ID   ZCCHV_HUMAN             Reviewed;         902 AA.
AC   Q7Z2W4; A4D1R2; A4D1S4; Q8IW57; Q8TAJ3; Q96N79; Q9H8R9; Q9P0Y7;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 3.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=Zinc finger CCCH-type antiviral protein 1;
DE   AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 13 {ECO:0000303|PubMed:20106667};
DE            Short=ARTD13 {ECO:0000303|PubMed:20106667};
DE   AltName: Full=Inactive Poly [ADP-ribose] polymerase 13 {ECO:0000305};
DE            Short=PARP13 {ECO:0000303|PubMed:25043379};
DE   AltName: Full=Zinc finger CCCH domain-containing protein 2;
DE   AltName: Full=Zinc finger antiviral protein;
DE            Short=ZAP;
GN   Name=ZC3HAV1 {ECO:0000312|HGNC:HGNC:23721}; Synonyms=ZC3HDC2;
GN   ORFNames=PRO1677;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT GLN-565.
RC   TISSUE=Fetal liver;
RA   Zhang C., Yu Y., Zhang S., Zhou G., Wei H., Bi J., Xu W., Zai Y., Feng F.,
RA   Liu M., He F.;
RT   "Functional prediction of the coding sequences of 5 new genes deduced by
RT   analysis of cDNA clones from human fetal liver.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANTS
RP   LYS-485; GLN-565 AND GLU-701.
RC   TISSUE=Kidney, and Ovarian carcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-701
RP   AND ILE-851.
RC   TISSUE=Endometrium;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP   GLU-701 AND ILE-851.
RC   TISSUE=Brain, and Uterus;
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [11]
RP   FUNCTION.
RX   PubMed=18225958; DOI=10.1371/journal.pgen.0040021;
RA   Kerns J.A., Emerman M., Malik H.S.;
RT   "Positive selection and increased antiviral activity associated with the
RT   PARP-containing isoform of human zinc-finger antiviral protein.";
RL   PLoS Genet. 4:E21-E21(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-273; SER-275;
RP   SER-284; SER-302; SER-378; SER-387 AND THR-393, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [13]
RP   REVIEW.
RX   PubMed=18418085; DOI=10.4161/rna.5.2.6044;
RA   Zhu Y., Gao G.;
RT   "ZAP-mediated mRNA degradation.";
RL   RNA Biol. 5:65-67(2008).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-284; SER-335;
RP   SER-387 AND THR-393, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   RNA-BINDING, AND DOMAIN N-TERMINAL.
RX   PubMed=20451500; DOI=10.1016/j.bbrc.2010.04.164;
RA   Jeong M.S., Kim E.J., Jang S.B.;
RT   "Expression and RNA-binding of human zinc-finger antiviral protein.";
RL   Biochem. Biophys. Res. Commun. 396:696-702(2010).
RN   [17]
RP   SUBUNIT.
RX   PubMed=20181706; DOI=10.1128/jvi.02018-09;
RA   Law L.M., Albin O.R., Carroll J.W., Jones C.T., Rice C.M., Macdonald M.R.;
RT   "Identification of a dominant negative inhibitor of human zinc finger
RT   antiviral protein reveals a functional endogenous pool and critical
RT   homotypic interactions.";
RL   J. Virol. 84:4504-4512(2010).
RN   [18]
RP   INTERACTION WITH DHX30.
RX   PubMed=21204022; DOI=10.1007/s13238-010-0117-8;
RA   Ye P., Liu S., Zhu Y., Chen G., Gao G.;
RT   "DEXH-Box protein DHX30 is required for optimal function of the zinc-finger
RT   antiviral protein.";
RL   Protein Cell 1:956-964(2010).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-302; SER-335;
RP   SER-378; THR-393 AND SER-492, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP   SER-572 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [20]
RP   NOMENCLATURE.
RX   PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA   Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT   "Toward a unified nomenclature for mammalian ADP-ribosyltransferases.";
RL   Trends Biochem. Sci. 35:208-219(2010).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [22]
RP   REVIEW.
