IFM1_HUMAN
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 03-AUG-2022, entry version 179.
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}.
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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; 359.
DR DIP; DIP-32672N; -.
DR IntAct; P13164; 9.
DR MINT; P13164; -.
DR STRING; 9606.ENSP00000386187; -.
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; P13164; -.
DR PeptideAtlas; P13164; -.
DR PRIDE; P13164; -.
DR ProteomicsDB; 52897; -.
DR TopDownProteomics; P13164; -.
DR Antibodypedia; 1282; 386 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 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; YGSVAIY; -.
DR OrthoDB; 1555189at2759; -.
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; 10 hits in 1075 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 197 other tissues.
DR Genevisible; P13164; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 interferon-gamma; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
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 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
