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IFIH1_MOUSE
ID   IFIH1_MOUSE             Reviewed;        1025 AA.
AC   Q8R5F7; A2AUY7; Q3U6S2; Q68EM4; Q8BYC9; Q8BZ01; Q8K5C7; Q8R144; Q8VE79;
AC   Q99KS4; Q9D2Z5;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Interferon-induced helicase C domain-containing protein 1;
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9BYX4};
DE   AltName: Full=Helicase with 2 CARD domains;
DE            Short=Helicard;
DE   AltName: Full=Interferon induced with helicase C domain protein 1;
DE   AltName: Full=Melanoma differentiation-associated protein 5;
DE            Short=MDA-5;
DE   AltName: Full=RIG-I-like receptor 2;
DE            Short=RLR-2;
GN   Name=Ifih1 {ECO:0000312|MGI:MGI:1918836};
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] (ISOFORM 1), FUNCTION, CLEAVAGE SITES,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12015121; DOI=10.1016/s0960-9822(02)00842-4;
RA   Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K.,
RA   Tschopp J.;
RT   "Overexpression of Helicard, a CARD-containing helicase cleaved during
RT   apoptosis, accelerates DNA degradation.";
RL   Curr. Biol. 12:838-843(2002).
RN   [2]
RP   ERRATUM OF PUBMED:12015121.
RA   Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K.,
RA   Tschopp J.;
RL   Curr. Biol. 12:1633-1633(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=11805321; DOI=10.1073/pnas.022637199;
RA   Kang D.-C., Gopalkrishnan R.V., Wu Q., Jankowsky E., Pyle A.M.,
RA   Fisher P.B.;
RT   "mda-5: an interferon-inducible putative RNA helicase with double-stranded
RT   RNA-dependent ATPase activity and melanoma growth-suppressive properties.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:637-642(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Cecum, Thymus, and Vagina;
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].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   FUNCTION.
RX   PubMed=16625202; DOI=10.1038/nature04734;
RA   Kato H., Takeuchi O., Sato S., Yoneyama M., Yamamoto M., Matsui K.,
RA   Uematsu S., Jung A., Kawai T., Ishii K.J., Yamaguchi O., Otsu K.,
RA   Tsujimura T., Koh C.S., Reis e Sousa C., Matsuura Y., Fujita T., Akira S.;
RT   "Differential roles of MDA5 and RIG-I helicases in the recognition of RNA
RT   viruses.";
RL   Nature 441:101-105(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-648, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   FUNCTION.
RX   PubMed=17942531; DOI=10.1128/jvi.01080-07;
RA   Loo Y.M., Fornek J., Crochet N., Bajwa G., Perwitasari O.,
RA   Martinez-Sobrido L., Akira S., Gill M.A., Garcia-Sastre A., Katze M.G.,
RA   Gale M. Jr.;
RT   "Distinct RIG-I and MDA5 signaling by RNA viruses in innate immunity.";
RL   J. Virol. 82:335-345(2008).
RN   [10]
RP   IDENTIFICATION BY 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   [11]
RP   FUNCTION.
RX   PubMed=19656871; DOI=10.1128/jvi.00770-09;
RA   Pichlmair A., Schulz O., Tan C.P., Rehwinkel J., Kato H., Takeuchi O.,
RA   Akira S., Way M., Schiavo G., Reis e Sousa C.;
RT   "Activation of MDA5 requires higher-order RNA structures generated during
RT   virus infection.";
RL   J. Virol. 83:10761-10769(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-291; SER-302;
RP   SER-645 AND SER-648, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC   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 ON FUNCTION.
RX   PubMed=21616437; DOI=10.1016/j.immuni.2011.05.003;
RA   Loo Y.M., Gale M. Jr.;
RT   "Immune signaling by RIG-I-like receptors.";
RL   Immunity 34:680-692(2011).
RN   [14]
RP   REVIEW ON FUNCTION.
