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Protein argonaute-1 (Argonaute1) (hAgo1) (Argonaute RISC catalytic component 1) (Eukaryotic translation initiation factor 2C 1) (eIF-2C 1) (eIF2C 1) (Putative RNA-binding protein Q99)

 AGO1_HUMAN              Reviewed;         857 AA.
Q9UL18; Q5TA57; Q6P4S0;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
21-FEB-2006, sequence version 3.
22-NOV-2017, entry version 152.
RecName: Full=Protein argonaute-1;
Short=Argonaute1;
Short=hAgo1;
AltName: Full=Argonaute RISC catalytic component 1;
AltName: Full=Eukaryotic translation initiation factor 2C 1;
Short=eIF-2C 1;
Short=eIF2C 1;
AltName: Full=Putative RNA-binding protein Q99;
Name=AGO1; Synonyms=EIF2C1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10534406; DOI=10.1006/geno.1999.5951;
Koesters R., Adams V., Betts D., Moos R., Schmid M., Siermann A.,
Hassam S., Weitz S., Lichter P., Heitz P.U., von Knebel Doeberitz M.,
Briner J.;
"Human eukaryotic initiation factor EIF2C1 gene: cDNA sequence,
genomic organization, localization to chromosomal bands 1p34-p35, and
expression.";
Genomics 61:210-218(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
ASSOCIATION WITH MIRNA.
PubMed=15260970; DOI=10.1016/j.molcel.2004.07.007;
Meister G., Landthaler M., Patkaniowska A., Dorsett Y., Teng G.,
Tuschl T.;
"Human Argonaute2 mediates RNA cleavage targeted by miRNAs and
siRNAs.";
Mol. Cell 15:185-197(2004).
[5]
FUNCTION, INTERACTION WITH DICER1; MOV10; PRMT5 AND TNRC6B, AND
SUBCELLULAR LOCATION.
PubMed=16289642; DOI=10.1016/j.cub.2005.10.048;
Meister G., Landthaler M., Peters L., Chen P.Y., Urlaub H.,
Luehrmann R., Tuschl T.;
"Identification of novel argonaute-associated proteins.";
Curr. Biol. 15:2149-2155(2005).
[6]
FUNCTION.
PubMed=16936728; DOI=10.1038/nsmb1140;
Janowski B.A., Huffman K.E., Schwartz J.C., Ram R., Nordsell R.,
Shames D.S., Minna J.D., Corey D.R.;
"Involvement of AGO1 and AGO2 in mammalian transcriptional
silencing.";
Nat. Struct. Mol. Biol. 13:787-792(2006).
[7]
INTERACTION WITH DDX6 AND AGO2.
PubMed=16756390; DOI=10.1371/journal.pbio.0040210;
Chu C.-Y., Rana T.M.;
"Translation repression in human cells by microRNA-induced gene
silencing requires RCK/p54.";
PLoS Biol. 4:E210-E210(2006).
[8]
ASSOCIATION WITH POLYSOMES AND MNRP, AND INTERACTION WITH DDB1; DDX5;
DHX30; DHX36; DDX47; ELAVL1; HNRNPF; IGF2BP1; ILF3; MATR3; PABPC1;
RBM4; SART3; UPF1 AND YBX1.
PubMed=17932509; DOI=10.1038/sj.embor.7401088;
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
Urlaub H., Meister G.;
"Proteomic and functional analysis of Argonaute-containing mRNA-
protein complexes in human cells.";
EMBO Rep. 8:1052-1060(2007).
[9]
FUNCTION.
PubMed=18771919; DOI=10.1016/j.cub.2008.07.072;
Wu L., Fan J., Belasco J.G.;
"Importance of translation and nonnucleolytic ago proteins for on-
target RNA interference.";
Curr. Biol. 18:1327-1332(2008).
[10]
INTERACTION WITH IMP8.
