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IFM2_HUMAN
ID   IFM2_HUMAN              Reviewed;         132 AA.
AC   Q01629; Q6FH82; Q96DA8;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Interferon-induced transmembrane protein 2 {ECO:0000305};
DE   AltName: Full=Dispanin subfamily A member 2c;
DE            Short=DSPA2c;
DE   AltName: Full=Interferon-inducible protein 1-8D;
GN   Name=IFITM2 {ECO:0000312|HGNC:HGNC:5413};
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 VARIANTS THR-41 AND VAL-121.
RX   PubMed=1906403; DOI=10.1111/j.1432-1033.1991.tb16139.x;
RA   Lewin A.R., Reid L.E., McMahon M., Stark G.R., Kerr I.M.;
RT   "Molecular analysis of a human interferon-inducible gene family.";
RL   Eur. J. Biochem. 199:417-423(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-33.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-33; THR-41 AND
RP   VAL-121.
RC   TISSUE=Lung;
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   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   [6]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=19544527; DOI=10.1002/ijc.24669;
RA   Daniel-Carmi V., Makovitzki-Avraham E., Reuven E.M., Goldstein I.,
RA   Zilkha N., Rotter V., Tzehoval E., Eisenbach L.;
RT   "The human 1-8D gene (IFITM2) is a novel p53 independent pro-apoptotic
RT   gene.";
RL   Int. J. Cancer 125:2810-2819(2009).
RN   [7]
RP   FUNCTION.
RX   PubMed=20534863; DOI=10.1128/jvi.02199-09;
RA   Jiang D., Weidner J.M., Qing M., Pan X.B., Guo H., Xu C., Zhang X.,
RA   Birk A., Chang J., Shi P.Y., Block T.M., Guo J.T.;
RT   "Identification of five interferon-induced cellular proteins that inhibit
RT   west nile virus and dengue virus infections.";
RL   J. Virol. 84:8332-8341(2010).
RN   [8]
RP   FUNCTION.
RX   PubMed=20943977; DOI=10.1128/jvi.01328-10;
RA   Weidner J.M., Jiang D., Pan X.B., Chang J., Block T.M., Guo J.T.;
RT   "Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit
RT   vesicular stomatitis virus infection via distinct mechanisms.";
RL   J. Virol. 84:12646-12657(2010).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [17]
RP   FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-19, PALMITOYLATION
RP   AT CYS-70; CYS-71 AND CYS-104, INTERACTION WITH CD81, AND MUTAGENESIS OF
RP   TYR-19; 70-CYS-CYS-71 AND CYS-104.
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   [18]
RP   FUNCION.
RX   PubMed=33239446; DOI=10.1073/pnas.2012197117;
RA   Zang R., Case J.B., Yutuc E., Ma X., Shen S., Gomez Castro M.F., Liu Z.,
RA   Zeng Q., Zhao H., Son J., Rothlauf P.W., Kreutzberger A.J.B., Hou G.,
RA   Zhang H., Bose S., Wang X., Vahey M.D., Mani K., Griffiths W.J.,
RA   Kirchhausen T., Fremont D.H., Guo H., Diwan A., Wang Y., Diamond M.S.,
RA   Whelan S.P.J., Ding S.;
RT   "Cholesterol 25-hydroxylase suppresses SARS-CoV-2 replication by blocking
RT   membrane fusion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 117:32105-32113(2020).
RN   [19]
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   [20]
RP   FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-19, AND INDUCTION BY
RP   IFNB1.
RX   PubMed=33563656; DOI=10.1128/jvi.02422-20;
RA   Winstone H., Lista M.J., Reid A.C., Bouton C., Pickering S., Galao R.P.,
RA   Kerridge C., Doores K.J., Swanson C., Neil S.;
RT   "The polybasic cleavage site in the SARS-CoV-2 spike modulates viral
RT   sensitivity to Type I interferon and IFITM2.";
RL   J. Virol. 0:0-0(2021).
