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Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Zinc finger CCCH domain-containing protein 2) (Zinc finger antiviral protein) (ZAP)

 ZCCHV_HUMAN             Reviewed;         902 AA.
Q7Z2W4; A4D1R2; A4D1S4; Q8IW57; Q8TAJ3; Q96N79; Q9H8R9; Q9P0Y7;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 3.
05-DEC-2018, entry version 155.
RecName: Full=Zinc finger CCCH-type antiviral protein 1;
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 13;
Short=ARTD13;
AltName: Full=Zinc finger CCCH domain-containing protein 2;
AltName: Full=Zinc finger antiviral protein;
Short=ZAP;
Name=ZC3HAV1; Synonyms=ZC3HDC2; ORFNames=PRO1677;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT
GLN-565.
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Zhou G., Wei H., Bi J., Xu W., Zai Y.,
Feng F., Liu M., He F.;
"Functional prediction of the coding sequences of 5 new genes deduced
by analysis of cDNA clones from human fetal liver.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
VARIANTS LYS-485; GLN-565 AND GLU-701.
TISSUE=Kidney, and Ovarian carcinoma;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLU-701 AND ILE-851.
TISSUE=Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS GLU-701 AND ILE-851.
TISSUE=Brain, and Uterus;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
FUNCTION.
PubMed=18225958; DOI=10.1371/journal.pgen.0040021;
Kerns J.A., Emerman M., Malik H.S.;
"Positive selection and increased antiviral activity associated with
the PARP-containing isoform of human zinc-finger antiviral protein.";
PLoS Genet. 4:E21-E21(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-273; SER-275;
SER-284; SER-302; SER-378; SER-387 AND THR-393, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
REVIEW.
PubMed=18418085; DOI=10.4161/rna.5.2.6044;
Zhu Y., Gao G.;
"ZAP-mediated mRNA degradation.";
RNA Biol. 5:65-67(2008).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-284; SER-335;
SER-387 AND THR-393, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES,
RNA-BINDING, AND DOMAIN N-TERMINAL.
PubMed=20451500; DOI=10.1016/j.bbrc.2010.04.164;
Jeong M.S., Kim E.J., Jang S.B.;
"Expression and RNA-binding of human zinc-finger antiviral protein.";
Biochem. Biophys. Res. Commun. 396:696-702(2010).
[17]
SUBUNIT.
PubMed=20181706; DOI=10.1128/JVI.02018-09;
Law L.M., Albin O.R., Carroll J.W., Jones C.T., Rice C.M.,
Macdonald M.R.;
"Identification of a dominant negative inhibitor of human zinc finger
antiviral protein reveals a functional endogenous pool and critical
homotypic interactions.";
J. Virol. 84:4504-4512(2010).
[18]
INTERACTION WITH DHX30.
PubMed=21204022; DOI=10.1007/s13238-010-0117-8;
Ye P., Liu S., Zhu Y., Chen G., Gao G.;
"DEXH-Box protein DHX30 is required for optimal function of the zinc-
finger antiviral protein.";
Protein Cell 1:956-964(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-302; SER-335;
SER-378; THR-393 AND SER-492, PHOSPHORYLATION [LARGE SCALE ANALYSIS]
AT SER-572 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
NOMENCLATURE.
PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
"Toward a unified nomenclature for mammalian ADP-
ribosyltransferases.";
Trends Biochem. Sci. 35:208-219(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
REVIEW.
PubMed=21169998; DOI=10.1038/ni0111-11;
Liu H.M., Gale M. Jr.;
"ZAPS electrifies RIG-I signaling.";
Nat. Immunol. 12:11-12(2011).
[23]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH
DDX58/RIG-I.
PubMed=21102435; DOI=10.1038/ni.1963;
Hayakawa S., Shiratori S., Yamato H., Kameyama T., Kitatsuji C.,
Kashigi F., Goto S., Kameoka S., Fujikura D., Yamada T., Mizutani T.,
Kazumata M., Sato M., Tanaka J., Asaka M., Ohba Y., Miyazaki T.,
Imamura M., Takaoka A.;
"ZAPS is a potent stimulator of signaling mediated by the RNA helicase
RIG-I during antiviral responses.";
Nat. Immunol. 12:37-44(2011).
