IFM3_MOUSE
ID IFM3_MOUSE Reviewed; 137 AA.
AC Q9CQW9; Q9D8L6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Interferon-induced transmembrane protein 3 {ECO:0000305};
DE AltName: Full=Dispanin subfamily A member 2b;
DE Short=DSPA2b;
DE AltName: Full=Fragilis protein;
DE AltName: Full=Interferon-inducible protein 15;
DE AltName: Full=Mouse ifitm-like protein 1;
DE Short=Mil-1;
GN Name=Ifitm3 {ECO:0000312|MGI:MGI:1913391};
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], AND DEVELOPMENTAL STAGE.
RX PubMed=14516695; DOI=10.1016/s0925-4773(03)00126-6;
RA Tanaka S.S., Matsui Y.;
RT "Developmentally regulated expression of mil-1 and mil-2, mouse interferon-
RT induced transmembrane protein like genes, during formation and
RT differentiation of primordial germ cells.";
RL Mech. Dev. 119:S261-S267(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=129/SvEv;
RX PubMed=12124616; DOI=10.1038/nature00927;
RA Saitou M., Barton S.C., Surani M.A.;
RT "A molecular programme for the specification of germ cell fate in mice.";
RL Nature 418:293-300(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=BALB/cJ;
RX PubMed=15184081; DOI=10.1016/j.bbrc.2004.05.085;
RA Ropolo A., Tomasini R., Grasso D., Dusetti N.J., Cerquetti M.C.,
RA Iovanna J.L., Vaccaro M.I.;
RT "Cloning of IP15, a pancreatitis-induced gene whose expression inhibits
RT cell growth.";
RL Biochem. Biophys. Res. Commun. 319:1001-1009(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Pancreas;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=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 [7]
RP TISSUE SPECIFICITY.
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 [8]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16326387; DOI=10.1016/j.devcel.2005.10.010;
RA Tanaka S.S., Yamaguchi Y.L., Tsoi B., Lickert H., Tam P.P.;
RT "IFITM/Mil/fragilis family proteins IFITM1 and IFITM3 play distinct roles
RT in mouse primordial germ cell homing and repulsion.";
RL Dev. Cell 9:745-756(2005).
RN [9]
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 [10]
RP FUNCTION.
RX PubMed=18505827; DOI=10.1128/mcb.00272-08;
RA Lange U.C., Adams D.J., Lee C., Barton S., Schneider R., Bradley A.,
RA Surani M.A.;
RT "Normal germ line establishment in mice carrying a deletion of the
RT Ifitm/Fragilis gene family cluster.";
RL Mol. Cell. Biol. 28:4688-4696(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-27, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [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.
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 [15]
RP FUNCTION, AND INTERACTION WITH ATP6V0B.
RX PubMed=22467717; DOI=10.1177/1753425912443392;
RA Wee Y.S., Roundy K.M., Weis J.J., Weis J.H.;
RT "Interferon-inducible transmembrane proteins of the innate immune response
RT act as membrane organizers by influencing clathrin and v-ATPase
RT localization and function.";
RL Inn. Immun. 18:834-845(2012).
RN [16]
RP INVOLVEMENT IN SUSCEPTIBILITY TO SEVERE INFLUENZA INFECTION.
RX PubMed=22446628; DOI=10.1038/nature10921;
RA Everitt A.R., Clare S., Pertel T., John S.P., Wash R.S., Smith S.E.,
RA Chin C.R., Feeley E.M., Sims J.S., Adams D.J., Wise H.M., Kane L.,
RA Goulding D., Digard P., Anttila V., Baillie J.K., Walsh T.S., Hume D.A.,
RA Palotie A., Xue Y., Colonna V., Tyler-Smith C., Dunning J., Gordon S.B.,
RA Smyth R.L., Openshaw P.J., Dougan G., Brass A.L., Kellam P.;
RT "IFITM3 restricts the morbidity and mortality associated with influenza.";
RL Nature 484:519-523(2012).
RN [17]
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 [18]
RP FUNCTION, MUTAGENESIS OF TYR-20; 71-CYS-CYS-72 AND CYS-105, AND SUBCELLULAR
RP LOCATION.
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).