PubMed=19167051; DOI=10.1016/j.cell.2008.12.023;
Weinmann L., Hoeck J., Ivacevic T., Ohrt T., Muetze J., Schwille P.,
Kremmer E., Benes V., Urlaub H., Meister G.;
"Importin 8 is a gene silencing factor that targets argonaute proteins
to distinct mRNAs.";
Cell 136:496-507(2009).
[11]
SUBCELLULAR LOCATION, AND INTERACTION WITH LIMD1; WTIP AND AJUBA.
PubMed=20616046; DOI=10.1073/pnas.0914987107;
James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M.,
Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J.,
Longmore G.D., Bushell M., Sharp T.V.;
"LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for
microRNA-mediated gene silencing.";
Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
INTERACTION WITH APOBEC3F; APOBEC3G AND APOBEC3H.
PubMed=22915799; DOI=10.1128/JVI.00595-12;
Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.;
"HIV-1 replication and APOBEC3 antiviral activity are not regulated by
P bodies.";
J. Virol. 86:11712-11724(2012).
[14]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 225-369, AND RNA-BINDING.
PubMed=15152257; DOI=10.1038/nature02519;
Ma J.-B., Ye K., Patel D.J.;
"Structural basis for overhang-specific small interfering RNA
recognition by the PAZ domain.";
Nature 429:318-322(2004).
[15]
X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH RNA,
RNA-BINDING, MUTAGENESIS OF PRO-670; PRO-675 AND ARG-805, AND LACK OF
CATALYTIC ACTIVITY.
PubMed=23809764; DOI=10.1016/j.celrep.2013.06.010;
Nakanishi K., Ascano M., Gogakos T., Ishibe-Murakami S.,
Serganov A.A., Briskin D., Morozov P., Tuschl T., Patel D.J.;
"Eukaryote-specific insertion elements control human ARGONAUTE slicer
activity.";
Cell Rep. 3:1893-1900(2013).
[16]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH RNA, LACK OF
CATALYTIC ACTIVITY, AND MUTAGENESIS OF LEU-674 AND ARG-805.
PubMed=23746446; DOI=10.1016/j.celrep.2013.05.033;
Faehnle C.R., Elkayam E., Haase A.D., Hannon G.J., Joshua-Tor L.;
"The making of a slicer: activation of human Argonaute-1.";
Cell Rep. 3:1901-1909(2013).
[17]
VARIANT SER-199.
PubMed=25003005; DOI=10.4161/rdis.26144;
Tuzovic L., Yu L., Zeng W., Li X., Lu H., Lu H.M., Gonzalez K.D.,
Chung W.K.;
"A human de novo mutation in MYH10 phenocopies the loss of function
mutation in mice.";
Rare Dis. 1:E26144-E26144(2013).
-!- FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds
to short RNAs such as microRNAs (miRNAs) or short interfering RNAs
(siRNAs), and represses the translation of mRNAs which are
complementary to them. Lacks endonuclease activity and does not
appear to cleave target mRNAs. Also required for transcriptional
gene silencing (TGS) of promoter regions which are complementary
to bound short antigene RNAs (agRNAs).
{ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16936728,
ECO:0000269|PubMed:18771919}.
-!- SUBUNIT: Interacts with DDB1, DDX5, DDX6, DHX30, DHX36, DDX47,
DICER1, AGO2, ELAVL1, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, MOV10,
PABPC1, PRMT5, RBM4, SART3, TNRC6B, UPF1 and YBX1. Associates with
polysomes and messenger ribonucleoproteins (mNRPs). Interacts with
LIMD1, WTIP and AJUBA. Interacts with APOBEC3F, APOBEC3G and
APOBEC3H. {ECO:0000269|PubMed:16289642,
ECO:0000269|PubMed:16756390, ECO:0000269|PubMed:17932509,
ECO:0000269|PubMed:19167051, ECO:0000269|PubMed:20616046,
ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23746446,
ECO:0000269|PubMed:23809764}.
