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Interferon-induced transmembrane protein 3 (Dispanin subfamily A member 2b) (DSPA2b) (Interferon-inducible protein 1-8U)

 IFM3_HUMAN              Reviewed;         133 AA.
Q01628; Q53Y76; Q96HK8; Q96J15;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 2.
28-FEB-2018, entry version 150.
RecName: Full=Interferon-induced transmembrane protein 3;
AltName: Full=Dispanin subfamily A member 2b;
Short=DSPA2b;
AltName: Full=Interferon-inducible protein 1-8U;
Name=IFITM3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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 [GENOMIC DNA], AND 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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-3.
TISSUE=Brain, Cervix, and Vascular endothelial cell;
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).
[8]
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).
[9]
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).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INVOLVEMENT IN SUSCEPTIBILITY TO
SEVERE INFLUENZA INFECTION.
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).
[11]
INTERACTION WITH SPP1.
PubMed=19901966; DOI=10.1038/onc.2009.379;
El-Tanani M.K., Jin D., Campbell F.C., Johnston P.G.;
"Interferon-induced transmembrane 3 binds osteopontin in vitro:
expressed in vivo IFITM3 reduced OPN expression.";
Oncogene 29:752-762(2010).
[12]
PALMITOYLATION AT CYS-71; CYS-72 AND CYS-105.
PubMed=20601941; DOI=10.1038/nchembio.405;
Yount J.S., Moltedo B., Yang Y.Y., Charron G., Moran T.M., Lopez C.B.,
Hang H.C.;
"Palmitoylome profiling reveals S-palmitoylation-dependent antiviral
activity of IFITM3.";
Nat. Chem. Biol. 6:610-614(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=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).
[15]
ERRATUM.
Lu J., Pan Q., Rong L., He W., Liu S.L., Liang C.;
J. Virol. 85:4043-4043(2011).
[16]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22046135; DOI=10.1371/journal.ppat.1002337;
Feeley E.M., Sims J.S., John S.P., Chin C.R., Pertel T., Chen L.M.,
Gaiha G.D., Ryan B.J., Donis R.O., Elledge S.J., Brass A.L.;
"IFITM3 inhibits influenza A virus infection by preventing cytosolic
entry.";
PLoS Pathog. 7:E1002337-E1002337(2011).
[17]
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).
[18]
UBIQUITINATION AT LYS-24; LYS-83; LYS-88 AND LYS-104, PALMITOYLATION,
TOPOLOGY, LACK OF GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=22511783; DOI=10.1074/jbc.M112.362095;
Yount J.S., Karssemeijer R.A., Hang H.C.;
"S-palmitoylation and ubiquitination differentially regulate
interferon-induced transmembrane protein 3 (IFITM3)-mediated
resistance to influenza virus.";
J. Biol. Chem. 287:19631-19641(2012).
[19]
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).
[20]
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).
[21]
FUNCTION, AND INTERACTION WITH VAPA.
PubMed=23601107; DOI=10.1016/j.chom.2013.03.006;
Amini-Bavil-Olyaee S., Choi Y.J., Lee J.H., Shi M., Huang I.C.,
Farzan M., Jung J.U.;
"The antiviral effector IFITM3 disrupts intracellular cholesterol
homeostasis to block viral entry.";
Cell Host Microbe 13:452-464(2013).
-!- FUNCTION: IFN-induced antiviral protein which disrupts
intracellular cholesterol homeostasis. Inhibits the entry of
viruses to the host cell cytoplasm by preventing viral fusion with
cholesterol depleted endosomes. May inactivate new enveloped
viruses which buds out of the infected cell, by letting them go
out with a cholesterol depleted membrane. 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), 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. 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.
{ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20534863,
ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21177806,
ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22046135,
ECO:0000269|PubMed:22479637, ECO:0000269|PubMed:23601107}.
-!- SUBUNIT: Interacts with ATP6V0B and CD81 (By similarity).
Interacts with SPP1; the interaction reduces OPN expression.
Interacts with VAPA. {ECO:0000250, ECO:0000269|PubMed:19901966,
ECO:0000269|PubMed:23601107}.
-!- INTERACTION:
P43490:NAMPT; NbExp=3; IntAct=EBI-7932862, EBI-2829310;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein. Late endosome membrane; Single-pass type II membrane
protein. Lysosome membrane; Single-pass type II membrane protein.
-!- INDUCTION: By IFN-alpha and IFNG/IFN-gamma.
-!- PTM: Palmitoylation on membrane-proximal cysteines controls
clustering in membrane compartments and antiviral activity against
influenza virus. {ECO:0000269|PubMed:20601941,
ECO:0000269|PubMed:22511783}.
