IFM2_MOUSE
ID IFM2_MOUSE Reviewed; 144 AA.
AC Q99J93; Q3TIG4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Interferon-induced transmembrane protein 2;
DE AltName: Full=Dispanin subfamily A member 2c;
DE Short=DSPA2c;
DE AltName: Full=Fragilis protein 3;
GN Name=Ifitm2;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; 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=FVB/N, and FVB/N-3; TISSUE=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 INTERACTION WITH CD81.
RX PubMed=16395393; DOI=10.1038/sj.gene.6364278;
RA Smith R.A., Young J., Weis J.J., Weis J.H.;
RT "Expression of the mouse fragilis gene products in immune cells and
RT association with receptor signaling complexes.";
RL Genes Immun. 7:113-121(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
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 [8]
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 [9]
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) and Ebola
CC virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV). Can
CC inhibit: influenza virus hemagglutinin protein-mediated viral entry,
CC MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-
CC mediated viral entry. Induces cell cycle arrest and mediates apoptosis
CC by caspase activation and in p53-independent manner.
CC {ECO:0000269|PubMed:21253575}.
CC -!- SUBUNIT: Interacts with CD81. {ECO:0000269|PubMed:16395393}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01629};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01629}.
CC Lysosome membrane {ECO:0000250|UniProtKB:Q01629}; Single-pass type II
CC membrane protein {ECO:0000250|UniProtKB:Q01629}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q01629}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q01629}.
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: From 5.5 dpc to 7.5 dpc expressed within the
CC epiblast. At 8.5 dpc expressed throughout the entire embryo. Expressed
CC in the gonadal germ cells at 11.5 dpc/12.5.
CC {ECO:0000269|PubMed:12659663}.
CC -!- PTM: Palmitoylation on membrane-proximal cysteines controls clustering
CC in membrane compartments and antiviral activity.
CC {ECO:0000250|UniProtKB:Q01629}.
CC -!- PTM: Phosphorylation at Tyr-19 is required for endosomal and lysosomal
CC location. {ECO:0000250|UniProtKB:Q01629}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR EMBL; AY082486; AAM03318.1; -; mRNA.
DR EMBL; AK141392; BAE24670.1; -; mRNA.
DR EMBL; AK167865; BAE39882.1; -; mRNA.
DR EMBL; CH466531; EDL17975.1; -; Genomic_DNA.
DR EMBL; BC002102; AAH02102.1; -; mRNA.
DR EMBL; BC002160; AAH02160.1; -; mRNA.
DR EMBL; BC084679; AAH84679.1; -; mRNA.
DR CCDS; CCDS21994.1; -.
DR RefSeq; NP_109619.1; NM_030694.1.
DR AlphaFoldDB; Q99J93; -.
DR BioGRID; 219823; 3.
DR STRING; 10090.ENSMUSP00000071470; -.
DR iPTMnet; Q99J93; -.
DR PhosphoSitePlus; Q99J93; -.
DR SwissPalm; Q99J93; -.
DR EPD; Q99J93; -.
DR jPOST; Q99J93; -.
DR MaxQB; Q99J93; -.
DR PaxDb; Q99J93; -.
DR PeptideAtlas; Q99J93; -.
DR PRIDE; Q99J93; -.
DR ProteomicsDB; 267280; -.
DR Ensembl; ENSMUST00000081649; ENSMUSP00000071470; ENSMUSG00000060591.
DR GeneID; 80876; -.
DR KEGG; mmu:80876; -.
DR UCSC; uc009kiz.1; mouse.
DR CTD; 10581; -.
DR MGI; MGI:1933382; Ifitm2.
DR VEuPathDB; HostDB:ENSMUSG00000060591; -.
DR eggNOG; ENOG502S9XK; Eukaryota.
DR GeneTree; ENSGT00950000182857; -.
DR HOGENOM; CLU_124511_3_0_1; -.
DR InParanoid; Q99J93; -.
DR OMA; VINICSE; -.
DR OrthoDB; 1555189at2759; -.
DR PhylomeDB; Q99J93; -.
DR TreeFam; TF334894; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 80876; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Ifitm2; mouse.
DR PRO; PR:Q99J93; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q99J93; protein.
DR Bgee; ENSMUSG00000060591; Expressed in adrenal gland and 68 other tissues.
DR Genevisible; Q99J93; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0035458; P:cellular response to interferon-beta; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:MGI.
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; IBA:GO_Central.
DR GO; GO:0035455; P:response to interferon-alpha; IBA:GO_Central.
DR GO; GO:0035456; P:response to interferon-beta; IBA:GO_Central.
DR GO; GO:0034341; P:response to interferon-gamma; IBA:GO_Central.
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..144
FT /note="Interferon-induced transmembrane protein 2"
FT /id="PRO_0000398566"
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..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q01629"
FT MOD_RES 19
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01629"
FT LIPID 70
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q01629"
FT LIPID 71
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q01629"
FT LIPID 104
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q01629"
SQ SEQUENCE 144 AA; 15743 MW; 99C7CDBA25CAF1A9 CRC64;
MSHNSQAFLS TNAGLPPSYE TIKEEYGVTE LGEPSNSAVV RTTVINMPRE VSVPDHVVWS
LFNTLFFNAC CLGFVAYAYS VKSRDRKMVG DVVGAQAYAS TAKCLNISSL IFSILMVIIC
IIIFSTTSVV VFQSFAQRTP HSGF