RX   PubMed=21169998; DOI=10.1038/ni0111-11;
RA   Liu H.M., Gale M. Jr.;
RT   "ZAPS electrifies RIG-I signaling.";
RL   Nat. Immunol. 12:11-12(2011).
RN   [23]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH RIGI.
RX   PubMed=21102435; DOI=10.1038/ni.1963;
RA   Hayakawa S., Shiratori S., Yamato H., Kameyama T., Kitatsuji C.,
RA   Kashigi F., Goto S., Kameoka S., Fujikura D., Yamada T., Mizutani T.,
RA   Kazumata M., Sato M., Tanaka J., Asaka M., Ohba Y., Miyazaki T.,
RA   Imamura M., Takaoka A.;
RT   "ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-
RT   I during antiviral responses.";
RL   Nat. Immunol. 12:37-44(2011).
RN   [24]
RP   FUNCTION, AND INTERACTION WITH EXOSC3; EXOSC7; PARN; DCP2; DCP1A AND XRN1.
RX   PubMed=21876179; DOI=10.1073/pnas.1101676108;
RA   Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T.,
RA   Gao G.;
RT   "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively
RT   targeting multiply spliced viral mRNAs for degradation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [26]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [27]
RP   FUNCTION.
RX   PubMed=22720057; DOI=10.1371/journal.pone.0039159;
RA   Wang X., Tu F., Zhu Y., Gao G.;
RT   "Zinc-finger antiviral protein inhibits XMRV infection.";
RL   PLoS ONE 7:E39159-E39159(2012).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; THR-273; SER-275;
RP   SER-284; SER-302; SER-335; SER-355; SER-378; THR-393; SER-407; SER-469;
RP   SER-492; SER-494; THR-554 AND SER-590, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-284 AND SER-492, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [30]
RP   LACK OF ADP-RIBOSYLTRANSFERASE ACTIVITY, AND NOMENCLATURE.
RX   PubMed=25043379; DOI=10.1038/ncomms5426;
RA   Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I.,
RA   Chang P.;
RT   "Family-wide analysis of poly(ADP-ribose) polymerase activity.";
RL   Nat. Commun. 5:4426-4426(2014).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 724-896, DOMAIN, AND MUTAGENESIS
RP   OF HIS-810 AND ASN-830.
RX   PubMed=25635049; DOI=10.1074/jbc.m114.630160;
RA   Karlberg T., Klepsch M., Thorsell A.G., Andersson C.D., Linusson A.,
RA   Schuler H.;
RT   "Structural basis for lack of ADP-ribosyltransferase activity in poly(ADP-
RT   ribose) polymerase-13/zinc finger antiviral protein.";
RL   J. Biol. Chem. 290:7336-7344(2015).
CC   -!- FUNCTION: Antiviral protein which inhibits the replication of viruses
CC       by recruiting the cellular RNA degradation machineries to degrade the
CC       viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the
CC       target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN
CC       to remove the poly(A) tail, and the 3'-5' exoribonuclease complex
CC       exosome to degrade the RNA body from the 3'-end. It also recruits the
CC       decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove
CC       the cap structure of the viral mRNA to initiate its degradation from
CC       the 5'-end. Its target viruses belong to families which include
CC       retroviridae: human immunodeficiency virus type 1 (HIV-1), moloney and
CC       murine leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV),
CC       filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae:
CC       sindbis virus (SINV) and Ross river virus (RRV). Specifically targets
CC       the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs
CC       for degradation. Isoform 1 is a more potent viral inhibitor than
CC       isoform 2. Isoform 2 acts as a positive regulator of RIGI signaling
CC       resulting in activation of the downstream effector IRF3 leading to the
CC       expression of type I IFNs and IFN stimulated genes (ISGs).
CC       {ECO:0000269|PubMed:18225958, ECO:0000269|PubMed:21102435,
CC       ECO:0000269|PubMed:21876179, ECO:0000269|PubMed:22720057}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable. {ECO:0000269|PubMed:20451500};
CC   -!- SUBUNIT: Homodimer or homooligomer. Homooligomerization is essential
CC       for its antiviral activity. Interacts with EXOSC5 (By similarity).