-!- INTERACTION:
Q9UKV8:AGO2; NbExp=3; IntAct=EBI-527363, EBI-528269;
Q9UPY3:DICER1; NbExp=5; IntAct=EBI-527363, EBI-395506;
P08238:HSP90AB1; NbExp=3; IntAct=EBI-527363, EBI-352572;
O15397:IPO8; NbExp=2; IntAct=EBI-527363, EBI-358808;
P53041:PPP5C; NbExp=2; IntAct=EBI-527363, EBI-716663;
P04156:PRNP; NbExp=2; IntAct=EBI-527363, EBI-977302;
Q8NDV7:TNRC6A; NbExp=5; IntAct=EBI-527363, EBI-2269715;
Q9UPQ9-2:TNRC6B; NbExp=4; IntAct=EBI-527363, EBI-6514011;
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body
{ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:20616046}.
-!- MISCELLANEOUS: Lacks RNA cleavage activity due to the absence of
the conserved His at position 805, but also because it binds the
RNA in a subtly different manner that precludes efficient
cleavage.
-!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
{ECO:0000305}.
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EMBL; AF093097; AAF00068.1; -; mRNA.
EMBL; AL139286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC063275; AAH63275.1; -; mRNA.
CCDS; CCDS398.1; -.
RefSeq; NP_001304051.1; NM_001317122.1.
RefSeq; NP_001304052.1; NM_001317123.1.
RefSeq; NP_036331.1; NM_012199.4.
UniGene; Hs.22867; -.
UniGene; Hs.656677; -.
PDB; 1SI2; X-ray; 2.60 A; A=225-369.
PDB; 1SI3; X-ray; 2.60 A; A=225-369.
PDB; 4KRE; X-ray; 1.75 A; A=1-857.
PDB; 4KRF; X-ray; 2.10 A; A=1-857.
PDB; 4KXT; X-ray; 2.29 A; A=1-857.
PDB; 5W6V; X-ray; 2.83 A; A=1-857.
PDBsum; 1SI2; -.
PDBsum; 1SI3; -.
PDBsum; 4KRE; -.
PDBsum; 4KRF; -.
PDBsum; 4KXT; -.
PDBsum; 5W6V; -.
ProteinModelPortal; Q9UL18; -.
SMR; Q9UL18; -.
BioGrid; 117726; 56.
DIP; DIP-29193N; -.
IntAct; Q9UL18; 184.
STRING; 9606.ENSP00000362300; -.
iPTMnet; Q9UL18; -.
PhosphoSitePlus; Q9UL18; -.
BioMuta; AGO1; -.
DMDM; 88984241; -.
EPD; Q9UL18; -.
MaxQB; Q9UL18; -.
PaxDb; Q9UL18; -.
PeptideAtlas; Q9UL18; -.
PRIDE; Q9UL18; -.
Ensembl; ENST00000373204; ENSP00000362300; ENSG00000092847.
GeneID; 26523; -.
KEGG; hsa:26523; -.
UCSC; uc001bzl.4; human.
CTD; 26523; -.
DisGeNET; 26523; -.
EuPathDB; HostDB:ENSG00000092847.11; -.
GeneCards; AGO1; -.
HGNC; HGNC:3262; AGO1.
MIM; 606228; gene.
neXtProt; NX_Q9UL18; -.
OpenTargets; ENSG00000092847; -.
PharmGKB; PA27693; -.
eggNOG; KOG1041; Eukaryota.
eggNOG; ENOG410XP07; LUCA.
GeneTree; ENSGT00760000119148; -.
HOGENOM; HOG000116043; -.
InParanoid; Q9UL18; -.
KO; K11593; -.
OMA; TNPNNIE; -.
OrthoDB; EOG091G020J; -.
PhylomeDB; Q9UL18; -.
TreeFam; TF101510; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
Reactome; R-HSA-426496; Post-transcriptional silencing by small RNAs.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8943723; Regulation of PTEN mRNA translation.
