GENTAUR Molecular Products.

 IFM2_HUMAN              Reviewed;         132 AA.
 Q01629; Q6FH82; Q96DA8;
 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
 02-MAR-2010, sequence version 2.
 20-JUN-2018, entry version 141.
 RecName: Full=Interferon-induced transmembrane protein 2;
 AltName: Full=Dispanin subfamily A member 2c;
          Short=DSPA2c;
 AltName: Full=Interferon-inducible protein 1-8D;
 Name=IFITM2;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-41 AND VAL-121.
 PubMed=1906403; DOI=10.1111/j.1432-1033.1991.tb16139.x;
 Lewin A.R., Reid L.E., McMahon M., Stark G.R., Kerr I.M.;
 "Molecular analysis of a human interferon-inducible gene family.";
 Eur. J. Biochem. 199:417-423(1991).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-33.
 Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
 "Cloning of human full open reading frames in Gateway(TM) system entry
 vector (pDONR201).";
 Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=16554811; DOI=10.1038/nature04632;
 Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
 Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
 Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
 FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
 Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
 Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
 Sakaki Y.;
 "Human chromosome 11 DNA sequence and analysis including novel gene
 identification.";
 Nature 440:497-500(2006).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-33; THR-41
 AND VAL-121.
 TISSUE=Lung;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [5]
 FUNCTION IN VIRAL RESISTANCE.
 PubMed=20064371; DOI=10.1016/j.cell.2009.12.017;
 Brass A.L., Huang I.C., Benita Y., John S.P., Krishnan M.N.,
 Feeley E.M., Ryan B.J., Weyer J.L., van der Weyden L., Fikrig E.,
 Adams D.J., Xavier R.J., Farzan M., Elledge S.J.;
 "The IFITM proteins mediate cellular resistance to influenza A H1N1
 virus, West Nile virus, and dengue virus.";
 Cell 139:1243-1254(2009).
 [6]
 FUNCTION, AND INDUCTION.
 PubMed=19544527; DOI=10.1002/ijc.24669;
 Daniel-Carmi V., Makovitzki-Avraham E., Reuven E.M., Goldstein I.,
 Zilkha N., Rotter V., Tzehoval E., Eisenbach L.;
 "The human 1-8D gene (IFITM2) is a novel p53 independent pro-apoptotic
 gene.";
 Int. J. Cancer 125:2810-2819(2009).
 [7]
 FUNCTION.
 PubMed=20534863; DOI=10.1128/JVI.02199-09;
 Jiang D., Weidner J.M., Qing M., Pan X.B., Guo H., Xu C., Zhang X.,
 Birk A., Chang J., Shi P.Y., Block T.M., Guo J.T.;
 "Identification of five interferon-induced cellular proteins that
 inhibit west nile virus and dengue virus infections.";
 J. Virol. 84:8332-8341(2010).
 [8]
 FUNCTION.
 PubMed=20943977; DOI=10.1128/JVI.01328-10;
 Weidner J.M., Jiang D., Pan X.B., Chang J., Block T.M., Guo J.T.;
 "Interferon-induced cell membrane proteins, IFITM3 and tetherin,
 inhibit vesicular stomatitis virus infection via distinct
 mechanisms.";
 J. Virol. 84:12646-12657(2010).
 [9]
 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
 MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=20068231; DOI=10.1126/scisignal.2000475;
 Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
 Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
 Mann M.;
 "Quantitative phosphoproteomics reveals widespread full
 phosphorylation site occupancy during mitosis.";
 Sci. Signal. 3:RA3-RA3(2010).
 [10]
 REVIEW.
 PubMed=21166591; DOI=10.1089/jir.2010.0112;
 Siegrist F., Ebeling M., Certa U.;
 "The small interferon-induced transmembrane genes and proteins.";
 J. Interferon Cytokine Res. 31:183-197(2011).
 [11]
 FUNCTION.
 PubMed=21177806; DOI=10.1128/JVI.01531-10;
 Lu J., Pan Q., Rong L., He W., Liu S.L., Liang C.;
 "The IFITM proteins inhibit HIV-1 infection.";
 J. Virol. 85:2126-2137(2011).
 [12]
 ERRATUM.
 Lu J., Pan Q., Rong L., He W., Liu S.L., Liang C.;
 J. Virol. 85:4043-4043(2011).
 [13]
 FUNCTION.
