ID ZNFX1_MOUSE Reviewed; 1909 AA.
AC Q8R151; A2A5R3; Q3U016; Q3UD71; Q3UEZ0;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 27-MAR-2024, entry version 148.
DE RecName: Full=NFX1-type zinc finger-containing protein 1 {ECO:0000305};
GN Name=Znfx1 {ECO:0000303|PubMed:31685995, ECO:0000312|MGI:MGI:2138982};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-869 AND 881-1909.
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Retina, and Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1316-1909.
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAVS, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=31685995; DOI=10.1038/s41556-019-0416-0;
RA Wang Y., Yuan S., Jia X., Ge Y., Ling T., Nie M., Lan X., Chen S., Xu A.;
RT "Mitochondria-localised ZNFX1 functions as a dsRNA sensor to initiate
RT antiviral responses through MAVS.";
RL Nat. Cell Biol. 21:1346-1356(2019).
CC -!- FUNCTION: RNA-binding protein that initiates the antiviral response and
CC is required to restrict the replication of RNA viruses
CC (PubMed:31685995). Acts as a double-stranded RNA (dsRNA) sensor that
CC recognizes viral RNA and then interacts with MAVS to initiate the type
CC I interferon response (PubMed:31685995). Also required for immunity
CC against some bacteria, such as mycobacteria (By similarity).
CC {ECO:0000250|UniProtKB:Q9P2E3, ECO:0000269|PubMed:31685995}.
CC -!- SUBUNIT: Interacts with MAVS. {ECO:0000269|PubMed:31685995}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:31685995}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q9P2E3}.
CC -!- INDUCTION: By interferons (IFNs) (PubMed:31685995). Expression is
CC induced upon viral infection (PubMed:31685995).
CC {ECO:0000269|PubMed:31685995}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable without obvious physiological or
CC behavioral abnormalities (PubMed:31685995). They however display
CC impaired innate immune responses against RNA virus infection by
CC producing less type I interferons (IFNs) (PubMed:31685995).
CC {ECO:0000269|PubMed:31685995}.
CC -!- SIMILARITY: Belongs to the ZNFX1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25488.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE34040.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL591711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL06496.1; -; Genomic_DNA.
DR EMBL; AK149249; BAE28771.1; -; mRNA.
DR EMBL; AK150223; BAE29390.1; -; mRNA.
DR EMBL; AK157301; BAE34040.1; ALT_INIT; mRNA.
DR EMBL; BC025488; AAH25488.1; ALT_INIT; mRNA.
DR CCDS; CCDS38337.1; -.
DR RefSeq; NP_001028368.2; NM_001033196.2.
DR RefSeq; XP_006500519.1; XM_006500456.3.
DR AlphaFoldDB; Q8R151; -.
DR SMR; Q8R151; -.
DR BioGRID; 221166; 5.
DR IntAct; Q8R151; 1.
DR STRING; 10090.ENSMUSP00000049404; -.
DR iPTMnet; Q8R151; -.
DR PhosphoSitePlus; Q8R151; -.
DR SwissPalm; Q8R151; -.
DR EPD; Q8R151; -.
DR MaxQB; Q8R151; -.
DR PaxDb; 10090-ENSMUSP00000049404; -.
DR PeptideAtlas; Q8R151; -.
DR ProteomicsDB; 275151; -.
DR Pumba; Q8R151; -.
DR Antibodypedia; 28464; 36 antibodies from 9 providers.
DR Ensembl; ENSMUST00000048988.14; ENSMUSP00000049404.8; ENSMUSG00000039501.15.
DR GeneID; 98999; -.
DR KEGG; mmu:98999; -.
DR UCSC; uc008nzc.2; mouse.
DR AGR; MGI:2138982; -.
DR CTD; 57169; -.
DR MGI; MGI:2138982; Znfx1.
DR VEuPathDB; HostDB:ENSMUSG00000039501; -.
DR eggNOG; KOG1807; Eukaryota.
DR GeneTree; ENSGT00940000155154; -.
DR HOGENOM; CLU_001066_0_1_1; -.
DR InParanoid; Q8R151; -.
DR OMA; PVCQVPI; -.
DR OrthoDB; 2971338at2759; -.
DR PhylomeDB; Q8R151; -.
DR TreeFam; TF323611; -.
DR BioGRID-ORCS; 98999; 2 hits in 80 CRISPR screens.
DR ChiTaRS; Znfx1; mouse.
DR PRO; PR:Q8R151; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R151; Protein.
DR Bgee; ENSMUSG00000039501; Expressed in animal zygote and 232 other cell types or tissues.
DR ExpressionAtlas; Q8R151; baseline and differential.
DR Genevisible; Q8R151; MM.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0031380; C:nuclear RNA-directed RNA polymerase complex; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002218; P:activation of innate immune response; IMP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0031048; P:regulatory ncRNA-mediated heterochromatin formation; IBA:GO_Central.
DR CDD; cd17936; EEXXEc_NFX1; 1.
DR CDD; cd06008; NF-X1-zinc-finger; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR046439; ZF_RZ_dom.
DR InterPro; IPR000967; Znf_NFX1.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF341; NFX1-TYPE ZINC FINGER-CONTAINING PROTEIN 1; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF20173; ZnF_RZ-type; 1.