-!- PTM: Not glycosylated.
-!- PTM: Polyubiquitinated with both 'Lys-48' and 'Lys-63' linkages.
Ubiquitination negatively regulates antiviral activity. Lys-24 is
the most prevalent ubiquitination site.
{ECO:0000269|PubMed:22511783}.
-!- POLYMORPHISM: Genetic variations in IFITM3 are responsible for
susceptibility to severe influenza virus infection [MIM:614680].
{ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:22446628}.
-!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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EMBL; X57352; CAA40626.1; -; mRNA.
EMBL; JQ610571; AFF60305.1; -; Genomic_DNA.
EMBL; JQ610572; AFF60306.1; -; Genomic_DNA.
EMBL; JQ610573; AFF60307.1; -; Genomic_DNA.
EMBL; JQ610574; AFF60308.1; -; Genomic_DNA.
EMBL; JQ610575; AFF60309.1; -; Genomic_DNA.
EMBL; JQ610576; AFF60310.1; -; Genomic_DNA.
EMBL; JQ610577; AFF60311.1; -; Genomic_DNA.
EMBL; JQ610578; AFF60312.1; -; Genomic_DNA.
EMBL; JQ610579; AFF60313.1; -; Genomic_DNA.
EMBL; JQ610580; AFF60314.1; -; Genomic_DNA.
EMBL; JQ610581; AFF60315.1; -; Genomic_DNA.
EMBL; JQ610582; AFF60316.1; -; Genomic_DNA.
EMBL; JQ610583; AFF60317.1; -; Genomic_DNA.
EMBL; JQ610585; AFF60319.1; -; Genomic_DNA.
EMBL; JQ610586; AFF60320.1; -; Genomic_DNA.
EMBL; JQ610587; AFF60321.1; -; Genomic_DNA.
EMBL; JQ610588; AFF60322.1; -; Genomic_DNA.
EMBL; JQ610589; AFF60323.1; -; Genomic_DNA.
EMBL; JQ610590; AFF60324.1; -; Genomic_DNA.
EMBL; JQ610591; AFF60325.1; -; Genomic_DNA.
EMBL; JQ610592; AFF60326.1; -; Genomic_DNA.
EMBL; JQ610593; AFF60327.1; -; Genomic_DNA.
EMBL; JQ610594; AFF60328.1; -; Genomic_DNA.
EMBL; JQ610595; AFF60329.1; -; Genomic_DNA.
EMBL; JQ610596; AFF60330.1; -; Genomic_DNA.
EMBL; JQ610597; AFF60331.1; -; Genomic_DNA.
EMBL; JQ610598; AFF60332.1; -; Genomic_DNA.
EMBL; JQ610599; AFF60333.1; -; Genomic_DNA.
EMBL; JQ610600; AFF60334.1; -; Genomic_DNA.
EMBL; JQ610601; AFF60335.1; -; Genomic_DNA.
EMBL; JQ610602; AFF60336.1; -; Genomic_DNA.
EMBL; JQ610603; AFF60337.1; -; Genomic_DNA.
EMBL; JQ610604; AFF60338.1; -; Genomic_DNA.
EMBL; JQ610605; AFF60339.1; -; Genomic_DNA.
EMBL; JQ610606; AFF60340.1; -; Genomic_DNA.
EMBL; JQ610607; AFF60341.1; -; Genomic_DNA.
EMBL; JQ610608; AFF60342.1; -; Genomic_DNA.
EMBL; JQ610609; AFF60343.1; -; Genomic_DNA.
EMBL; JQ610610; AFF60344.1; -; Genomic_DNA.
EMBL; JQ610611; AFF60345.1; -; Genomic_DNA.
EMBL; JQ610613; AFF60347.1; -; Genomic_DNA.
EMBL; JQ610614; AFF60348.1; -; Genomic_DNA.
EMBL; JQ610615; AFF60349.1; -; Genomic_DNA.
EMBL; JQ610616; AFF60350.1; -; Genomic_DNA.
EMBL; JQ610617; AFF60351.1; -; Genomic_DNA.
EMBL; JQ610618; AFF60352.1; -; Genomic_DNA.
EMBL; JQ610620; AFF60354.1; -; Genomic_DNA.
EMBL; JQ610621; AFF60355.1; -; Genomic_DNA.
EMBL; BT006892; AAP35538.1; -; mRNA.
EMBL; AK292173; BAF84862.1; -; mRNA.
EMBL; AC136475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH891444; EAW50866.1; -; Genomic_DNA.
EMBL; BC006794; AAH06794.1; -; mRNA.
EMBL; BC008417; AAH08417.1; -; mRNA.