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 (PubMed:33563656, PubMed:26354436). Active against multiple
CC       viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and
CC       SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus
CC       (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-
CC       1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV)
CC       (PubMed:33563656, PubMed:26354436, PubMed:33270927, PubMed:33239446).
CC       Can inhibit: influenza virus hemagglutinin protein-mediated viral
CC       entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV and SARS-CoV-
CC       2 S protein-mediated viral entry and VSV G protein-mediated viral entry
CC       (PubMed:33563656). Induces cell cycle arrest and mediates apoptosis by
CC       caspase activation and in p53-independent manner. In hepatocytes, IFITM
CC       proteins act in a coordinated manner to restrict HCV infection by
CC       targeting the endocytosed HCV virion for lysosomal degradation
CC       (PubMed:26354436). IFITM2 and IFITM3 display anti-HCV activity that may
CC       complement the anti-HCV activity of IFITM1 by inhibiting the late
CC       stages of HCV entry, possibly in a coordinated manner by trapping the
CC       virion in the endosomal pathway and targeting it for degradation at the
CC       lysosome (PubMed:26354436). {ECO:0000269|PubMed:19544527,
CC       ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20534863,
CC       ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21177806,
CC       ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22479637,
CC       ECO:0000269|PubMed:26354436, ECO:0000269|PubMed:33239446,
CC       ECO:0000269|PubMed:33270927, ECO:0000269|PubMed:33563656}.
CC   -!- SUBUNIT: Interacts with CD81. {ECO:0000250|UniProtKB:Q99J93}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:33563656};
CC       Single-pass type II membrane protein {ECO:0000305}. Lysosome membrane
CC       {ECO:0000269|PubMed:26354436}; Single-pass type II membrane protein
CC       {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:26354436};
CC       Single-pass type II membrane protein {ECO:0000305}.
CC   -!- INDUCTION: By IFN-alpha, IFNB1/IFN-beta and IFNG/IFN-gamma. Down-
CC       regulated by p53/TP53. {ECO:0000269|PubMed:19544527,
CC       ECO:0000269|PubMed:33563656}.
CC   -!- PTM: Palmitoylation on membrane-proximal cysteines controls clustering
CC       in membrane compartments and antiviral activity.
CC       {ECO:0000305|PubMed:26354436}.
CC   -!- PTM: Phosphorylation at Tyr-19 is required for endosomal and lysosomal
CC       location. {ECO:0000269|PubMed:26354436}.
CC   -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR   EMBL; X57351; CAA40625.1; -; mRNA.
DR   EMBL; CR541874; CAG46672.1; -; mRNA.
DR   EMBL; AC136475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC009696; AAH09696.1; -; mRNA.
DR   CCDS; CCDS41583.1; -.
DR   PIR; S17183; S17183.
DR   RefSeq; NP_006426.2; NM_006435.2.
DR   AlphaFoldDB; Q01629; -.
DR   SMR; Q01629; -.
DR   BioGRID; 115832; 6.
DR   IntAct; Q01629; 6.
DR   STRING; 9606.ENSP00000484689; -.
DR   TCDB; 8.A.58.1.2; the dispanin (dispanin) family.
DR   iPTMnet; Q01629; -.
DR   PhosphoSitePlus; Q01629; -.
DR   SwissPalm; Q01629; -.
DR   BioMuta; IFITM2; -.
DR   DMDM; 290457648; -.
DR   EPD; Q01629; -.
DR   jPOST; Q01629; -.
DR   MassIVE; Q01629; -.
DR   MaxQB; Q01629; -.
DR   PaxDb; Q01629; -.
DR   PeptideAtlas; Q01629; -.
DR   PRIDE; Q01629; -.
DR   ProteomicsDB; 57974; -.
DR   Antibodypedia; 22433; 274 antibodies from 25 providers.
DR   DNASU; 10581; -.