Reactome; R-HSA-8948700; Competing endogenous RNAs (ceRNAs) regulate PTEN translation.
EvolutionaryTrace; Q9UL18; -.
GeneWiki; EIF2C1; -.
GenomeRNAi; 26523; -.
PRO; PR:Q9UL18; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000092847; -.
CleanEx; HS_EIF2C1; -.
ExpressionAtlas; Q9UL18; baseline and differential.
Genevisible; Q9UL18; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IC:BHF-UCL.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0005844; C:polysome; IDA:UniProtKB.
GO; GO:0016442; C:RISC complex; IDA:BHF-UCL.
GO; GO:0070578; C:RISC-loading complex; IDA:BHF-UCL.
GO; GO:0001047; F:core promoter binding; IMP:BHF-UCL.
GO; GO:0003725; F:double-stranded RNA binding; IDA:BHF-UCL.
GO; GO:0035198; F:miRNA binding; IDA:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core binding; IDA:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003727; F:single-stranded RNA binding; IDA:BHF-UCL.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0035278; P:miRNA mediated inhibition of translation; IDA:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IEA:Ensembl.
GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0035194; P:posttranscriptional gene silencing by RNA; TAS:Reactome.
GO; GO:0031054; P:pre-miRNA processing; IDA:BHF-UCL.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0010501; P:RNA secondary structure unwinding; IDA:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR014811; ArgoL1.
InterPro; IPR032472; ArgoL2.
InterPro; IPR032473; Argonaute_Mid_dom.
InterPro; IPR032474; Argonaute_N.
InterPro; IPR003100; PAZ_dom.
InterPro; IPR036085; PAZ_dom_sf.
InterPro; IPR003165; Piwi.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF08699; ArgoL1; 1.
Pfam; PF16488; ArgoL2; 1.
Pfam; PF16487; ArgoMid; 1.
Pfam; PF16486; ArgoN; 1.
Pfam; PF02170; PAZ; 1.
Pfam; PF02171; Piwi; 1.
SMART; SM01163; DUF1785; 1.
SMART; SM00949; PAZ; 1.
SMART; SM00950; Piwi; 1.
SUPFAM; SSF101690; SSF101690; 1.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS50821; PAZ; 1.
PROSITE; PS50822; PIWI; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Disease mutation;
Reference proteome; Repressor; Ribonucleoprotein; RNA-binding;
RNA-mediated gene silencing; Transcription; Transcription regulation;
Translation regulation.
CHAIN 1 857 Protein argonaute-1.
/FTId=PRO_0000194055.
DOMAIN 226 346 PAZ. {ECO:0000255|PROSITE-
ProRule:PRU00142}.
DOMAIN 515 816 Piwi. {ECO:0000255|PROSITE-
ProRule:PRU00150}.
REGION 309 314 Interaction with guide RNA.
REGION 522 564 Interaction with guide RNA.
REGION 670 675 Impairs access of bound RNA to the active
site.
REGION 708 712 Interaction with guide RNA.
REGION 751 759 Interaction with guide RNA.
REGION 788 813 Interaction with guide RNA.
VARIANT 199 199 G -> S (probable disease-associated
mutation found in a patient with moderate
intellectual disability and epilepsy).
{ECO:0000269|PubMed:25003005}.
/FTId=VAR_078651.
MUTAGEN 670 670 P->S: Confers modest RNA cleavage
activity; when associated with Q-675 and
H-805. {ECO:0000269|PubMed:23809764}.
MUTAGEN 674 674 L->F: Confers modest RNA cleavage
activity; when associated with H-805.
{ECO:0000269|PubMed:23746446}.
MUTAGEN 675 675 P->Q: Does not confer enzyme activity by
itself. Confers low RNA cleavage
activity; when associated with H-805.
Confers modest RNA cleavage activity;
when associated with S-670 and H-805.
{ECO:0000269|PubMed:23809764}.
