ZCCHV_HUMAN
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 03-AUG-2022, entry version 178.
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
RP DDX58/RIG-I.
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 DDX58/RIG-I
CC signaling resulting in activation of the downstream effector IRF3
CC leading to the expression of type I IFNs and IFN stimulated genes
CC (ISGs). {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 DDX58/RIG-I in an RNA-dependent manner. Interacts (via N-terminal
CC domain) with DHX30 (via N-terminus) in an RNA-independent manner.
CC {ECO:0000250, ECO:0000269|PubMed:20181706, ECO:0000269|PubMed:21102435,
CC ECO:0000269|PubMed:21204022, ECO:0000269|PubMed:21876179}.
CC -!- INTERACTION:
CC Q7Z2W4; O95786: DDX58; NbExp=3; IntAct=EBI-922540, EBI-995350;
CC Q7Z2W4; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-922540, EBI-12012928;
CC Q7Z2W4; Q99750: MDFI; NbExp=3; IntAct=EBI-922540, EBI-724076;
CC Q7Z2W4-2; O95786: DDX58; 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; 563.
DR DIP; DIP-37896N; -.
DR IntAct; Q7Z2W4; 151.
DR MINT; Q7Z2W4; -.
DR STRING; 9606.ENSP00000242351; -.
DR ChEMBL; CHEMBL4295879; -.
DR GlyGen; Q7Z2W4; 3 sites, 1 O-linked glycan (2 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; Q7Z2W4; -.
DR PeptideAtlas; Q7Z2W4; -.
DR PRIDE; 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 Antibodypedia; 46163; 134 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 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; WKSPTSW; -.
DR OrthoDB; 782733at2759; -.
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; 13 hits in 1089 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 196 other tissues.
DR ExpressionAtlas; Q7Z2W4; baseline and differential.
DR Genevisible; Q7Z2W4; HS.
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 I-kappaB kinase/NF-kappaB signaling; 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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.720.50; -; 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 Pfam; PF18606; HTH_53; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR Pfam; PF18633; zf-CCCH_8; 1.
DR SUPFAM; SSF117839; SSF117839; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 1.
DR PROSITE; PS50103; ZF_C3H1; 3.
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:7KZH"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 533..542
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:7KZH"
FT HELIX 552..560
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 566..569
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:7KZH"
FT TURN 576..579
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 584..590
FT /evidence="ECO:0007829|PDB:7KZH"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:7KZH"
FT HELIX 635..644
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 649..654
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 657..662
FT /evidence="ECO:0007829|PDB:7KZH"
FT TURN 663..666
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 667..670
FT /evidence="ECO:0007829|PDB:7KZH"
FT TURN 671..673
FT /evidence="ECO:0007829|PDB:7KZH"
FT STRAND 676..683
FT /evidence="ECO:0007829|PDB:7KZH"
FT HELIX 688..695
FT /evidence="ECO:0007829|PDB:7KZH"
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