RX   PubMed=21884169; DOI=10.1111/j.1600-065x.2011.01052.x;
RA   Kato H., Takahasi K., Fujita T.;
RT   "RIG-I-like receptors: cytoplasmic sensors for non-self RNA.";
RL   Immunol. Rev. 243:91-98(2011).
RN   [15]
RP   REVIEW ON FUNCTION.
RX   PubMed=20950133; DOI=10.1089/jir.2010.0057;
RA   Onoguchi K., Yoneyama M., Fujita T.;
RT   "Retinoic acid-inducible gene-I-like receptors.";
RL   J. Interferon Cytokine Res. 31:27-31(2011).
RN   [16]
RP   REVIEW ON FUNCTION.
RX   PubMed=21245900; DOI=10.1038/ni0211-114;
RA   Garcia-Sastre A.;
RT   "2 methylate or not 2 methylate: viral evasion of the type I interferon
RT   response.";
RL   Nat. Immunol. 12:114-115(2011).
RN   [17]
RP   FUNCTION.
RX   PubMed=21217758; DOI=10.1038/ni.1979;
RA   Zuest R., Cervantes-Barragan L., Habjan M., Maier R., Neuman B.W.,
RA   Ziebuhr J., Szretter K.J., Baker S.C., Barchet W., Diamond M.S.,
RA   Siddell S.G., Ludewig B., Thiel V.;
RT   "Ribose 2'-O-methylation provides a molecular signature for the distinction
RT   of self and non-self mRNA dependent on the RNA sensor Mda5.";
RL   Nat. Immunol. 12:137-143(2011).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 545-697, AND SUBUNIT.
RX   PubMed=22314235; DOI=10.1038/emboj.2012.19;
RA   Berke I.C., Modis Y.;
RT   "MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding
RT   double-stranded RNA.";
RL   EMBO J. 31:1714-1726(2012).
CC   -!- FUNCTION: Innate immune receptor which acts as a cytoplasmic sensor of
CC       viral nucleic acids and plays a major role in sensing viral infection
CC       and in the activation of a cascade of antiviral responses including the
CC       induction of type I interferons and pro-inflammatory cytokines. Its
CC       ligands include mRNA lacking 2'-O-methylation at their 5' cap and long-
CC       dsRNA (>1 kb in length). Upon ligand binding it associates with
CC       mitochondria antiviral signaling protein (MAVS/IPS1) which activates
CC       the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon
CC       regulatory factors: IRF3 and IRF7 which in turn activate transcription
CC       of antiviral immunological genes, including interferons (IFNs); IFN-
CC       alpha and IFN-beta. Responsible for detecting the Picornaviridae family
CC       members such as encephalomyocarditis virus (EMCV), mengo
CC       encephalomyocarditis virus (ENMG), and theiler's murine
CC       encephalomyelitis virus (TMEV). Can also detect other viruses such as
CC       dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved
CC       in antiviral signaling in response to viruses containing a dsDNA
CC       genome, such as vaccinia virus. Plays an important role in amplifying
CC       innate immune signaling through recognition of RNA metabolites that are
CC       produced during virus infection by ribonuclease L (RNase L). May play
CC       an important role in enhancing natural killer cell function and may be
CC       involved in growth inhibition and apoptosis in several tumor cell
CC       lines. {ECO:0000269|PubMed:12015121, ECO:0000269|PubMed:16625202,
CC       ECO:0000269|PubMed:17942531, ECO:0000269|PubMed:19656871,
CC       ECO:0000269|PubMed:21217758}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYX4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYX4};
CC   -!- SUBUNIT: Monomer in the absence of ligands and homodimerizes in the
CC       presence of dsRNA ligands. Can assemble into helical or linear
CC       polymeric filaments on long dsRNA. Interacts with MAVS/IPS1. Interacts
CC       (via the CARD domains) with TKFC, the interaction is inhibited by viral
CC       infection. Interacts with PCBP2. Interacts with NLRC5. Interacts with
CC       PIAS2-beta. Interacts with DDX60. Interacts with ANKRD17. Interacts
CC       with IKBKE. Interacts with ATG5 and ATG12, either as ATG5 and ATG12
CC       monomers or as ATG12-ATG5 conjugates. Interacts with ZCCHC3; leading to
CC       activate IFIH1/MDA5. Interacts with RNF123. Interacts with DDX3X.
