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Interferon-induced transmembrane protein 3 (Dispanin subfamily A member 2b) (DSPA2b) (Fragilis protein) (Interferon-inducible protein 15) (Mouse ifitm-like protein 1) (Mil-1)

 IFM3_MOUSE              Reviewed;         137 AA.
Q9CQW9; Q9D8L6;
05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
05-JUL-2017, entry version 116.
RecName: Full=Interferon-induced transmembrane protein 3;
AltName: Full=Dispanin subfamily A member 2b;
Short=DSPA2b;
AltName: Full=Fragilis protein;
AltName: Full=Interferon-inducible protein 15;
AltName: Full=Mouse ifitm-like protein 1;
Short=Mil-1;
Name=Ifitm3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
PubMed=14516695; DOI=10.1016/S0925-4773(03)00126-6;
Tanaka S.S., Matsui Y.;
"Developmentally regulated expression of mil-1 and mil-2, mouse
interferon-induced transmembrane protein like genes, during formation
and differentiation of primordial germ cells.";
Mech. Dev. 119:S261-S267(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
STRAIN=129/SvEv;
PubMed=12124616; DOI=10.1038/nature00927;
Saitou M., Barton S.C., Surani M.A.;
"A molecular programme for the specification of germ cell fate in
mice.";
Nature 418:293-300(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=BALB/cJ;
PubMed=15184081; DOI=10.1016/j.bbrc.2004.05.085;
Ropolo A., Tomasini R., Grasso D., Dusetti N.J., Cerquetti M.C.,
Iovanna J.L., Vaccaro M.I.;
"Cloning of IP15, a pancreatitis-induced gene whose expression
inhibits cell growth.";
Biochem. Biophys. Res. Commun. 319:1001-1009(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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).
[7]
TISSUE SPECIFICITY.
PubMed=12659663; DOI=10.1186/1471-213X-3-1;
Lange U.C., Saitou M., Western P.S., Barton S.C., Surani M.A.;
"The fragilis interferon-inducible gene family of transmembrane
proteins is associated with germ cell specification in mice.";
BMC Dev. Biol. 3:1-1(2003).
[8]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=16326387; DOI=10.1016/j.devcel.2005.10.010;
Tanaka S.S., Yamaguchi Y.L., Tsoi B., Lickert H., Tam P.P.;
"IFITM/Mil/fragilis family proteins IFITM1 and IFITM3 play distinct
roles in mouse primordial germ cell homing and repulsion.";
Dev. Cell 9:745-756(2005).
[9]
INTERACTION WITH CD81.
PubMed=16395393; DOI=10.1038/sj.gene.6364278;
Smith R.A., Young J., Weis J.J., Weis J.H.;
"Expression of the mouse fragilis gene products in immune cells and
association with receptor signaling complexes.";
Genes Immun. 7:113-121(2006).
[10]
FUNCTION.
PubMed=18505827; DOI=10.1128/MCB.00272-08;
Lange U.C., Adams D.J., Lee C., Barton S., Schneider R., Bradley A.,
Surani M.A.;
"Normal germ line establishment in mice carrying a deletion of the
Ifitm/Fragilis gene family cluster.";
Mol. Cell. Biol. 28:4688-4696(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-27, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
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).
[14]
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).
[15]
FUNCTION, AND INTERACTION WITH ATP6V0B.
PubMed=22467717; DOI=10.1177/1753425912443392;
Wee Y.S., Roundy K.M., Weis J.J., Weis J.H.;
"Interferon-inducible transmembrane proteins of the innate immune
response act as membrane organizers by influencing clathrin and v-
ATPase localization and function.";
Inn. Immun. 18:834-845(2012).
[16]
INVOLVEMENT IN SUSCEPTIBILITY TO SEVERE INFLUENZA INFECTION.
PubMed=22446628; DOI=10.1038/nature10921;
Everitt A.R., Clare S., Pertel T., John S.P., Wash R.S., Smith S.E.,
Chin C.R., Feeley E.M., Sims J.S., Adams D.J., Wise H.M., Kane L.,
Goulding D., Digard P., Anttila V., Baillie J.K., Walsh T.S.,
Hume D.A., Palotie A., Xue Y., Colonna V., Tyler-Smith C., Dunning J.,
Gordon S.B., Smyth R.L., Openshaw P.J., Dougan G., Brass A.L.,
Kellam P.;
"IFITM3 restricts the morbidity and mortality associated with
influenza.";
Nature 484:519-523(2012).
[17]
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).