[24]
FUNCTION, AND INTERACTION WITH EXOSC3; EXOSC7; PARN; DCP2; DCP1A AND
XRN1.
PubMed=21876179; DOI=10.1073/pnas.1101676108;
Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L.,
Zheng Y.T., Gao G.;
"Zinc-finger antiviral protein inhibits HIV-1 infection by selectively
targeting multiply spliced viral mRNAs for degradation.";
Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[27]
FUNCTION.
PubMed=22720057; DOI=10.1371/journal.pone.0039159;
Wang X., Tu F., Zhu Y., Gao G.;
"Zinc-finger antiviral protein inhibits XMRV infection.";
PLoS ONE 7:E39159-E39159(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; THR-273; SER-275;
SER-284; SER-302; SER-335; SER-355; SER-378; THR-393; SER-407;
SER-469; SER-492; SER-494; THR-554 AND SER-590, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-284 AND
SER-492, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 724-896, DOMAIN, AND
MUTAGENESIS OF HIS-810 AND ASN-830.
PubMed=25635049; DOI=10.1074/jbc.M114.630160;
Karlberg T., Klepsch M., Thorsell A.G., Andersson C.D., Linusson A.,
Schuler H.;
"Structural basis for lack of ADP-ribosyltransferase activity in
poly(ADP-ribose) polymerase-13/zinc finger antiviral protein.";
J. Biol. Chem. 290:7336-7344(2015).
-!- FUNCTION: Antiviral protein which inhibits the replication of
viruses by recruiting the cellular RNA degradation machineries to
degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE)
present in the target viral mRNA, recruits cellular poly(A)-
specific ribonuclease PARN to remove the poly(A) tail, and the 3'-
5' exoribonuclease complex exosome to degrade the RNA body from
the 3'-end. It also recruits the decapping complex DCP1-DCP2
through RNA helicase p72 (DDX17) to remove the cap structure of
the viral mRNA to initiate its degradation from the 5'-end. Its
target viruses belong to families which include retroviridae:
human immunodeficiency virus type 1 (HIV-1), moloney and murine
leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV),
filoviridae: ebola virus (EBOV) and marburg virus (MARV),
togaviridae: sindbis virus (SINV) and Ross river virus (RRV).
Specifically targets the multiply spliced but not unspliced or
singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more
potent viral inhibitor than isoform 2. Isoform 2 acts as a
positive regulator of DDX58/RIG-I signaling resulting in
activation of the downstream effector IRF3 leading to the
expression of type I IFNs and IFN stimulated genes (ISGs).
{ECO:0000269|PubMed:18225958, ECO:0000269|PubMed:21102435,
ECO:0000269|PubMed:21876179, ECO:0000269|PubMed:22720057}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Thermostable. {ECO:0000269|PubMed:20451500};
-!- SUBUNIT: Homodimer or homooligomer. Homooligomerization is
essential for its antiviral activity. Interacts with EXOSC5 (By
similarity). Interacts (via N-terminal domain) with DDX17 in an
RNA-independent manner (By similarity). Interacts with EXOSC3,
EXOSC7, DCP2 and DCP1A. Interacts with PARN in an RNA-independent
manner. Interacts with XRN1 in an RNA-dependent manner. Isoform 2
interacts (via zinc-fingers) with DDX58/RIG-I in an RNA-dependent
manner. Interacts (via N-terminal domain) with DHX30 (via N-
terminus) in an RNA-independent manner. {ECO:0000250,
ECO:0000269|PubMed:20181706, ECO:0000269|PubMed:21102435,
ECO:0000269|PubMed:21204022, ECO:0000269|PubMed:21876179}.
-!- INTERACTION:
O95786:DDX58; NbExp=4; IntAct=EBI-922559, EBI-995350;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.
Note=Localizes in the cytoplasm at steady state, but shuttles
between nucleus and cytoplasm in a XPO1-dependent manner.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=ZAPL;
IsoId=Q7Z2W4-1; Sequence=Displayed;
Name=2; Synonyms=ZAPS;
IsoId=Q7Z2W4-2; Sequence=VSP_010269;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q7Z2W4-3; Sequence=VSP_010270, VSP_010271;
Note=No experimental confirmation available. Contains a
phosphoserine at position 572. {ECO:0000244|PubMed:20068231};
Name=4;
IsoId=Q7Z2W4-4; Sequence=VSP_010268;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q7Z2W4-5; Sequence=VSP_010268, VSP_010269;
Note=No experimental confirmation available.;
-!- INDUCTION: By type I interferon (IFN) and viruses. Isoform 2 is
up-regulated by 3'-PPP-RNA. {ECO:0000269|PubMed:21102435}.