MUTAGEN 805 805 R->H: Does not confer enzyme activity by
itself. Confers modest RNA cleavage
activity; when associated with F-674.
{ECO:0000269|PubMed:23746446,
ECO:0000269|PubMed:23809764}.
CONFLICT 242 242 D -> N (in Ref. 3; AAH63275).
{ECO:0000305}.
STRAND 33 46 {ECO:0000244|PDB:4KRE}.
STRAND 51 62 {ECO:0000244|PDB:4KRE}.
HELIX 66 79 {ECO:0000244|PDB:4KRE}.
HELIX 81 85 {ECO:0000244|PDB:4KRF}.
STRAND 94 102 {ECO:0000244|PDB:4KRE}.
TURN 105 108 {ECO:0000244|PDB:4KXT}.
STRAND 110 115 {ECO:0000244|PDB:4KRE}.
STRAND 125 137 {ECO:0000244|PDB:4KRE}.
HELIX 138 147 {ECO:0000244|PDB:4KRE}.
HELIX 154 171 {ECO:0000244|PDB:4KRE}.
STRAND 172 175 {ECO:0000244|PDB:4KRE}.
STRAND 178 180 {ECO:0000244|PDB:4KRE}.
STRAND 189 191 {ECO:0000244|PDB:4KRE}.
STRAND 194 206 {ECO:0000244|PDB:4KRE}.
STRAND 208 223 {ECO:0000244|PDB:4KRE}.
HELIX 228 236 {ECO:0000244|PDB:4KRE}.
TURN 241 243 {ECO:0000244|PDB:1SI2}.
HELIX 250 260 {ECO:0000244|PDB:4KRE}.
STRAND 264 268 {ECO:0000244|PDB:4KRE}.
TURN 269 272 {ECO:0000244|PDB:1SI2}.
STRAND 276 286 {ECO:0000244|PDB:4KRE}.
TURN 287 289 {ECO:0000244|PDB:4KRE}.
STRAND 291 295 {ECO:0000244|PDB:4KRE}.
STRAND 301 305 {ECO:0000244|PDB:4KRE}.
HELIX 306 314 {ECO:0000244|PDB:4KRE}.
STRAND 323 328 {ECO:0000244|PDB:4KRE}.
HELIX 331 333 {ECO:0000244|PDB:1SI2}.
STRAND 335 338 {ECO:0000244|PDB:4KRE}.
HELIX 339 341 {ECO:0000244|PDB:4KRE}.
STRAND 342 344 {ECO:0000244|PDB:4KRE}.
HELIX 356 366 {ECO:0000244|PDB:4KRE}.
HELIX 370 384 {ECO:0000244|PDB:4KRE}.
HELIX 386 388 {ECO:0000244|PDB:4KRE}.
HELIX 390 394 {ECO:0000244|PDB:4KRE}.
STRAND 404 410 {ECO:0000244|PDB:4KRE}.
TURN 420 423 {ECO:0000244|PDB:4KRE}.
STRAND 448 453 {ECO:0000244|PDB:4KRE}.
TURN 457 459 {ECO:0000244|PDB:4KRE}.
HELIX 462 478 {ECO:0000244|PDB:4KRE}.
STRAND 488 492 {ECO:0000244|PDB:4KRE}.
HELIX 496 498 {ECO:0000244|PDB:4KRE}.
HELIX 499 509 {ECO:0000244|PDB:4KRE}.
STRAND 515 520 {ECO:0000244|PDB:4KRE}.
HELIX 526 535 {ECO:0000244|PDB:4KRE}.
TURN 536 538 {ECO:0000244|PDB:4KRE}.
STRAND 542 546 {ECO:0000244|PDB:4KRE}.
HELIX 547 551 {ECO:0000244|PDB:4KRE}.
HELIX 555 568 {ECO:0000244|PDB:4KRE}.
HELIX 578 580 {ECO:0000244|PDB:4KRE}.
HELIX 583 586 {ECO:0000244|PDB:4KRE}.