-!- 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) and Ebola virus (EBOV), Dengue virus (DNV), West Nile virus
(WNV) and human immunodeficiency virus type 1 (HIV-1). Can
inhibit: influenza virus hemagglutinin protein-mediated viral
entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S
protein-mediated viral entry. Plays a critical role in the
structural stability and function of vacuolar ATPase (v-ATPase).
Establishes physical contact with the v-ATPase of endosomes which
is critical for proper clathrin localization and is also required
for the function of the v-ATPase to lower the pH in phagocytic
endosomes thus establishing an antiviral state. Involved in
initiating germ cell competence and specification, and in the
demarcation of PGCs from their somatic neighbors.
{ECO:0000269|PubMed:12124616, ECO:0000269|PubMed:18505827,
ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22467717}.
-!- SUBUNIT: Interacts with SPP1; the interaction reduces OPN
expression (By similarity). Interacts with ATP6V0B and CD81.
{ECO:0000250, ECO:0000269|PubMed:16395393,
ECO:0000269|PubMed:22467717}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein. Late endosome membrane {ECO:0000250}; Single-pass type II
membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in acinar cell. Predominantly
expressed in nascent primordial germ cells, as well as in gonadal
germ cells. {ECO:0000269|PubMed:12659663,
ECO:0000269|PubMed:15184081}.
-!- DEVELOPMENTAL STAGE: At E7.25 strong expression is found at the
base of the incipient allantois and weak expression in the
mesodermal portion of the posterior amnion, and, importantly, the
expression did not extend to the allantois. Expression persisted
until the late bud stage (E7.5), but gradually faded around the
early head fold stage (E7.75). At an earlier stage, only weak
expression is seen throughout the epiblast in E6.0. But around
E6.25-E6.5 (before gastrulation), marked expression is evident
within the most proximal layer of the epiblast that is in intimate
contact with the extraembryonic ectoderm. Expression is indeed
induced by extraembryonic ectoderm through signaling molecules.
During germ cell formation, is expressed in putative PGC ancestors
in embryos at 6.5-7.5 dpc. In migrating PGCs, expression is
continuous. After the beginning of gastrulation, the expression
migrates to the posterior end of the developing primitive streak
at the early/mid streak stage and became very intense in the
position where PGCs (Primordial germ cells) differentiate from
late streak stage onward. {ECO:0000269|PubMed:12124616,
ECO:0000269|PubMed:14516695, ECO:0000269|PubMed:16326387}.
-!- INDUCTION: By alpha interferon. Induced in pancreas during
caerulein-induced pancreatitis. Induced in pancreas under
systemic-lipopolysaccharide treatment and in intestine under
Salmonella infection. {ECO:0000269|PubMed:15184081}.
-!- PTM: Polyubiquitinated with both 'Lys-48' and 'Lys-63' linkages.
Ubiquitination negatively regulates antiviral activity. Lys-24 is
the most prevalent ubiquitination site (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
-!- CAUTION: It has been previously shown that mediates migration of
early primordial germ cells (PGCs) (PubMed:16326387). But
according to PubMed:16326387, have no detectable effects on
development of the germ line or on the generation of live young,
hence, is not essential for PGC migration.
{ECO:0000305|PubMed:16326387}.
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EMBL; AY082484; AAM03316.1; -; mRNA.
EMBL; AY594690; AAT06089.1; -; mRNA.
EMBL; AK003407; BAB22771.1; -; mRNA.
EMBL; AK007916; BAB25347.1; -; mRNA.
EMBL; AK007919; BAB25350.1; -; mRNA.
EMBL; AK151890; BAE30774.1; -; mRNA.
EMBL; CH466531; EDL17977.1; -; Genomic_DNA.
EMBL; BC010291; AAH10291.1; -; mRNA.
CCDS; CCDS21996.1; -.
RefSeq; NP_079654.1; NM_025378.2.
UniGene; Mm.141021; -.
BioGrid; 211244; 3.
IntAct; Q9CQW9; 3.
MINT; MINT-1870107; -.
STRING; 10090.ENSMUSP00000026565; -.
iPTMnet; Q9CQW9; -.
PhosphoSitePlus; Q9CQW9; -.
SwissPalm; Q9CQW9; -.
EPD; Q9CQW9; -.
MaxQB; Q9CQW9; -.
PaxDb; Q9CQW9; -.
PeptideAtlas; Q9CQW9; -.
PRIDE; Q9CQW9; -.
Ensembl; ENSMUST00000026565; ENSMUSP00000026565; ENSMUSG00000025492.
GeneID; 66141; -.
KEGG; mmu:66141; -.
UCSC; uc009kjc.1; mouse.