CC       Interacts with NOD1; this interaction promotes transcription of
CC       antiviral genes and inhibition of viral replication.
CC       {ECO:0000250|UniProtKB:Q9BYX4}.
CC   -!- INTERACTION:
CC       Q8R5F7-1; P11207: P/V; Xeno; NbExp=3; IntAct=EBI-16019291, EBI-6148694;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12015121}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9BYX4}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q9BYX4}. Note=Upon viral RNA stimulation and
CC       ISGylation, translocates from cytosol to mitochondrion. May be found in
CC       the nucleus, during apoptosis. {ECO:0000250|UniProtKB:Q9BYX4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R5F7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R5F7-2; Sequence=VSP_013339;
CC   -!- TISSUE SPECIFICITY: Expression is prominent in lung, liver, kidney,
CC       heart and spleen (at protein level). Widely expressed at low level.
CC       {ECO:0000269|PubMed:12015121}.
CC   -!- INDUCTION: By interferon (IFN).
CC   -!- PTM: During apoptosis, processed into 3 cleavage products. The
CC       helicase-containing fragment, once liberated from the CARD domains,
CC       translocate from the cytoplasm to the nucleus. The processed protein
CC       significantly sensitizes cells to DNA degradation.
CC       {ECO:0000269|PubMed:12015121}.
CC   -!- PTM: Sumoylated. Sumoylation positively regulates its role in type I
CC       interferon induction and is enhanced by PIAS2-beta.
CC       {ECO:0000250|UniProtKB:Q9BYX4}.
CC   -!- PTM: Ubiquitinated by RNF125, leading to its degradation by the
CC       proteasome. USP17/UPS17L2-dependent deubiquitination positively
CC       regulates the receptor. Ubiquitinated by TRIM25 via 'Lys-63'-linked
CC       ubiquitination, promoting activation of IFIH1/MDA5. Ubiquitinated by
CC       TRIM40 via 'Lys-48'-linked ubiquitination; leading to proteasomal
CC       degradation. {ECO:0000250|UniProtKB:Q9BYX4}.
CC   -!- PTM: ISGylated by ISG15. ISGylation increases upon infection with
CC       viruses. ISGylation at Lys-23 and Lys-43 is dependent of
CC       dephosphorylation, regulates mitochondrial translocation and
CC       oligomerization. Essential for IFIH1/MDA5-mediated cytokine responses
CC       and restriction of virus replication. {ECO:0000250|UniProtKB:Q9BYX4}.
CC   -!- PTM: Phosphorylated. Dephosphorylated by phsophatases PP1;
CC       dephosphorylation precedes and is required for ISGylation.
CC       {ECO:0000250|UniProtKB:Q9BYX4}.
CC   -!- SIMILARITY: Belongs to the helicase family. RLR subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25508.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY075132; AAL77205.1; -; mRNA.
DR   EMBL; AF374384; AAM21359.1; -; mRNA.
DR   EMBL; AK018602; BAB31303.2; -; mRNA.
DR   EMBL; AK037057; BAC29687.2; -; mRNA.
DR   EMBL; AK040519; BAC30614.1; -; mRNA.
DR   EMBL; AK153018; BAE31652.1; -; mRNA.
DR   EMBL; AL929246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004031; AAH04031.1; -; mRNA.
DR   EMBL; BC019605; AAH19605.1; -; mRNA.
DR   EMBL; BC025508; AAH25508.1; ALT_INIT; mRNA.