CC -!- FUNCTION: IFN-induced antiviral protein which disrupts intracellular
CC cholesterol homeostasis. Inhibits the entry of viruses to the host cell
CC cytoplasm by preventing viral fusion with cholesterol depleted
CC endosomes. May inactivate new enveloped viruses which buds out of the
CC infected cell, by letting them go out with a cholesterol depleted
CC membrane. Active against multiple viruses, including influenza A virus,
CC SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV),
CC Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human
CC immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and
CC vesicular stomatitis virus (VSV) (PubMed:33270927). Can inhibit:
CC influenza virus hemagglutinin protein-mediated viral entry, MARV and
CC EBOV GP1,2-mediated viral entry, SARS-CoV and SARS-CoV-2 S protein-
CC mediated viral entry and VSV G protein-mediated viral entry
CC (PubMed:33270927). Plays a critical role in the structural stability
CC and function of vacuolar ATPase (v-ATPase). Establishes physical
CC contact with the v-ATPase of endosomes which is critical for proper
CC clathrin localization and is also required for the function of the v-
CC ATPase to lower the pH in phagocytic endosomes thus establishing an
CC antiviral state. In hepatocytes, IFITM proteins act in a coordinated
CC manner to restrict HCV infection by targeting the endocytosed HCV
CC virion for lysosomal degradation. 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. Exerts opposing activities on SARS-
CC CoV-2, including amphipathicity-dependent restriction of virus at
CC endosomes and amphipathicity-independent enhancement of infection at
CC the plasma membrane. {ECO:0000269|PubMed:12124616,
CC ECO:0000269|PubMed:18505827, ECO:0000269|PubMed:21253575,
CC ECO:0000269|PubMed:22467717, ECO:0000269|PubMed:33270927}.
CC -!- SUBUNIT: Interacts with ATP6V0B (PubMed:22467717). Interacts with CD81
CC (PubMed:16395393). Interacts with SPP1; the interaction reduces OPN
CC expression (By similarity). Interacts with BRI3 (By similarity).
CC {ECO:0000250|UniProtKB:Q01628, ECO:0000269|PubMed:16395393,
CC ECO:0000269|PubMed:22467717}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01628};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01628}.
CC Late endosome membrane {ECO:0000269|PubMed:33270927}; Single-pass type
CC II membrane protein {ECO:0000250|UniProtKB:Q01628}. Early endosome
CC membrane {ECO:0000269|PubMed:33270927}; Single-pass type II membrane
CC protein {ECO:0000250|UniProtKB:Q01628}. Lysosome membrane
CC {ECO:0000269|PubMed:33270927}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q01628}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q01628}. Note=Co-localizes with BRI3 isoform 1
CC at the perinuclear region. {ECO:0000250|UniProtKB:Q01628}.
CC -!- TISSUE SPECIFICITY: Expressed in acinar cell. Predominantly expressed
CC in nascent primordial germ cells, as well as in gonadal germ cells.
CC {ECO:0000269|PubMed:12659663, ECO:0000269|PubMed:15184081}.
CC -!- DEVELOPMENTAL STAGE: At 7.25 dpc strong expression is found at the base
CC of the incipient allantois and weak expression in the mesodermal
CC portion of the posterior amnion, and, importantly, the expression did
CC not extend to the allantois. Expression persisted until the late bud
CC stage (7.5 dpc), but gradually faded around the early head fold stage
CC (7.75 dpc). At an earlier stage, only weak expression is seen
CC throughout the epiblast in 6.0 dpc. But around 6.25-6.5 dpc (before
CC gastrulation), marked expression is evident within the most proximal
CC layer of the epiblast that is in intimate contact with the
CC extraembryonic ectoderm. Expression is indeed induced by extraembryonic
CC ectoderm through signaling molecules. During germ cell formation, is
CC expressed in putative PGC ancestors in embryos at 6.5-7.5 dpc. In
CC migrating PGCs, expression is continuous. After the beginning of
CC gastrulation, the expression migrates to the posterior end of the
CC developing primitive streak at the early/mid streak stage and became
CC very intense in the position where PGCs (Primordial germ cells)
CC differentiate from late streak stage onward.
CC {ECO:0000269|PubMed:12124616, ECO:0000269|PubMed:14516695,
CC ECO:0000269|PubMed:16326387}.
CC -!- INDUCTION: By alpha interferon. Induced in pancreas during caerulein-
CC induced pancreatitis. Induced in pancreas under systemic-
CC lipopolysaccharide treatment and in intestine under Salmonella
CC infection. {ECO:0000269|PubMed:15184081}.
CC -!- PTM: Polyubiquitinated with both 'Lys-48' and 'Lys-63' linkages.
CC Ubiquitination negatively regulates antiviral activity. Lys-24 is the
CC most prevalent ubiquitination site. {ECO:0000250|UniProtKB:Q01628}.
CC -!- PTM: Phosphorylation at Tyr-20 is required for endosomal and lysosomal
CC location. {ECO:0000250|UniProtKB:Q01628}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
CC -!- CAUTION: It has been previously shown that mediates migration of early
CC primordial germ cells (PGCs) (PubMed:16326387). But according to
CC PubMed:16326387, have no detectable effects on development of the germ
CC line or on the generation of live young, hence, is not essential for
CC PGC migration. {ECO:0000305|PubMed:16326387}.
