ZCCHV_MOUSE
ID ZCCHV_MOUSE Reviewed; 946 AA.
AC Q3UPF5; Q9CTU4; Q9DBS7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Zinc finger CCCH-type antiviral protein 1;
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 13;
DE Short=ARTD13;
DE AltName: Full=Inactive Poly [ADP-ribose] polymerase 13 {ECO:0000305};
DE Short=PARP13 {ECO:0000305};
GN Name=Zc3hav1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, Cecum, Lung, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND SER-324, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508 AND SER-553, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-265; SER-269;
RP SER-273; THR-277; SER-324 AND SER-350, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION.
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).
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) and moloney
CC and murine leukemia virus (MoMLV), filoviridae: ebola virus (EBOV) and
CC marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river
CC virus (RRV). Specifically targets the multiply spliced but not
CC unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a
CC more potent viral inhibitor than isoform 2. Isoform 2 acts as a
CC positive regulator of DDX58/RIG-I signaling resulting in activation of
CC the downstream effector IRF3 leading to the expression of type I IFNs
CC and IFN stimulated genes (ISGs). {ECO:0000269|PubMed:21102435}.
CC -!- SUBUNIT: Homodimer or homooligomer. Homooligomerization is essential
CC for its antiviral activity (By similarity). Interacts with EXOSC5 (By
CC similarity). Interacts (via N-terminal domain) with DDX17 in an RNA-
CC independent manner (By similarity). Interacts with EXOSC3, EXOSC7, DCP2
CC and DCP1A (By similarity). Interacts with PARN in an RNA-independent
CC manner (By similarity). Interacts with XRN1 in an RNA-dependent manner
CC (By similarity). Interacts (via N-terminal domain) with DHX30 (via N-
CC terminus) in an RNA-independent manner (By similarity). Isoform 2
CC interacts (via zinc-fingers) with DDX58/RIG-I in an RNA-dependent
CC manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3Y6}. Nucleus
CC {ECO:0000250|UniProtKB:Q8K3Y6}. Note=Localizes in the cytoplasm at
CC steady state, but shuttles between nucleus and cytoplasm in a XPO1-
CC dependent manner. {ECO:0000250|UniProtKB:Q8K3Y6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ZAPL;
CC IsoId=Q3UPF5-1; Sequence=Displayed;
CC Name=2; Synonyms=ZAPS;
CC IsoId=Q3UPF5-2; Sequence=VSP_033213, VSP_033214;
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. Contains a divergent PARP
CC homology ADP-ribosyltransferase domain which lacks the structural
CC requirements for NAD[+] binding. It is therefore inactive.
CC {ECO:0000250|UniProtKB:Q7Z2W4}.
CC -!- PTM: Phosphorylation at Ser-273 is essential for sequential
CC phosphorylation of Ser-269, Ser-265, Ser-262 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; AK004770; BAB23549.1; -; mRNA.
DR EMBL; AK080334; BAC37881.1; -; mRNA.
DR EMBL; AK143568; BAE25440.1; -; mRNA.
DR EMBL; AK169402; BAE41148.1; -; mRNA.
DR EMBL; AK172379; BAE42974.1; -; mRNA.
DR EMBL; AK020263; BAB32047.2; -; mRNA.
DR CCDS; CCDS20012.1; -. [Q3UPF5-2]
DR CCDS; CCDS80522.1; -. [Q3UPF5-1]
DR RefSeq; NP_082697.1; NM_028421.1. [Q3UPF5-1]
DR RefSeq; NP_083140.1; NM_028864.2. [Q3UPF5-2]
DR PDB; 6L1W; X-ray; 2.19 A; A=1-227.
DR PDBsum; 6L1W; -.
DR AlphaFoldDB; Q3UPF5; -.
DR SMR; Q3UPF5; -.
DR BioGRID; 219626; 6.
DR IntAct; Q3UPF5; 3.
DR MINT; Q3UPF5; -.
DR STRING; 10090.ENSMUSP00000031850; -.
DR iPTMnet; Q3UPF5; -.
DR PhosphoSitePlus; Q3UPF5; -.
DR SwissPalm; Q3UPF5; -.
DR EPD; Q3UPF5; -.
DR jPOST; Q3UPF5; -.
DR MaxQB; Q3UPF5; -.
DR PaxDb; Q3UPF5; -.
DR PeptideAtlas; Q3UPF5; -.
DR PRIDE; Q3UPF5; -.
DR ProteomicsDB; 298502; -. [Q3UPF5-1]
DR ProteomicsDB; 298503; -. [Q3UPF5-2]
DR Antibodypedia; 46163; 134 antibodies from 29 providers.
DR Ensembl; ENSMUST00000031850; ENSMUSP00000031850; ENSMUSG00000029826. [Q3UPF5-2]
DR Ensembl; ENSMUST00000143702; ENSMUSP00000144312; ENSMUSG00000029826. [Q3UPF5-1]
DR GeneID; 78781; -.