CTD; 10410; -.
MGI; MGI:1913391; Ifitm3.
eggNOG; ENOG410J2DU; Eukaryota.
eggNOG; ENOG4112C1U; LUCA.
GeneTree; ENSGT00390000003476; -.
HOGENOM; HOG000115781; -.
HOVERGEN; HBG001182; -.
InParanoid; Q9CQW9; -.
KO; K06566; -.
OMA; VLIFQAY; -.
OrthoDB; EOG091G1143; -.
PhylomeDB; Q9CQW9; -.
TreeFam; TF334894; -.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
ChiTaRS; Ifitm3; mouse.
PRO; PR:Q9CQW9; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000025492; -.
Genevisible; Q9CQW9; MM.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0051607; P:defense response to virus; IDA:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
GO; GO:0032897; P:negative regulation of viral transcription; ISO:MGI.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:MGI.
GO; GO:0035455; P:response to interferon-alpha; ISO:MGI.
GO; GO:0035456; P:response to interferon-beta; ISO:MGI.
GO; GO:0034341; P:response to interferon-gamma; ISO:MGI.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; IDA:MGI.
InterPro; IPR007593; CD225/Dispanin_fam.
Pfam; PF04505; CD225; 1.
1: Evidence at protein level;
Antiviral defense; Cell membrane; Complete proteome; Endosome;
Immunity; Innate immunity; Isopeptide bond; Lipoprotein; Lysosome;
Membrane; Palmitate; Phosphoprotein; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 137 Interferon-induced transmembrane protein
3.
/FTId=PRO_0000398567.
TOPO_DOM 1 57 Cytoplasmic. {ECO:0000255}.
INTRAMEM 58 78 Helical. {ECO:0000255}.
TOPO_DOM 79 109 Cytoplasmic. {ECO:0000255}.
TRANSMEM 110 130 Helical. {ECO:0000255}.
TOPO_DOM 131 137 Extracellular. {ECO:0000255}.
REGION 60 93 Interaction with SPP1. {ECO:0000250}.
MOD_RES 27 27 Phosphotyrosine.
{ECO:0000244|PubMed:19144319}.
LIPID 71 71 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 72 72 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 105 105 S-palmitoyl cysteine. {ECO:0000250}.
CROSSLNK 24 24 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q01628}.
CROSSLNK 83 83 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q01628}.
CROSSLNK 88 88 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q01628}.
CROSSLNK 104 104 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q01628}.
CONFLICT 130 130 L -> F (in Ref. 3; BAB25347).
{ECO:0000305}.
SEQUENCE 137 AA; 14954 MW; 4BEBED26E38D3511 CRC64;
MNHTSQAFIT AASGGQPPNY ERIKEEYEVA EMGAPHGSAS VRTTVINMPR EVSVPDHVVW
SLFNTLFMNF CCLGFIAYAY SVKSRDRKMV GDVTGAQAYA STAKCLNIST LVLSILMVVI
TIVSVIIIVL NAQNLHT


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U1928m CLIA C-X-C motif chemokine 9,Cxcl9,Gamma-interferon-induced monokine,MIG,Mig,Monokine induced by interferon-gamma,Mouse,MuMIG,Mus musculus,Protein m119,Scyb9,Small-inducible cytokine B9 96T
E1928m ELISA kit C-X-C motif chemokine 9,Cxcl9,Gamma-interferon-induced monokine,MIG,Mig,Monokine induced by interferon-gamma,Mouse,MuMIG,Mus musculus,Protein m119,Scyb9,Small-inducible cytokine B9 96T
U1928m CLIA kit C-X-C motif chemokine 9,Cxcl9,Gamma-interferon-induced monokine,MIG,Mig,Monokine induced by interferon-gamma,Mouse,MuMIG,Mus musculus,Protein m119,Scyb9,Small-inducible cytokine B9 96T
EIAAB42834 Homo sapiens,Human,IFITMD2,Interferon-induced transmembrane domain-containing protein D2,TMEM233,Transmembrane protein 233
EIAAB11573 DnaJ homolog subfamily C member 3,DNAJC3,Homo sapiens,Human,Interferon-induced, double-stranded RNA-activated protein kinase inhibitor,P58IPK,PRKRI,Protein kinase inhibitor of 58 kDa,Protein kinase in
EIAAB11571 Bos taurus,Bovine,DnaJ homolog subfamily C member 3,DNAJC3,Interferon-induced, double-stranded RNA-activated protein kinase inhibitor,P58IPK,Protein kinase inhibitor of 58 kDa,Protein kinase inhibitor


 

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