DR SMART; SM00438; ZnF_NFX; 5.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51981; ZF_RZ; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Coiled coil; Cytoplasm; Immunity; Innate immunity;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..1909
FT /note="NFX1-type zinc finger-containing protein 1"
FT /id="PRO_0000050796"
FT ZN_FING 1291..1313
FT /note="NF-X1-type 1"
FT ZN_FING 1375..1393
FT /note="NF-X1-type 2"
FT ZN_FING 1433..1455
FT /note="NF-X1-type 3"
FT ZN_FING 1463..1480
FT /note="NF-X1-type 4"
FT ZN_FING 1818..1889
FT /note="RZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 939..964
FT /evidence="ECO:0000255"
FT COILED 1733..1764
FT /evidence="ECO:0000255"
FT COMPBIAS 54..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1840
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 1844
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 1860
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 1863
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT CONFLICT 212
FT /note="V -> I (in Ref. 3; BAE29390)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="R -> G (in Ref. 3; BAE29390)"
FT /evidence="ECO:0000305"
FT CONFLICT 1130
FT /note="V -> L (in Ref. 3; BAE34040)"
FT /evidence="ECO:0000305"
FT CONFLICT 1793
FT /note="T -> N (in Ref. 3; BAE34040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1909 AA; 218828 MW; 0F566F1DE54F5140 CRC64;
MEDRRPHLEA RPRNPPANHR GPMDGELPPR ARNQTNNPAA TNHAGRHLRA SNHPAPFRQR
EERFRAMGRN PHQGRRNQEG HTSDEARDQR QSQNDTRRRN DDQEGRSHRP PWSSDTFQQW
HTPPQKPGEQ PQQTKRLGYK FLESLLQKEP SEVAITLATS LGLKELLSHS SMKPSFLQLI
CQVLRKACSS RIDRQSILHV LGILNNSKFL RVCLPAYVVG MITEPSPDIR NQYPEHISNI
ISLLQDLVSV FPASSMQETS MLISLLPTSL NALRASGVDI EEETEKNLEK VQAIIKYLQE
KRRQGSLRVD TYTLVQAEAE GEVESYRAMP IYPTYNEVHL DEKPFLRPNI ISGKYESTAV
YLDTHFRLLR EDFVRPLREG ILKLLQSFED QCLRKRKFDD IRIYFDARII TPMCSASGIV
YKVQFDTKPL KLVRWQNSKR LLYGSLVCMS KDNFETFLFA TVSNREHEDL CQGIVQLCFN
EQSQQLLADV QPSDSFLMVE TTAYFEAYRH VLEGLQEVQE EDVPFQRNIV QCDSYVRNPR
YLLMGGRYDF TPLMENPSAM RKSLRGAEAL RHPRINVFDF GQWPSKEALK LDDSQMEALQ
FALTKELAII QGPPGTGKTY VGLKIVQALL TNKSVWQINT QTFPILVVCY TNHALDQFLE
GIYGCQKTSI VRVGGRSNSE ILKQFTLREL RNKREFRRTL PMHLRRAYMS IVTEMKESEQ
KLQEGAQTLE CTMHGVLREQ HLEKYISAQH WESLMSGPVQ DADWVCVQPS KHSMILEWLG
LGVGSFTQSA SPAGPENTAQ AEGEEEEEGE EEGSLIEIAE EADLIQADRV IEEEEVVRPR
RRKKEENGTD QELAKMLLAM RLDQEVPGTT AGPEQATEEW ETQRGQKKKM KRRVKVELRK
LNTMTKAEAN GIQDVWQLDL SSRWQLYRLW LQMYQADTRR RILSYERQYR TWAERMAELR
LQEDLHILKD AEVVGMTTTG AAKYRQILQQ VEPRIVIVEE AAEVLEAHTI ATLSKACQHL
ILIGDHQQLR PSANVYDLAK NFNLEVSLFE RLVKVNIPFV RLNYQHRMRP EIARLLTPHI
YQDLENHPSV LKYEQIKGVS SNLFFVEHNF PEQEIQEGKS HQNQHEAHFV VELCQYLLCQ
EYLPSQITIL TTYTGQLFCL RKLMPVKTFA GIKVHVVDKY QGEENDIILL SLVRSNQEGK
VGFLQIPNRI CVALSRAKKG MYCIGNMQML AKVPLWSRII HTLRENNQIG PSLRLCCQNH
PETHTLVSKA SDFQKVPEGG CSRPCEFRLA CGHVCTRACH PYDSSHKEFQ CMKPCQKVLC
QDGHRCPNVC FQECQPCQVK VPKIILKCGH KQMVPCSMSE SEFCCQEPCS KILRCGHRCS
HLCGEDCVRL CSERVTVELK CGHSQLVKCG NVEDIKYGLP VKCTTKCDTT LDCGHPCPGS
CHSCFEGRFH ERCQQPCKRL LICSHKCQEP CTGECPPCQR TCQNRCVHSQ CKKKCGELCS
PCVEPCVWRC QHYQCTKLCS EPCNRPPCYV PCTKLLACGH PCIGLCGEPC PKKCRVCQPD
EVTQIFFGFE DEPDARFVQL EDCSHIFEVQ ALDRFMNEQK DDEVAIKLKV CPICQVPIRK
NLRYGTSIKQ RLEEIEIVKE KIQGSAGEIS TSQEQLKALL KSKTLFHQLR PEEFLILQEK
LAQKNLSVKD LGLVENSIRF YDHLANLEGS LEKVHCGEQQ SVRTRLEQVH EWLAKKRLSF
SSQELSDLQS EIQRLTYLVN LLMRCKMAEK VKGSIAEEVS SIRNILEKTS KFTQEDEQLV
QKKMDALKTT LPCSGLGISD EERVQIVTAM GVPRGHWFKC PNGHIYVITE CGGAMQRSTC
PECQEVIGGE NHTLERSNHL ASEMDGAQHP AWSNTANNFM NFEEIHRMM
//