STRAND 589 597 {ECO:0000244|PDB:4KRE}.
STRAND 608 615 {ECO:0000244|PDB:4KRE}.
STRAND 617 620 {ECO:0000244|PDB:4KRE}.
STRAND 623 631 {ECO:0000244|PDB:4KRE}.
HELIX 640 655 {ECO:0000244|PDB:4KRE}.
STRAND 660 666 {ECO:0000244|PDB:4KRE}.
HELIX 671 673 {ECO:0000244|PDB:4KRF}.
HELIX 674 692 {ECO:0000244|PDB:4KRE}.
STRAND 699 706 {ECO:0000244|PDB:4KRE}.
STRAND 713 717 {ECO:0000244|PDB:4KRE}.
HELIX 718 720 {ECO:0000244|PDB:4KRE}.
TURN 723 726 {ECO:0000244|PDB:4KRE}.
STRAND 732 734 {ECO:0000244|PDB:4KRE}.
STRAND 736 739 {ECO:0000244|PDB:4KRE}.
STRAND 741 743 {ECO:0000244|PDB:4KRE}.
STRAND 745 749 {ECO:0000244|PDB:4KRE}.
STRAND 755 757 {ECO:0000244|PDB:4KRE}.
STRAND 761 768 {ECO:0000244|PDB:4KRE}.
HELIX 774 784 {ECO:0000244|PDB:4KRE}.
STRAND 791 793 {ECO:0000244|PDB:5W6V}.
HELIX 799 814 {ECO:0000244|PDB:4KRE}.
HELIX 837 843 {ECO:0000244|PDB:4KRE}.
HELIX 848 851 {ECO:0000244|PDB:4KRE}.
SEQUENCE 857 AA; 97214 MW; 1DBB524AE7CBAF66 CRC64;
MEAGPSGAAA GAYLPPLQQV FQAPRRPGIG TVGKPIKLLA NYFEVDIPKI DVYHYEVDIK
PDKCPRRVNR EVVEYMVQHF KPQIFGDRKP VYDGKKNIYT VTALPIGNER VDFEVTIPGE
GKDRIFKVSI KWLAIVSWRM LHEALVSGQI PVPLESVQAL DVAMRHLASM RYTPVGRSFF
SPPEGYYHPL GGGREVWFGF HQSVRPAMWK MMLNIDVSAT AFYKAQPVIE FMCEVLDIRN
IDEQPKPLTD SQRVRFTKEI KGLKVEVTHC GQMKRKYRVC NVTRRPASHQ TFPLQLESGQ
TVECTVAQYF KQKYNLQLKY PHLPCLQVGQ EQKHTYLPLE VCNIVAGQRC IKKLTDNQTS
TMIKATARSA PDRQEEISRL MKNASYNLDP YIQEFGIKVK DDMTEVTGRV LPAPILQYGG
RNRAIATPNQ GVWDMRGKQF YNGIEIKVWA IACFAPQKQC REEVLKNFTD QLRKISKDAG
MPIQGQPCFC KYAQGADSVE PMFRHLKNTY SGLQLIIVIL PGKTPVYAEV KRVGDTLLGM
ATQCVQVKNV VKTSPQTLSN LCLKINVKLG GINNILVPHQ RSAVFQQPVI FLGADVTHPP
AGDGKKPSIT AVVGSMDAHP SRYCATVRVQ RPRQEIIEDL SYMVRELLIQ FYKSTRFKPT
RIIFYRDGVP EGQLPQILHY ELLAIRDACI KLEKDYQPGI TYIVVQKRHH TRLFCADKNE
RIGKSGNIPA GTTVDTNITH PFEFDFYLCS HAGIQGTSRP SHYYVLWDDN RFTADELQIL
TYQLCHTYVR CTRSVSIPAP AYYARLVAFR ARYHLVDKEH DSGEGSHISG QSNGRDPQAL
AKAVQVHQDT LRTMYFA


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