DR   Ensembl; ENST00000616316.3; ENSP00000484689.1; ENSG00000185201.18.
DR   Ensembl; ENST00000680197.1; ENSP00000505840.1; ENSG00000185201.18.
DR   GeneID; 10581; -.
DR   KEGG; hsa:10581; -.
DR   MANE-Select; ENST00000616316.3; ENSP00000484689.1; NM_006435.3; NP_006426.2.
DR   UCSC; uc001lox.5; human.
DR   CTD; 10581; -.
DR   DisGeNET; 10581; -.
DR   GeneCards; IFITM2; -.
DR   HGNC; HGNC:5413; IFITM2.
DR   HPA; ENSG00000185201; Low tissue specificity.
DR   MIM; 605578; gene.
DR   neXtProt; NX_Q01629; -.
DR   OpenTargets; ENSG00000185201; -.
DR   PharmGKB; PA29654; -.
DR   VEuPathDB; HostDB:ENSG00000185201; -.
DR   eggNOG; ENOG502S9XK; Eukaryota.
DR   GeneTree; ENSGT00950000182857; -.
DR   InParanoid; Q01629; -.
DR   OMA; SHHNELH; -.
DR   OrthoDB; 1555189at2759; -.
DR   PhylomeDB; Q01629; -.
DR   TreeFam; TF334894; -.
DR   PathwayCommons; Q01629; -.
DR   Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR   SignaLink; Q01629; -.
DR   BioGRID-ORCS; 10581; 319 hits in 1040 CRISPR screens.
DR   ChiTaRS; IFITM2; human.
DR   GenomeRNAi; 10581; -.
DR   Pharos; Q01629; Tbio.
DR   PRO; PR:Q01629; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q01629; protein.
DR   Bgee; ENSG00000185201; Expressed in blood and 208 other tissues.
DR   ExpressionAtlas; Q01629; baseline and differential.
DR   Genevisible; Q01629; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR   GO; GO:0035458; P:cellular response to interferon-beta; IDA:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
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: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   Acetylation; Antiviral defense; Cell membrane; Endosome; Immunity;
KW   Innate immunity; Lipoprotein; Lysosome; Membrane; Palmitate;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..132
FT                   /note="Interferon-induced transmembrane protein 2"
FT                   /id="PRO_0000153728"
FT   TOPO_DOM        1..56
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P13164"
FT   TOPO_DOM        78..106
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..132
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         19
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:26354436"
FT   LIPID           70
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:26354436"
FT   LIPID           71
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:26354436"
FT   LIPID           104
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:26354436"
FT   VARIANT         33
FT                   /note="V -> A (in dbSNP:rs1058900)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT                   /id="VAR_062677"
FT   VARIANT         41
FT                   /note="M -> T (in dbSNP:rs14408)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:1906403"
FT                   /id="VAR_014848"
FT   VARIANT         121
FT                   /note="I -> V (in dbSNP:rs1059091)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:1906403"
FT                   /id="VAR_060470"
FT   MUTAGEN         19
FT                   /note="Y->F,A: Loss of phosphorylation. Accumulates at the
FT                   plasma membrane. Increases infection with influenza A virus
FT                   and SARS-CoV-2. Increases anti-HCV properties."
FT                   /evidence="ECO:0000269|PubMed:26354436,
FT                   ECO:0000269|PubMed:33563656"
FT   MUTAGEN         70..71
FT                   /note="CC->AA: No effect on anti-HCV activity. Partial loss
FT                   of endosomal location."
FT                   /evidence="ECO:0000269|PubMed:26354436"
FT   MUTAGEN         104
FT                   /note="C->A: Loss of anti-HCV activity. Partial loss of
FT                   endosomal location."
FT                   /evidence="ECO:0000269|PubMed:26354436"
FT   CONFLICT        33
FT                   /note="V -> G (in Ref. 1; CAA40625)"
FT                   /evidence="ECO:0000305"
SQ   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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