DR   EMBL; BC080200; AAH80200.1; -; mRNA.
DR   CCDS; CCDS16068.1; -. [Q8R5F7-1]
DR   CCDS; CCDS50594.1; -. [Q8R5F7-2]
DR   RefSeq; NP_001157949.1; NM_001164477.1. [Q8R5F7-2]
DR   RefSeq; NP_082111.2; NM_027835.3. [Q8R5F7-1]
DR   PDB; 3TS9; X-ray; 2.00 A; A=545-697.
DR   PDB; 6G19; EM; 3.68 A; A=307-1020.
DR   PDB; 6G1S; EM; 3.93 A; A=310-1020.
DR   PDB; 6G1X; EM; 3.93 A; A=307-1020.
DR   PDB; 6GJZ; EM; 4.06 A; A=1-1025.
DR   PDB; 6GKH; EM; 4.06 A; A=1-1025.
DR   PDB; 6GKM; EM; 3.87 A; A=1-1025.
DR   PDB; 6H61; EM; 4.02 A; A=1-1025.
DR   PDB; 6H66; EM; 4.16 A; A=1-1025.
DR   PDB; 7BKP; EM; 2.80 A; A=1-1025.
DR   PDB; 7BKQ; EM; 3.40 A; A=307-1020.
DR   PDB; 7NGA; EM; 3.90 A; A=1-1025.
DR   PDB; 7NIC; EM; 4.30 A; A=1-1025.
DR   PDB; 7NIQ; EM; 4.30 A; B=1-1025.
DR   PDBsum; 3TS9; -.
DR   PDBsum; 6G19; -.
DR   PDBsum; 6G1S; -.
DR   PDBsum; 6G1X; -.
DR   PDBsum; 6GJZ; -.
DR   PDBsum; 6GKH; -.
DR   PDBsum; 6GKM; -.
DR   PDBsum; 6H61; -.
DR   PDBsum; 6H66; -.
DR   PDBsum; 7BKP; -.
DR   PDBsum; 7BKQ; -.
DR   PDBsum; 7NGA; -.
DR   PDBsum; 7NIC; -.
DR   PDBsum; 7NIQ; -.
DR   AlphaFoldDB; Q8R5F7; -.
DR   SMR; Q8R5F7; -.
DR   BioGRID; 214799; 4.
DR   DIP; DIP-60085N; -.
DR   IntAct; Q8R5F7; 1.
DR   STRING; 10090.ENSMUSP00000028259; -.
DR   iPTMnet; Q8R5F7; -.
DR   PhosphoSitePlus; Q8R5F7; -.
DR   SwissPalm; Q8R5F7; -.
DR   EPD; Q8R5F7; -.
DR   jPOST; Q8R5F7; -.
DR   MaxQB; Q8R5F7; -.
DR   PaxDb; Q8R5F7; -.
DR   PeptideAtlas; Q8R5F7; -.
DR   PRIDE; Q8R5F7; -.
DR   ProteomicsDB; 273099; -. [Q8R5F7-1]
DR   ProteomicsDB; 273100; -. [Q8R5F7-2]
DR   Antibodypedia; 805; 514 antibodies from 42 providers.
DR   DNASU; 71586; -.
DR   Ensembl; ENSMUST00000028259; ENSMUSP00000028259; ENSMUSG00000026896. [Q8R5F7-1]
DR   Ensembl; ENSMUST00000112459; ENSMUSP00000108078; ENSMUSG00000026896. [Q8R5F7-2]
DR   GeneID; 71586; -.
DR   KEGG; mmu:71586; -.
DR   UCSC; uc008jvm.2; mouse. [Q8R5F7-1]
DR   UCSC; uc012bvy.1; mouse. [Q8R5F7-2]
DR   CTD; 64135; -.
DR   MGI; MGI:1918836; Ifih1.
DR   VEuPathDB; HostDB:ENSMUSG00000026896; -.