-!- DOMAIN: The N-terminal domain is sufficient to bind to viral RNAs
and promote their degradation. The second and fourth zinc fingers
are involved in binding to specific viral RNAs (PubMed:20451500).
Contains a divergent PARP homology ADP-ribosyltransferase domain
which lacks the structural requirements for NAD[+] binding. It is
therefore inactive (PubMed:25635049).
{ECO:0000269|PubMed:20451500, ECO:0000269|PubMed:25635049}.
-!- PTM: Phosphorylation at Ser-275 is essential for sequential
phosphorylation of Ser-271, Ser-267, Ser-263 and Ser-257 by GSK3-
beta. Phosphorylation by GSK3-beta enhances its antiviral activity
(By similarity). {ECO:0000250}.
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EMBL; AF138863; AAF61195.1; -; mRNA.
EMBL; AK055851; BAB71028.1; -; mRNA.
EMBL; AK023350; BAB14537.1; -; mRNA.
EMBL; BX571742; CAE11868.1; -; mRNA.
EMBL; CH236950; EAL24040.1; -; Genomic_DNA.
EMBL; CH236950; EAL24041.1; -; Genomic_DNA.
EMBL; BC025308; AAH25308.1; -; mRNA.
EMBL; BC027462; AAH27462.1; -; mRNA.
EMBL; BC033105; AAH33105.1; -; mRNA.
EMBL; BC040956; AAH40956.1; -; mRNA.
CCDS; CCDS55171.1; -. [Q7Z2W4-2]
CCDS; CCDS5851.1; -. [Q7Z2W4-1]
RefSeq; NP_064504.2; NM_020119.3. [Q7Z2W4-1]
RefSeq; NP_078901.3; NM_024625.3. [Q7Z2W4-2]
UniGene; Hs.133512; -.
PDB; 2X5Y; X-ray; 1.05 A; A=724-896.
PDB; 4X52; X-ray; 2.08 A; A/B/C/D=726-896.
PDBsum; 2X5Y; -.
PDBsum; 4X52; -.
ProteinModelPortal; Q7Z2W4; -.
SMR; Q7Z2W4; -.
BioGrid; 121203; 164.
DIP; DIP-37896N; -.
IntAct; Q7Z2W4; 44.
MINT; Q7Z2W4; -.
STRING; 9606.ENSP00000242351; -.
iPTMnet; Q7Z2W4; -.
PhosphoSitePlus; Q7Z2W4; -.
SwissPalm; Q7Z2W4; -.
BioMuta; ZC3HAV1; -.
DMDM; 223634727; -.
EPD; Q7Z2W4; -.
MaxQB; Q7Z2W4; -.
PaxDb; Q7Z2W4; -.
PeptideAtlas; Q7Z2W4; -.
PRIDE; Q7Z2W4; -.
ProteomicsDB; 68971; -.
ProteomicsDB; 68972; -. [Q7Z2W4-2]
ProteomicsDB; 68973; -. [Q7Z2W4-3]
ProteomicsDB; 68974; -. [Q7Z2W4-4]
ProteomicsDB; 68975; -. [Q7Z2W4-5]
Ensembl; ENST00000242351; ENSP00000242351; ENSG00000105939. [Q7Z2W4-1]
Ensembl; ENST00000471652; ENSP00000419855; ENSG00000105939. [Q7Z2W4-2]
GeneID; 56829; -.
KEGG; hsa:56829; -.
UCSC; uc003vun.4; human. [Q7Z2W4-1]
CTD; 56829; -.
DisGeNET; 56829; -.
EuPathDB; HostDB:ENSG00000105939.12; -.
GeneCards; ZC3HAV1; -.
H-InvDB; HIX0007129; -.
HGNC; HGNC:23721; ZC3HAV1.
HPA; HPA047818; -.
HPA; HPA059096; -.
MIM; 607312; gene.
neXtProt; NX_Q7Z2W4; -.