CC       Interacts (via N-terminal domain) with DDX17 in an RNA-independent
CC       manner (By similarity). Interacts with EXOSC3, EXOSC7, DCP2 and DCP1A.
CC       Interacts with PARN in an RNA-independent manner. Interacts with XRN1
CC       in an RNA-dependent manner. Isoform 2 interacts (via zinc-fingers) with
CC       RIGI in an RNA-dependent manner. Interacts (via N-terminal domain) with
CC       DHX30 (via N-terminus) in an RNA-independent manner. {ECO:0000250,
CC       ECO:0000269|PubMed:20181706, ECO:0000269|PubMed:21102435,
CC       ECO:0000269|PubMed:21204022, ECO:0000269|PubMed:21876179}.
CC   -!- INTERACTION:
CC       Q7Z2W4; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-922540, EBI-12012928;
CC       Q7Z2W4; Q99750: MDFI; NbExp=3; IntAct=EBI-922540, EBI-724076;
CC       Q7Z2W4; O95786: RIGI; NbExp=3; IntAct=EBI-922540, EBI-995350;
CC       Q7Z2W4-2; O95786: RIGI; NbExp=4; IntAct=EBI-922559, EBI-995350;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8K3Y6}. Nucleus {ECO:0000250|UniProtKB:Q8K3Y6}.
CC       Note=Localizes in the cytoplasm at steady state, but shuttles between
CC       nucleus and cytoplasm in a XPO1-dependent manner.
CC       {ECO:0000250|UniProtKB:Q8K3Y6}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000269|PubMed:21102435}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=ZAPL;
CC         IsoId=Q7Z2W4-1; Sequence=Displayed;
CC       Name=2; Synonyms=ZAPS {ECO:0000303|PubMed:21102435};
CC         IsoId=Q7Z2W4-2; Sequence=VSP_010269;
CC       Name=3;
CC         IsoId=Q7Z2W4-3; Sequence=VSP_010270, VSP_010271;
CC       Name=4;
CC         IsoId=Q7Z2W4-4; Sequence=VSP_010268;
CC       Name=5;
CC         IsoId=Q7Z2W4-5; Sequence=VSP_010268, VSP_010269;
CC   -!- INDUCTION: By type I interferon (IFN) and viruses. Isoform 2 is up-
CC       regulated by 3'-PPP-RNA. {ECO:0000269|PubMed:21102435}.
CC   -!- DOMAIN: The N-terminal domain is sufficient to bind to viral RNAs and
CC       promote their degradation. The second and fourth zinc fingers are
CC       involved in binding to specific viral RNAs (PubMed:20451500). Contains
CC       a divergent PARP homology ADP-ribosyltransferase domain which lacks the
CC       structural requirements for NAD[+] binding (PubMed:25635049). It is
CC       therefore inactive (PubMed:25043379, PubMed:25635049).
CC       {ECO:0000269|PubMed:20451500, ECO:0000269|PubMed:25043379,
CC       ECO:0000269|PubMed:25635049}.
CC   -!- PTM: Phosphorylation at Ser-275 is essential for sequential
CC       phosphorylation of Ser-271, Ser-267, Ser-263 and Ser-257 by GSK3-beta.
CC       Phosphorylation by GSK3-beta enhances its antiviral activity (By
CC       similarity). {ECO:0000250|UniProtKB:Q8K3Y6}.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR   EMBL; AF138863; AAF61195.1; -; mRNA.
DR   EMBL; AK055851; BAB71028.1; -; mRNA.
DR   EMBL; AK023350; BAB14537.1; -; mRNA.
DR   EMBL; BX571742; CAE11868.1; -; mRNA.
DR   EMBL; CH236950; EAL24040.1; -; Genomic_DNA.
DR   EMBL; CH236950; EAL24041.1; -; Genomic_DNA.