DR KEGG; mmu:78781; -.
DR UCSC; uc009bjz.2; mouse. [Q3UPF5-1]
DR UCSC; uc009bka.1; mouse. [Q3UPF5-2]
DR CTD; 56829; -.
DR MGI; MGI:1926031; Zc3hav1.
DR VEuPathDB; HostDB:ENSMUSG00000029826; -.
DR eggNOG; ENOG502QSC4; Eukaryota.
DR GeneTree; ENSGT00940000162001; -.
DR InParanoid; Q3UPF5; -.
DR PhylomeDB; Q3UPF5; -.
DR TreeFam; TF338389; -.
DR BioGRID-ORCS; 78781; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Zc3hav1; mouse.
DR PRO; PR:Q3UPF5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3UPF5; protein.
DR Bgee; ENSMUSG00000029826; Expressed in paneth cell and 183 other tissues.
DR ExpressionAtlas; Q3UPF5; baseline and differential.
DR Genevisible; Q3UPF5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IDA:MGI.
DR GO; GO:0098586; P:cellular response to virus; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISO:MGI.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:MGI.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISO:MGI.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IDA:MGI.
DR GO; GO:0050691; P:regulation of defense response to virus by host; ISO:MGI.
DR GO; GO:0009615; P:response to virus; ISS: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; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense; Cytoplasm; Immunity;
KW Innate immunity; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..946
FT /note="Zinc finger CCCH-type antiviral protein 1"
FT /id="PRO_0000331461"
FT DOMAIN 684..771
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 805..946
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 87..113
FT /note="C3H1-type 1"
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 173..194
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..254
FT /note="N-terminal domain"
FT REGION 221..283
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 302..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..570
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 283..290
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 412..413
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 228..250
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 262
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2W4"
FT MOD_RES 508
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2W4"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2W4"
FT VAR_SEQ 789
FT /note="D -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033213"
FT VAR_SEQ 790..946
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033214"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:6L1W"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:6L1W"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6L1W"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:6L1W"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:6L1W"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:6L1W"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:6L1W"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6L1W"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6L1W"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:6L1W"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6L1W"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6L1W"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:6L1W"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:6L1W"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6L1W"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:6L1W"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:6L1W"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:6L1W"
SQ SEQUENCE 946 AA; 106688 MW; BE2EFE5FBC6062EA CRC64;
MTDPEVFCFI TKILCAHGGR MTLEELLGEI SLPEAQLYEL LKAAGPDRFV LLETGDQAGI
TRSVVATTRA RVCRRKYCQR PCDSLHLCKL NLLGRCHYAQ SQRNLCKYSH DVLSEQNFQV
LKNHELSGLN QEELAVLLVQ SDPFFMPEIC KSYKGEGRKQ ICGQPQPCER LHICEHFTRG
NCSYLNCLRS HNLMDRKVLA IMREHGLSSD VVQNIQDICN NKHTRRNPPS MRAPHPHRRG
GAHRDRSKSR DRFHHNSLEV LSTVSPLGSG PPSPDVTGCK DPLEDVSADV TQKFKYLGTQ
DRAQLSSVSS KAAGVRGPSQ MRASQEFLED GDPDGLFSRN RSDSSTSRTS AAGFPLVAAQ
RNEAGAMKMG MPSGHHVEVK GKNEDIDRVP FLNSYIDGVT MEEATVSGIL GKRATDNGLE
EMILSSNHQK SVAKTQDPQT AGRITDSGQD TAFLHSKYEE NPAWPGTSTH NGPNGFSQIM
DETPNVSKSS PTGFGIKSAV TGGKEAVYSG VQSLRSHVLA MPGETTTPVQ GSNRLPPSPL
SSSTSHRVAA SGSPGKSSTH ASVSPASEPS RMMMMMSDPA EYSLCYIVNP VSPRMDDHGL
KEICLDHLYR GCQQVNCNKN HFHLPYRWQL FILPTWMDFQ DMEYIERAYC DPQIEIIVIE
KHRINFKKMT CDSYPIRRLS TPSFVEKTLN SVFTTKWLWY WRNELNEYTQ YGHESPSHTS
SEINSAYLES FFHSCPRGVL QFHAGSQNYE LSFQGMIQTN IASKTQRHVV RRPVFVSSKD
VEQKRRGPDH QPVMPQADAL TLFSSPQRNA STVSSNEYEF IELNNQDEEY AKISEQFKAS
MKQFKIVTIK RIWNQKLWDT FERKKQKMKN KTEMFLFHAV GRIHMDYICK NNFEWILHGN
REIRYGKGLC WRRENCDSSH AHGFLEMPLA SLGRTASLDS SGLQRK
