164; HS. PE 1: Evidence at protein level; KW Antiviral defense; Cell membrane; Immunity; Innate immunity; Lipoprotein; KW Lysosome; Membrane; Osteogenesis; Palmitate; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..125 FT /note="Interferon-induced transmembrane protein 1" FT /id="PRO_0000153727" FT TOPO_DOM 1..36 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT INTRAMEM 37..57 FT /note="Helical" FT /evidence="ECO:0000303|PubMed:25105503" FT TOPO_DOM 58..86 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 87..107 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 108..125 FT /note="Extracellular" FT /evidence="ECO:0000255" FT REGION 84..125 FT /note="Interaction with CAV1" FT /evidence="ECO:0000269|PubMed:19499152" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT LIPID 50 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:26354436" FT LIPID 51 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:26354436" FT LIPID 84 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:26354436" FT VARIANT 13 FT /note="P -> A (in dbSNP:rs9667990)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2492664, FT ECO:0000269|PubMed:7559564, ECO:0000269|Ref.3, FT ECO:0000269|Ref.6, ECO:0007744|PubMed:21269460, FT ECO:0007744|PubMed:23186163" FT /id="VAR_047422" FT MUTAGEN 50..51 FT /note="CC->AA: No effect on anti-HCV activity. Only FT localizes at the lysosome." FT /evidence="ECO:0000269|PubMed:26354436" FT MUTAGEN 84 FT /note="C->A: Loss of anti-HCV activity. Only localizes at FT the lysosome." FT /evidence="ECO:0000269|PubMed:26354436" FT CONFLICT 103 FT /note="L -> S (in Ref. 1; AAA35494)" FT /evidence="ECO:0000305" SQ SEQUENCE 125 AA; 13964 MW; 10EE5B64894838ED CRC64; MHKEEHEVAV LGPPPSTILP RSTVINIHSE TSVPDHVVWS LFNTLFLNWC CLGFIAFAYS VKSRDRKMVG DVTGAQAYAS TAKCLNIWAL ILGILMTIGF ILLLVFGSVT VYHIMLQIIQ EKRGY //