DR   EMBL; BC025308; AAH25308.1; -; mRNA.
DR   EMBL; BC027462; AAH27462.1; -; mRNA.
DR   EMBL; BC033105; AAH33105.1; -; mRNA.
DR   EMBL; BC040956; AAH40956.1; -; mRNA.
DR   CCDS; CCDS55171.1; -. [Q7Z2W4-2]
DR   CCDS; CCDS5851.1; -. [Q7Z2W4-1]
DR   RefSeq; NP_064504.2; NM_020119.3. [Q7Z2W4-1]
DR   RefSeq; NP_078901.3; NM_024625.3. [Q7Z2W4-2]
DR   PDB; 2X5Y; X-ray; 1.05 A; A=724-896.
DR   PDB; 4X52; X-ray; 2.08 A; A/B/C/D=726-896.
DR   PDB; 6UEI; X-ray; 2.51 A; A=2-227.
DR   PDB; 6UEJ; X-ray; 2.21 A; A=2-227.
DR   PDB; 7KZH; X-ray; 2.49 A; A=498-699.
DR   PDB; 7TGQ; X-ray; 2.00 A; A=498-699.
DR   PDBsum; 2X5Y; -.
DR   PDBsum; 4X52; -.
DR   PDBsum; 6UEI; -.
DR   PDBsum; 6UEJ; -.
DR   PDBsum; 7KZH; -.
DR   PDBsum; 7TGQ; -.
DR   AlphaFoldDB; Q7Z2W4; -.
DR   SMR; Q7Z2W4; -.
DR   BioGRID; 121203; 623.
DR   DIP; DIP-37896N; -.
DR   IntAct; Q7Z2W4; 164.
DR   MINT; Q7Z2W4; -.
DR   STRING; 9606.ENSP00000242351; -.
DR   ChEMBL; CHEMBL4295879; -.
DR   GlyCosmos; Q7Z2W4; 2 sites, 1 glycan.
DR   GlyGen; Q7Z2W4; 7 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; Q7Z2W4; -.
DR   MetOSite; Q7Z2W4; -.
DR   PhosphoSitePlus; Q7Z2W4; -.
DR   SwissPalm; Q7Z2W4; -.
DR   BioMuta; ZC3HAV1; -.
DR   DMDM; 223634727; -.
DR   EPD; Q7Z2W4; -.
DR   jPOST; Q7Z2W4; -.
DR   MassIVE; Q7Z2W4; -.
DR   MaxQB; Q7Z2W4; -.
DR   PaxDb; 9606-ENSP00000242351; -.
DR   PeptideAtlas; Q7Z2W4; -.
DR   ProteomicsDB; 68971; -. [Q7Z2W4-1]
DR   ProteomicsDB; 68972; -. [Q7Z2W4-2]
DR   ProteomicsDB; 68973; -. [Q7Z2W4-3]
DR   ProteomicsDB; 68974; -. [Q7Z2W4-4]
DR   ProteomicsDB; 68975; -. [Q7Z2W4-5]
DR   Pumba; Q7Z2W4; -.
DR   Antibodypedia; 46163; 159 antibodies from 29 providers.
DR   DNASU; 56829; -.
DR   Ensembl; ENST00000242351.10; ENSP00000242351.5; ENSG00000105939.14. [Q7Z2W4-1]
DR   Ensembl; ENST00000471652.1; ENSP00000419855.1; ENSG00000105939.14. [Q7Z2W4-2]
DR   GeneID; 56829; -.
DR   KEGG; hsa:56829; -.
DR   MANE-Select; ENST00000242351.10; ENSP00000242351.5; NM_020119.4; NP_064504.2.
DR   UCSC; uc003vun.4; human. [Q7Z2W4-1]
DR   AGR; HGNC:23721; -.
DR   CTD; 56829; -.
DR   DisGeNET; 56829; -.
DR   GeneCards; ZC3HAV1; -.
DR   HGNC; HGNC:23721; ZC3HAV1.