 PubMed=21253575; DOI=10.1371/journal.ppat.1001258;
 Huang I.C., Bailey C.C., Weyer J.L., Radoshitzky S.R., Becker M.M.,
 Chiang J.J., Brass A.L., Ahmed A.A., Chi X., Dong L., Longobardi L.E.,
 Boltz D., Kuhn J.H., Elledge S.J., Bavari S., Denison M.R., Choe H.,
 Farzan M.;
 "Distinct patterns of IFITM-mediated restriction of filoviruses, SARS
 coronavirus, and influenza A virus.";
 PLoS Pathog. 7:E1001258-E1001258(2011).
 [14]
 FUNCTION.
 PubMed=22479637; DOI=10.1371/journal.pone.0034508;
 Chan Y.K., Huang I.C., Farzan M.;
 "IFITM proteins restrict antibody-dependent enhancement of dengue
 virus infection.";
 PLoS ONE 7:E34508-E34508(2012).
 [15]
 GENE FAMILY.
 PubMed=22363774; DOI=10.1371/journal.pone.0031961;
 Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.;
 "The dispanins: a novel gene family of ancient origin that contains 14
 human members.";
 PLoS ONE 7:E31961-E31961(2012).
 [16]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Erythroleukemia;
 PubMed=23186163; DOI=10.1021/pr300630k;
 Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
 Mohammed S.;
 "Toward a comprehensive characterization of a human cancer cell
 phosphoproteome.";
 J. Proteome Res. 12:260-271(2013).
 -!- FUNCTION: IFN-induced antiviral protein which inhibits the entry
     of viruses to the host cell cytoplasm, permitting endocytosis, but
     preventing subsequent viral fusion and release of viral contents
     into the cytosol. Active against multiple viruses, including
     influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus
     (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus
     (WNV), human immunodeficiency virus type 1 (HIV-1) and vesicular
     stomatitis virus (VSV). Can inhibit: influenza virus hemagglutinin
     protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral
     entry, SARS-CoV S protein-mediated viral entry and VSV G protein-
     mediated viral entry. Induces cell cycle arrest and mediates
     apoptosis by caspase activation and in p53-independent manner.
     {ECO:0000269|PubMed:19544527, ECO:0000269|PubMed:20064371,
     ECO:0000269|PubMed:20534863, ECO:0000269|PubMed:20943977,
     ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575,
     ECO:0000269|PubMed:22479637}.
 -!- SUBUNIT: Interacts with CD81. {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
     membrane protein {ECO:0000305}.
 -!- INDUCTION: By IFN-alpha and IFNG/IFN-gamma. Down-regulated by
     p53/TP53. {ECO:0000269|PubMed:19544527}.
 -!- PTM: Palmitoylation on membrane-proximal cysteines controls
     clustering in membrane compartments and antiviral activity against
     influenza virus. {ECO:0000250}.
 -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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 EMBL; X57351; CAA40625.1; -; mRNA.
 EMBL; CR541874; CAG46672.1; -; mRNA.
 EMBL; AC136475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; BC009696; AAH09696.1; -; mRNA.
 CCDS; CCDS41583.1; -.
 PIR; S17183; S17183.
 RefSeq; NP_006426.2; NM_006435.2.
 UniGene; Hs.709321; -.
 ProteinModelPortal; Q01629; -.
 BioGrid; 115832; 2.
 IntAct; Q01629; 6.
 STRING; 9606.ENSP00000382714; -.
 TCDB; 8.A.58.1.2; the dispanin (dispanin) family.
 iPTMnet; Q01629; -.
 PhosphoSitePlus; Q01629; -.
 SwissPalm; Q01629; -.
 BioMuta; IFITM2; -.
 DMDM; 290457648; -.
 EPD; Q01629; -.
 MaxQB; Q01629; -.
 PaxDb; Q01629; -.
 PeptideAtlas; Q01629; -.
 PRIDE; Q01629; -.
 ProteomicsDB; 57974; -.
 DNASU; 10581; -.
 Ensembl; ENST00000399817; ENSP00000382714; ENSG00000185201.
 Ensembl; ENST00000616316; ENSP00000484689; ENSG00000185201.
 GeneID; 10581; -.
 KEGG; hsa:10581; -.
 UCSC; uc001lox.5; human.
 CTD; 10581; -.
