IFM3_RAT
ID IFM3_RAT Reviewed; 137 AA.
AC P26376; B5DER6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Interferon-induced transmembrane protein 3 {ECO:0000305};
DE AltName: Full=Dispanin subfamily A member 2b;
DE Short=DSPA2b;
GN Name=ifitm3 {ECO:0000312|EMBL:CAA43655.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=1639276; DOI=10.1016/0378-1119(92)90739-c;
RA Hayzer D.J., Brinson E., Runge M.S.;
RT "A rat beta-interferon-induced mRNA: sequence characterization.";
RL Gene 117:277-278(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 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. Plays a critical role in the
CC structural stability and function of vacuolar ATPase (v-ATPase).
CC Establishes physical contact with the v-ATPase of endosomes which is
CC critical for proper clathrin localization and is also required for the
CC function of the v-ATPase to lower the pH in phagocytic endosomes thus
CC establishing an antiviral state. {ECO:0000250|UniProtKB:Q01628,
CC ECO:0000250|UniProtKB:Q9CQW9}.
CC -!- SUBUNIT: Interacts with ATP6V0B (By similarity). Interacts with CD81
CC (By similarity). Interacts with SPP1; the interaction reduces OPN
CC expression (By similarity). Interacts with BRI3 (By similarity).
CC {ECO:0000250|UniProtKB:Q01628, ECO:0000250|UniProtKB:Q9CQW9}.
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:0000250|UniProtKB:Q01628}; Single-pass type
CC II membrane protein {ECO:0000250|UniProtKB:Q01628}. Early endosome
CC membrane {ECO:0000250|UniProtKB:Q01628}; Single-pass type II membrane
CC protein {ECO:0000250|UniProtKB:Q01628}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q01628}; 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 -!- INDUCTION: By interferon beta. {ECO:0000269|PubMed:1639276}.
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}.
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DR EMBL; X61381; CAA43655.1; -; mRNA.
DR EMBL; BC168774; AAI68774.1; -; mRNA.
DR EMBL; CH473953; EDM11956.1; -; Genomic_DNA.
DR PIR; JC1241; JC1241.
DR RefSeq; NP_001129596.1; NM_001136124.1.
DR AlphaFoldDB; P26376; -.
DR BioGRID; 262866; 1.
DR IntAct; P26376; 1.
DR STRING; 10116.ENSRNOP00000020265; -.
DR iPTMnet; P26376; -.
DR PhosphoSitePlus; P26376; -.
DR PaxDb; P26376; -.
DR PRIDE; P26376; -.
DR Ensembl; ENSRNOT00000020265; ENSRNOP00000020265; ENSRNOG00000015078.
DR GeneID; 361673; -.
DR KEGG; rno:361673; -.
DR CTD; 10410; -.
DR eggNOG; ENOG502S9XK; Eukaryota.
DR GeneTree; ENSGT00950000182857; -.
DR HOGENOM; CLU_124511_3_0_1; -.
DR InParanoid; P26376; -.
DR OMA; RIACILN; -.
DR OrthoDB; 1555189at2759; -.
DR PhylomeDB; P26376; -.
DR TreeFam; TF334894; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR PRO; PR:P26376; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000015078; Expressed in ovary and 20 other tissues.
DR Genevisible; P26376; RN.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
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:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISS: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:0060337; P:type I interferon signaling pathway; IBA:GO_Central.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Cell membrane; Cytoplasm; Endosome; Isopeptide bond;
KW Lipoprotein; Lysosome; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..137
FT /note="Interferon-induced transmembrane protein 3"
FT /id="PRO_0000153730"
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:0000250|UniProtKB:Q9CQW9"
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"
SQ SEQUENCE 137 AA; 14971 MW; 9D3F92264E0C0FC2 CRC64;
MNHTSQAFVN AATGGQPPNY ERIKEEYEVS ELGAPHGSAS VRTTVINMPR EVSVPDHVVW
SLFNTLFMNF CCLGFIAYAY SVKSRDRKMV GDMTGAQAYA STAKCLNISS LVLSILMVII
TIVTVVIIAL NAPRLQT