OpenTargets; ENSG00000105939; -.
PharmGKB; PA134944289; -.
eggNOG; ENOG410IEI4; Eukaryota.
eggNOG; ENOG410ZFB8; LUCA.
GeneTree; ENSGT00940000162001; -.
HOVERGEN; HBG050384; -.
InParanoid; Q7Z2W4; -.
KO; K15259; -.
PhylomeDB; Q7Z2W4; -.
TreeFam; TF338389; -.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
ChiTaRS; ZC3HAV1; human.
EvolutionaryTrace; Q7Z2W4; -.
GeneWiki; ZC3HAV1; -.
GenomeRNAi; 56829; -.
PMAP-CutDB; Q7Z2W4; -.
PRO; PR:Q7Z2W4; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000105939; Expressed in 216 organ(s), highest expression level in blood.
CleanEx; HS_ZC3HAV1; -.
ExpressionAtlas; Q7Z2W4; baseline and differential.
Genevisible; Q7Z2W4; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:UniProtKB.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; IDA:UniProtKB.
GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IMP:UniProtKB.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 3.30.720.50; -; 1.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR004170; WWE-dom.
InterPro; IPR037197; WWE_dom_sf.
InterPro; IPR000571; Znf_CCCH.
Pfam; PF00644; PARP; 1.
Pfam; PF02825; WWE; 1.
SUPFAM; SSF117839; SSF117839; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS50918; WWE; 1.
PROSITE; PS50103; ZF_C3H1; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Antiviral defense;
Complete proteome; Cytoplasm; Immunity; Innate immunity;
Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CHAIN 2 902 Zinc finger CCCH-type antiviral protein
1.
/FTId=PRO_0000211343.
DOMAIN 594 681 WWE. {ECO:0000255|PROSITE-
ProRule:PRU00248}.
DOMAIN 716 902 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
ZN_FING 73 86 C3H1-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 88 110 C3H1-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 150 172 C3H1-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 169 193 C3H1-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
REGION 2 254 N-terminal domain.
REGION 224 254 Binding to EXOSC5. {ECO:0000250}.
MOTIF 69 76 Nuclear localization signal.
{ECO:0000250}.
MOTIF 285 292 Nuclear export signal. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 257 257 Phosphoserine; by GSK3-beta.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 263 263 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q8K3Y6}.
MOD_RES 267 267 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q8K3Y6}.
MOD_RES 271 271 Phosphoserine; by GSK3-beta.
{ECO:0000244|PubMed:18669648}.
MOD_RES 273 273 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UPF5}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 387 387 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 393 393 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 494 494 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 554 554 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 590 590 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 539 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.1}.
/FTId=VSP_010268.
VAR_SEQ 491 624 DSLSDVTSTTSSRVDDHDSEEICLDHLCKGCPLNGSCSKVH
FHLPYRWQMLIGKTWTDFEHMETIEKGYCNPGIHLCSVGSY
TINFRVMSCDSFPIRRLSTPSSVTKPANSVFTTKWIWYWKN
ESGTWIQYGEE -> GKYKGKTLWASTFVHDIPNGSSQVVD
KTTDVEKTGATGFGLTMAVKAEKDMLCTGSQSLRNLVPTTP
GESTAPAQVSTLPQSPAALSSSNRAAVWGAQGQNCTQVPVS
SASELTRKTTGSAQCKSLKDKGASVS (in isoform
3). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_010270.
VAR_SEQ 625 902 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010271.
VAR_SEQ 699 902 DHQPAKTSSVSLTATFRPQEDFCFLSSKKYKLSEIHHLHPE
YVRVSEHFKASMKNFKIEKIKKIENSELLDKFTWKKSQMKE
EGKLLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFA
KDAIYSHKNCPYDAKNVVMFVAQVLVGKFTEGNITYTSPPP
QFDSCVDTRSNPSVFVIFQKDQVYPQYVIEYTEDKACVIS
-> E (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.1}.
/FTId=VSP_010269.
VARIANT 485 485 R -> K (in dbSNP:rs2236426).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_018454.
VARIANT 565 565 H -> Q (in dbSNP:rs2297241).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.1}.
/FTId=VAR_018455.
VARIANT 701 701 Q -> E (in dbSNP:rs2297236).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_054319.