 DisGeNET; 10581; -.
 EuPathDB; HostDB:ENSG00000185201.16; -.
 GeneCards; IFITM2; -.
 HGNC; HGNC:5413; IFITM2.
 HPA; HPA004337; -.
 MIM; 605578; gene.
 neXtProt; NX_Q01629; -.
 OpenTargets; ENSG00000185201; -.
 PharmGKB; PA29654; -.
 eggNOG; ENOG410J2DU; Eukaryota.
 eggNOG; ENOG4112C1U; LUCA.
 GeneTree; ENSGT00390000003476; -.
 HOGENOM; HOG000115781; -.
 HOVERGEN; HBG001182; -.
 InParanoid; Q01629; -.
 KO; K06566; -.
 OMA; EEHEVAT; -.
 OrthoDB; EOG091G1143; -.
 PhylomeDB; Q01629; -.
 TreeFam; TF334894; -.
 Reactome; R-HSA-909733; Interferon alpha/beta signaling.
 ChiTaRS; IFITM2; human.
 GenomeRNAi; 10581; -.
 PRO; PR:Q01629; -.
 Proteomes; UP000005640; Chromosome 11.
 Bgee; ENSG00000185201; -.
 CleanEx; HS_IFITM2; -.
 ExpressionAtlas; Q01629; baseline and differential.
 Genevisible; Q01629; HS.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
 GO; GO:0005886; C:plasma membrane; TAS:Reactome.
 GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO; GO:0006955; P:immune response; TAS:ProtInc.
 GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
 GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
 GO; GO:0035455; P:response to interferon-alpha; IDA:UniProtKB.
 GO; GO:0035456; P:response to interferon-beta; IDA:UniProtKB.
 GO; GO:0034341; P:response to interferon-gamma; IDA:UniProtKB.
 GO; GO:0009615; P:response to virus; IDA:UniProtKB.
 GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
 InterPro; IPR007593; CD225/Dispanin_fam.
 Pfam; PF04505; CD225; 1.
 1: Evidence at protein level;
 Acetylation; Antiviral defense; Cell membrane; Complete proteome;
 Immunity; Innate immunity; Lipoprotein; Membrane; Palmitate;
 Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
 CHAIN         1    132       Interferon-induced transmembrane protein
                              2.
                              /FTId=PRO_0000153728.
 TOPO_DOM      1     56       Cytoplasmic. {ECO:0000255}.
 INTRAMEM     57     77       Helical. {ECO:0000250|UniProtKB:P13164}.
 TOPO_DOM     78    106       Cytoplasmic. {ECO:0000255}.
 TRANSMEM    107    127       Helical. {ECO:0000255}.
 TOPO_DOM    128    132       Extracellular. {ECO:0000255}.
 MOD_RES       1      1       N-acetylmethionine.
                              {ECO:0000244|PubMed:20068231}.
 LIPID        70     70       S-palmitoyl cysteine. {ECO:0000250}.
 LIPID        71     71       S-palmitoyl cysteine. {ECO:0000250}.
 LIPID       104    104       S-palmitoyl cysteine. {ECO:0000250}.
 VARIANT      33     33       V -> A (in dbSNP:rs1058900).
                              {ECO:0000269|PubMed:15489334,
                              ECO:0000269|Ref.2}.
                              /FTId=VAR_062677.
 VARIANT      41     41       M -> T (in dbSNP:rs14408).
                              {ECO:0000269|PubMed:15489334,
                              ECO:0000269|PubMed:1906403}.
                              /FTId=VAR_014848.
 VARIANT     121    121       I -> V (in dbSNP:rs1059091).
                              {ECO:0000269|PubMed:15489334,
                              ECO:0000269|PubMed:1906403}.
                              /FTId=VAR_060470.
 CONFLICT     33     33       V -> G (in Ref. 1; CAA40625).
                              {ECO:0000305}.
 SEQUENCE   132 AA;  14632 MW;  232A32D109EEBF5D CRC64;
 MNHIVQTFSP VNSGQPPNYE MLKEEQEVAM LGVPHNPAPP MSTVIHIRSE TSVPDHVVWS
 LFNTLFMNTC CLGFIAFAYS VKSRDRKMVG DVTGAQAYAS TAKCLNIWAL ILGIFMTILL
 IIIPVLVVQA QR

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