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DR EMBL; AY082484; AAM03316.1; -; mRNA.
DR EMBL; AY594690; AAT06089.1; -; mRNA.
DR EMBL; AK003407; BAB22771.1; -; mRNA.
DR EMBL; AK007916; BAB25347.1; -; mRNA.
DR EMBL; AK007919; BAB25350.1; -; mRNA.
DR EMBL; AK151890; BAE30774.1; -; mRNA.
DR EMBL; CH466531; EDL17977.1; -; Genomic_DNA.
DR EMBL; BC010291; AAH10291.1; -; mRNA.
DR CCDS; CCDS21996.1; -.
DR RefSeq; NP_079654.1; NM_025378.2.
DR AlphaFoldDB; Q9CQW9; -.
DR BioGRID; 211244; 7.
DR STRING; 10090.ENSMUSP00000026565; -.
DR iPTMnet; Q9CQW9; -.
DR PhosphoSitePlus; Q9CQW9; -.
DR SwissPalm; Q9CQW9; -.
DR EPD; Q9CQW9; -.
DR jPOST; Q9CQW9; -.
DR MaxQB; Q9CQW9; -.
DR PaxDb; Q9CQW9; -.
DR PeptideAtlas; Q9CQW9; -.
DR PRIDE; Q9CQW9; -.
DR ProteomicsDB; 267199; -.
DR DNASU; 66141; -.
DR Ensembl; ENSMUST00000026565; ENSMUSP00000026565; ENSMUSG00000025492.
DR GeneID; 66141; -.
DR KEGG; mmu:66141; -.
DR UCSC; uc009kjc.1; mouse.
DR CTD; 10410; -.
DR MGI; MGI:1913391; Ifitm3.
DR VEuPathDB; HostDB:ENSMUSG00000025492; -.
DR eggNOG; ENOG502S9XK; Eukaryota.
DR GeneTree; ENSGT00950000182857; -.
DR HOGENOM; CLU_124511_3_0_1; -.
DR InParanoid; Q9CQW9; -.
DR OMA; RIACILN; -.
DR OrthoDB; 1555189at2759; -.
DR PhylomeDB; Q9CQW9; -.
DR TreeFam; TF334894; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 66141; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Ifitm3; mouse.
DR PRO; PR:Q9CQW9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CQW9; protein.
DR Bgee; ENSMUSG00000025492; Expressed in aortic valve and 256 other tissues.
DR Genevisible; Q9CQW9; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; IDA:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; 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:0006898; P:receptor-mediated endocytosis; IMP:MGI.
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; IDA:MGI.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Cell membrane; Cytoplasm; Endosome; Immunity;
KW Innate immunity; Isopeptide bond; Lipoprotein; Lysosome; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..137
FT /note="Interferon-induced transmembrane protein 3"
FT /id="PRO_0000398567"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 60..93
FT /note="Interaction with SPP1"
FT /evidence="ECO:0000250|UniProtKB:Q01628"
FT REGION 108..133
FT /note="Interaction with VAPA"
FT /evidence="ECO:0000250|UniProtKB:Q01628"
FT MOD_RES 20
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01628"
FT MOD_RES 27
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT LIPID 71
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q01628"
FT LIPID 72
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q01628"
FT LIPID 105
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q01628"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q01628"
FT CROSSLNK 83
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q01628"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q01628"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q01628"
FT MUTAGEN 20
FT /note="Y->A: Accumulates at the plasma membrane. No effect
FT on anti-SARS-CoV-2 activity."
FT /evidence="ECO:0000269|PubMed:33270927"
FT MUTAGEN 71..72
FT /note="CC->AA: No effect on SARS-CoV-2 infection; when
FT associated with A-105."
FT /evidence="ECO:0000269|PubMed:33270927"
FT MUTAGEN 105
FT /note="C->A: No effect on SARS-CoV-2 infection; when
FT associated with 71-A-A-72."
FT /evidence="ECO:0000269|PubMed:33270927"
FT CONFLICT 130
FT /note="L -> F (in Ref. 3; BAB25347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 137 AA; 14954 MW; 4BEBED26E38D3511 CRC64;
MNHTSQAFIT AASGGQPPNY ERIKEEYEVA EMGAPHGSAS VRTTVINMPR EVSVPDHVVW
SLFNTLFMNF CCLGFIAYAY SVKSRDRKMV GDVTGAQAYA STAKCLNIST LVLSILMVVI
TIVSVIIIVL NAQNLHT