VARIANT 851 851 T -> I (in dbSNP:rs3735007).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_018456.
MUTAGEN 810 810 H->N: No effect on the structural
inability to bind NAD(+); when associated
with Y-830.
{ECO:0000269|PubMed:25635049}.
MUTAGEN 830 830 N->Y: No effect on the structural
inability to bind NAD(+); when associated
with N-810.
{ECO:0000269|PubMed:25635049}.
CONFLICT 245 245 A -> T (in Ref. 3; CAE11868).
{ECO:0000305}.
STRAND 729 732 {ECO:0000244|PDB:2X5Y}.
HELIX 738 748 {ECO:0000244|PDB:2X5Y}.
STRAND 754 763 {ECO:0000244|PDB:2X5Y}.
HELIX 765 778 {ECO:0000244|PDB:2X5Y}.
STRAND 783 790 {ECO:0000244|PDB:2X5Y}.
HELIX 791 793 {ECO:0000244|PDB:2X5Y}.
HELIX 794 800 {ECO:0000244|PDB:2X5Y}.
HELIX 804 807 {ECO:0000244|PDB:2X5Y}.
STRAND 812 814 {ECO:0000244|PDB:2X5Y}.
STRAND 816 823 {ECO:0000244|PDB:2X5Y}.
HELIX 824 830 {ECO:0000244|PDB:2X5Y}.
HELIX 835 837 {ECO:0000244|PDB:2X5Y}.
STRAND 838 845 {ECO:0000244|PDB:2X5Y}.
STRAND 849 852 {ECO:0000244|PDB:2X5Y}.
STRAND 866 869 {ECO:0000244|PDB:2X5Y}.
STRAND 871 873 {ECO:0000244|PDB:2X5Y}.
STRAND 876 879 {ECO:0000244|PDB:2X5Y}.
HELIX 882 884 {ECO:0000244|PDB:2X5Y}.
STRAND 885 895 {ECO:0000244|PDB:2X5Y}.
SEQUENCE 902 AA; 101431 MW; 72AB311D23658E24 CRC64;
MADPEVCCFI TKILCAHGGR MALDALLQEI ALSEPQLCEV LQVAGPDRFV VLETGGEAGI
TRSVVATTRA RVCRRKYCQR PCDNLHLCKL NLLGRCNYSQ SERNLCKYSH EVLSEENFKV
LKNHELSGLN KEELAVLLLQ SDPFFMPEIC KSYKGEGRQQ ICNQQPPCSR LHICDHFTRG
NCRFPNCLRS HNLMDRKVLA IMREHGLNPD VVQNIQDICN SKHMQKNPPG PRAPSSHRRN
MAYRARSKSR DRFFQGSQEF LASASASAER SCTPSPDQIS HRASLEDAPV DDLTRKFTYL
GSQDRARPPS GSSKATDLGG TSQAGTSQRF LENGSQEDLL HGNPGSTYLA SNSTSAPNWK
SLTSWTNDQG ARRKTVFSPT LPAARSSLGS LQTPEAVTTR KGTGLLSSDY RIINGKSGTQ
DIQPGPLFNN NADGVATDIT STRSLNYKST SSGHREISSP RIQDAGPASR DVQATGRIAD
DADPRVALVN DSLSDVTSTT SSRVDDHDSE EICLDHLCKG CPLNGSCSKV HFHLPYRWQM
LIGKTWTDFE HMETIEKGYC NPGIHLCSVG SYTINFRVMS CDSFPIRRLS TPSSVTKPAN
SVFTTKWIWY WKNESGTWIQ YGEEKDKRKN SNVDSSYLES LYQSCPRGVV PFQAGSRNYE
LSFQGMIQTN IASKTQKDVI RRPTFVPQWY VQQMKRGPDH QPAKTSSVSL TATFRPQEDF
CFLSSKKYKL SEIHHLHPEY VRVSEHFKAS MKNFKIEKIK KIENSELLDK FTWKKSQMKE
EGKLLFYATS RAYVESICSN NFDSFLHETH ENKYGKGIYF AKDAIYSHKN CPYDAKNVVM
FVAQVLVGKF TEGNITYTSP PPQFDSCVDT RSNPSVFVIF QKDQVYPQYV IEYTEDKACV
IS


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