DR   eggNOG; KOG0354; Eukaryota.
DR   GeneTree; ENSGT00940000153173; -.
DR   HOGENOM; CLU_006888_0_0_1; -.
DR   InParanoid; Q8R5F7; -.
DR   OMA; IQTFCQM; -.
DR   PhylomeDB; Q8R5F7; -.
DR   TreeFam; TF330258; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 71586; 1 hit in 74 CRISPR screens.
DR   PRO; PR:Q8R5F7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8R5F7; protein.
DR   Bgee; ENSMUSG00000026896; Expressed in small intestine Peyer's patch and 188 other tissues.
DR   ExpressionAtlas; Q8R5F7; baseline and differential.
DR   Genevisible; Q8R5F7; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; ISO:MGI.
DR   GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR   GO; GO:0039530; P:MDA-5 signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB.
DR   GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
DR   GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR   GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISS:UniProtKB.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR   GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; IMP:UniProtKB.
DR   Gene3D; 1.10.533.10; -; 2.
DR   Gene3D; 2.170.150.30; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR031964; CARD_dom.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041204; RIG-I_C.
DR   InterPro; IPR038557; RLR_C_sf.
DR   InterPro; IPR021673; RLR_CTR.
DR   Pfam; PF16739; CARD_2; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF18119; RIG-I_C; 1.
DR   Pfam; PF11648; RIG-I_C-RD; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF47986; SSF47986; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51789; RLR_CTR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Antiviral defense; ATP-binding;
KW   Cytoplasm; Helicase; Hydrolase; Immunity; Innate immunity; Isopeptide bond;
KW   Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding; Ubl conjugation; Zinc.
FT   CHAIN           1..1025
FT                   /note="Interferon-induced helicase C domain-containing
FT                   protein 1"
FT                   /id="PRO_0000102013"
FT   DOMAIN          7..97
FT                   /note="CARD 1"
FT   DOMAIN          110..190
FT                   /note="CARD 2"
FT   DOMAIN          317..510
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          700..872
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          893..1020
FT                   /note="RLR CTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01125"
FT   REGION          273..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         907
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01125"
FT   BINDING         910
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01125"
FT   BINDING         962
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01125"
FT   BINDING         964
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01125"
FT   SITE            208..209
FT                   /note="Cleavage"
FT   SITE            216..217
FT                   /note="Cleavage"
FT   SITE            251..252
FT                   /note="Cleavage"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         291
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         645
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         648
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         828
FT                   /note="Phosphoserine; by RIOK3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYX4"
FT   CROSSLNK        23
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ISG15)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYX4"
FT   CROSSLNK        43
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ISG15)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYX4"
FT   VAR_SEQ         207..255
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_013339"
FT   CONFLICT        100
FT                   /note="T -> I (in Ref. 6; AAH80200)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="V -> E (in Ref. 4; BAE31652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        412..414
FT                   /note="IST -> TRP (in Ref. 6; AAH25508)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624
FT                   /note="Y -> H (in Ref. 6; AAH25508)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        629
FT                   /note="T -> A (in Ref. 3; AAM21359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        647
FT                   /note="K -> E (in Ref. 6; AAH25508/AAH04031/AAH80200)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        889
FT                   /note="K -> E (in Ref. 4; BAB31303)"
FT                   /evidence="ECO:0000305"
FT   HELIX           311..321
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          326..329
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           336..353
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          360..365
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           367..376
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           379..382
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   TURN            383..385
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          388..390
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          393..395
FT                   /evidence="ECO:0007829|PDB:7BKQ"
FT   HELIX           397..400