DR   HPA; ENSG00000105939; Tissue enhanced (bone).
DR   MIM; 607312; gene.
DR   neXtProt; NX_Q7Z2W4; -.
DR   OpenTargets; ENSG00000105939; -.
DR   PharmGKB; PA134944289; -.
DR   VEuPathDB; HostDB:ENSG00000105939; -.
DR   eggNOG; ENOG502QSC4; Eukaryota.
DR   GeneTree; ENSGT00940000162001; -.
DR   HOGENOM; CLU_014825_2_0_1; -.
DR   InParanoid; Q7Z2W4; -.
DR   OMA; KWKSPTS; -.
DR   OrthoDB; 5490222at2759; -.
DR   PhylomeDB; Q7Z2W4; -.
DR   TreeFam; TF338389; -.
DR   PathwayCommons; Q7Z2W4; -.
DR   Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR   SignaLink; Q7Z2W4; -.
DR   SIGNOR; Q7Z2W4; -.
DR   BioGRID-ORCS; 56829; 20 hits in 1172 CRISPR screens.
DR   ChiTaRS; ZC3HAV1; human.
DR   EvolutionaryTrace; Q7Z2W4; -.
DR   GeneWiki; ZC3HAV1; -.
DR   GenomeRNAi; 56829; -.
DR   Pharos; Q7Z2W4; Tbio.
DR   PRO; PR:Q7Z2W4; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q7Z2W4; Protein.
DR   Bgee; ENSG00000105939; Expressed in trabecular bone tissue and 198 other cell types or tissues.
DR   ExpressionAtlas; Q7Z2W4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IMP:UniProtKB.
DR   GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:UniProtKB.
DR   GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:UniProtKB.
DR   GO; GO:0061014; P:positive regulation of mRNA catabolic process; IDA:UniProtKB.
DR   GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IMP:UniProtKB.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; IBA:GO_Central.
DR   GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR   CDD; cd01439; TCCD_inducible_PARP_like; 1.
DR   Gene3D; 3.30.720.50; -; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR004170; WWE-dom.
DR   InterPro; IPR037197; WWE_dom_sf.
DR   InterPro; IPR041360; ZAP_HTH.
DR   InterPro; IPR040954; Znf-CCCH_8.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR45740; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR   PANTHER; PTHR45740:SF8; ZINC FINGER CCCH-TYPE ANTIVIRAL PROTEIN 1; 1.
DR   Pfam; PF18606; HTH_53; 1.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF02825; WWE; 1.
DR   Pfam; PF18633; zf-CCCH_8; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF117839; WWE domain; 1.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS50918; WWE; 1.
DR   PROSITE; PS50103; ZF_C3H1; 3.
DR   Genevisible; Q7Z2W4; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Antiviral defense;
KW   Cytoplasm; Immunity; Innate immunity; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   CHAIN           2..902
FT                   /note="Zinc finger CCCH-type antiviral protein 1"
FT                   /id="PRO_0000211343"
FT   DOMAIN          594..681
FT                   /note="WWE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT   DOMAIN          716..902
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT   ZN_FING         73..86
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         88..110
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         150..172
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         169..193
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          2..254
FT                   /note="N-terminal domain"
FT   REGION          221..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..254
FT                   /note="Binding to EXOSC5"
FT                   /evidence="ECO:0000250"
FT   REGION          265..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           69..76
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           285..292
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        265..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   MOD_RES         257
FT                   /note="Phosphoserine; by GSK3-beta"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         263
FT                   /note="Phosphoserine; by GSK3-beta"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3Y6"
FT   MOD_RES         267
FT                   /note="Phosphoserine; by GSK3-beta"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3Y6"
FT   MOD_RES         271
FT                   /note="Phosphoserine; by GSK3-beta"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         273
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         327
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UPF5"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         378
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         387
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         393
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         469
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         492
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         494
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         554
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         590
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..539
FT                   /note="Missing (in isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT                   /id="VSP_010268"
FT   VAR_SEQ         491..624
FT                   /note="DSLSDVTSTTSSRVDDHDSEEICLDHLCKGCPLNGSCSKVHFHLPYRWQMLI
FT                   GKTWTDFEHMETIEKGYCNPGIHLCSVGSYTINFRVMSCDSFPIRRLSTPSSVTKPANS
FT                   VFTTKWIWYWKNESGTWIQYGEE -> GKYKGKTLWASTFVHDIPNGSSQVVDKTTDVE
FT                   KTGATGFGLTMAVKAEKDMLCTGSQSLRNLVPTTPGESTAPAQVSTLPQSPAALSSSNR
FT                   AAVWGAQGQNCTQVPVSSASELTRKTTGSAQCKSLKDKGASVS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_010270"
FT   VAR_SEQ         625..902
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_010271"
FT   VAR_SEQ         699..902
FT                   /note="DHQPAKTSSVSLTATFRPQEDFCFLSSKKYKLSEIHHLHPEYVRVSEHFKAS