EMBL; BC022439; AAH22439.1; -; mRNA.
EMBL; BC070243; AAH70243.1; -; mRNA.
CCDS; CCDS41585.1; -.
PIR; S17182; S17182.
RefSeq; NP_066362.2; NM_021034.2.
UniGene; Hs.374650; -.
ProteinModelPortal; Q01628; -.
BioGrid; 115681; 6.
IntAct; Q01628; 4.
MINT; Q01628; -.
STRING; 9606.ENSP00000382707; -.
TCDB; 8.A.58.1.3; the dispanin (dispanin) family.
iPTMnet; Q01628; -.
PhosphoSitePlus; Q01628; -.
SwissPalm; Q01628; -.
BioMuta; IFITM3; -.
DMDM; 20178301; -.
EPD; Q01628; -.
PaxDb; Q01628; -.
PeptideAtlas; Q01628; -.
PRIDE; Q01628; -.
TopDownProteomics; Q01628; -.
DNASU; 10410; -.
Ensembl; ENST00000399808; ENSP00000382707; ENSG00000142089.
GeneID; 10410; -.
KEGG; hsa:10410; -.
UCSC; uc001lpa.3; human.
CTD; 10410; -.
DisGeNET; 10410; -.
EuPathDB; HostDB:ENSG00000142089.15; -.
GeneCards; IFITM3; -.
HGNC; HGNC:5414; IFITM3.
HPA; HPA004337; -.
MalaCards; IFITM3; -.
MIM; 605579; gene.
MIM; 614680; phenotype.
neXtProt; NX_Q01628; -.
OpenTargets; ENSG00000142089; -.
PharmGKB; PA29655; -.
eggNOG; ENOG410J2DU; Eukaryota.
eggNOG; ENOG4112C1U; LUCA.
GeneTree; ENSGT00390000003476; -.
HOGENOM; HOG000115781; -.
HOVERGEN; HBG001182; -.
InParanoid; Q01628; -.
KO; K06566; -.
OMA; VLIFQAY; -.
OrthoDB; EOG091G1143; -.
PhylomeDB; Q01628; -.
TreeFam; TF334894; -.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
ChiTaRS; IFITM3; human.
GeneWiki; IFITM3; -.
GenomeRNAi; 10410; -.
PRO; PR:Q01628; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000142089; -.
CleanEx; HS_IFITM3; -.
ExpressionAtlas; Q01628; baseline and differential.
Genevisible; Q01628; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
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:0032897; P:negative regulation of viral transcription; 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;
Antiviral defense; Cell membrane; Complete proteome; Endosome;
Immunity; Innate immunity; Isopeptide bond; Lipoprotein; Lysosome;
Membrane; Palmitate; Polymorphism; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 133 Interferon-induced transmembrane protein
3.
/FTId=PRO_0000153729.
TOPO_DOM 1 57 Cytoplasmic. {ECO:0000255}.
INTRAMEM 58 78 Helical. {ECO:0000255}.
TOPO_DOM 79 107 Cytoplasmic. {ECO:0000255}.
TRANSMEM 108 128 Helical. {ECO:0000255}.
TOPO_DOM 129 133 Extracellular. {ECO:0000255}.
REGION 60 93 Interaction with SPP1.
{ECO:0000269|PubMed:19901966}.
REGION 108 133 Interaction with VAPA.
{ECO:0000269|PubMed:23601107}.
LIPID 71 71 S-palmitoyl cysteine.
{ECO:0000269|PubMed:20601941}.
LIPID 72 72 S-palmitoyl cysteine.
{ECO:0000269|PubMed:20601941}.
LIPID 105 105 S-palmitoyl cysteine.
{ECO:0000269|PubMed:20601941}.
CROSSLNK 24 24 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22511783}.
CROSSLNK 83 83 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22511783}.
CROSSLNK 88 88 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22511783}.
CROSSLNK 104 104 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22511783}.
VARIANT 3 3 H -> Q (in dbSNP:rs1136853).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_053810.
CONFLICT 2 2 N -> S (in Ref. 1; CAA40626).
{ECO:0000305}.
CONFLICT 34 34 A -> G (in Ref. 1; CAA40626).
{ECO:0000305}.
SEQUENCE 133 AA; 14632 MW; 9FFB2E4623F7A1DD CRC64;
MNHTVQTFFS PVNSGQPPNY EMLKEEHEVA VLGAPHNPAP PTSTVIHIRS ETSVPDHVVW
SLFNTLFMNP CCLGFIAFAY SVKSRDRKMV GDVTGAQAYA STAKCLNIWA LILGILMTIL
LIVIPVLIFQ AYG


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