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           401..407
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          409..414
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           415..426
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          428..430
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           435..437
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          439..445
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           446..448
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           454..474
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          475..477
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          484..490
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           500..513
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           526..532
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          537..543
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           550..565
FT                   /evidence="ECO:0007829|PDB:3TS9"
FT   STRAND          574..576
FT                   /evidence="ECO:0007829|PDB:7BKQ"
FT   HELIX           577..593
FT                   /evidence="ECO:0007829|PDB:3TS9"
FT   HELIX           596..617
FT                   /evidence="ECO:0007829|PDB:3TS9"
FT   HELIX           620..640
FT                   /evidence="ECO:0007829|PDB:3TS9"
FT   HELIX           671..691
FT                   /evidence="ECO:0007829|PDB:3TS9"
FT   HELIX           694..696
FT                   /evidence="ECO:0007829|PDB:3TS9"
FT   HELIX           699..715
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          721..724
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           728..740
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           742..747
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          751..754
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          761..763
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           768..780
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          785..789
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           790..792
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          793..795
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          802..808
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           813..821
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          825..827
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          829..839
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           840..862
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           866..890
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           900..902
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          904..910
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          913..916
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          919..923
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   TURN            924..926
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          927..930
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           933..936
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          940..942
FT                   /evidence="ECO:0007829|PDB:7BKQ"
FT   HELIX           945..948
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          959..961
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          967..974
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          977..982
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           984..986
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          987..990
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   STRAND          992..994
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   HELIX           1003..1005
FT                   /evidence="ECO:0007829|PDB:7BKP"
FT   TURN            1015..1018
FT                   /evidence="ECO:0007829|PDB:7BKQ"
SQ   SEQUENCE   1025 AA;  115971 MW;  708FCAC690C9F6D8 CRC64;
     MSIVCSAEDS FRNLILFFRP RLKMYIQVEP VLDHLIFLSA ETKEQILKKI NTCGNTSAAE
     LLLSTLEQGQ WPLGWTQMFV EALEHSGNPL AARYVKPTLT DLPSPSSETA HDECLHLLTL
     LQPTLVDKLL INDVLDTCFE KGLLTVEDRN RISAAGNSGN ESGVRELLRR IVQKENWFST
     FLDVLRQTGN DALFQELTGG GCPEDNTDLA NSSHRDGPAA NECLLPAVDE SSLETEAWNV
     DDILPEASCT DSSVTTESDT SLAEGSVSCF DESLGHNSNM GRDSGTMGSD SDESVIQTKR
     VSPEPELQLR PYQMEVAQPA LDGKNIIICL PTGSGKTRVA VYITKDHLDK KKQASESGKV
     IVLVNKVMLA EQLFRKEFNP YLKKWYRIIG LSGDTQLKIS FPEVVKSYDV IISTAQILEN
     SLLNLESGDD DGVQLSDFSL IIIDECHHTN KEAVYNNIMR RYLKQKLRNN DLKKQNKPAI
     PLPQILGLTA SPGVGAAKKQ SEAEKHILNI CANLDAFTIK TVKENLGQLK HQIKEPCKKF
     VIADDTRENP FKEKLLEIMA SIQTYCQKSP MSDFGTQHYE QWAIQMEKKA AKDGNRKDRV
     CAEHLRKYNE ALQINDTIRM IDAYSHLETF YTDEKEKKFA VLNDSDKSDD EASSCNDQLK
     GDVKKSLKLD ETDEFLMNLF FDNKKMLKKL AENPKYENEK LIKLRNTILE QFTRSEESSR
     GIIFTKTRQS TYALSQWIME NAKFAEVGVK AHHLIGAGHS SEVKPMTQTE QKEVISKFRT
     GEINLLIATT VAEEGLDIKE CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVTSSGSGV
     TEREIVNDFR EKMMYKAINR VQNMKPEEYA HKILELQVQS ILEKKMKVKR SIAKQYNDNP
     SLITLLCKNC SMLVCSGENI HVIEKMHHVN MTPEFKGLYI VRENKALQKK FADYQTNGEI
     ICKCGQAWGT MMVHKGLDLP CLKIRNFVVN FKNNSPKKQY KKWVELPIRF PDLDYSEYCL
     YSDED
 
 
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