FT                   MKNFKIEKIKKIENSELLDKFTWKKSQMKEEGKLLFYATSRAYVESICSNNFDSFLHET
FT                   HENKYGKGIYFAKDAIYSHKNCPYDAKNVVMFVAQVLVGKFTEGNITYTSPPPQFDSCV
FT                   DTRSNPSVFVIFQKDQVYPQYVIEYTEDKACVIS -> E (in isoform 2 and
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT                   /id="VSP_010269"
FT   VARIANT         485
FT                   /note="R -> K (in dbSNP:rs2236426)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_018454"
FT   VARIANT         565
FT                   /note="H -> Q (in dbSNP:rs2297241)"
FT                   /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1"
FT                   /id="VAR_018455"
FT   VARIANT         701
FT                   /note="Q -> E (in dbSNP:rs2297236)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT                   /id="VAR_054319"
FT   VARIANT         851
FT                   /note="T -> I (in dbSNP:rs3735007)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:17974005"
FT                   /id="VAR_018456"
FT   MUTAGEN         810
FT                   /note="H->N: No effect on the structural inability to bind
FT                   NAD(+); when associated with Y-830."
FT                   /evidence="ECO:0000269|PubMed:25635049"
FT   MUTAGEN         830
FT                   /note="N->Y: No effect on the structural inability to bind
FT                   NAD(+); when associated with N-810."
FT                   /evidence="ECO:0000269|PubMed:25635049"
FT   CONFLICT        245
FT                   /note="A -> T (in Ref. 3; CAE11868)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..16
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   TURN            17..19
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   HELIX           23..30
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   HELIX           34..44
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   HELIX           89..92
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   HELIX           115..123
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   HELIX           131..141
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   STRAND          156..159
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:6UEI"
FT   HELIX           175..178
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   HELIX           196..204
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   HELIX           209..224
FT                   /evidence="ECO:0007829|PDB:6UEJ"
FT   HELIX           514..517
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   HELIX           524..526
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          528..530
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          533..542
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          545..548
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   HELIX           552..559
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          566..569
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          572..575
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   TURN            576..579
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          584..590
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   HELIX           594..596
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          607..612
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          618..620
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   HELIX           635..644
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          649..654
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          657..662
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   TURN            663..666
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          667..670
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   TURN            671..673
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          676..683
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   HELIX           688..695
FT                   /evidence="ECO:0007829|PDB:7TGQ"
FT   STRAND          729..732
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   HELIX           738..748
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   STRAND          754..763
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   HELIX           765..778
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   STRAND          783..790
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   HELIX           791..793
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   HELIX           794..800
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   HELIX           804..807
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   STRAND          812..814
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   STRAND          816..823
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   HELIX           824..830
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   HELIX           835..837
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   STRAND          838..845
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   STRAND          849..852
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   STRAND          866..869
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   STRAND          871..873
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   STRAND          876..879
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   HELIX           882..884
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   STRAND          885..895
FT                   /evidence="ECO:0007829|PDB:2X5Y"
FT   MOD_RES         Q7Z2W4-3:572
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
SQ   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
//