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Protein argonaute-3 (Argonaute3) (hAgo3) (Argonaute RISC catalytic component 3) (Eukaryotic translation initiation factor 2C 3) (eIF-2C 3) (eIF2C 3)

 AGO3_HUMAN              Reviewed;         860 AA.
Q9H9G7; B1ALI0; Q5TA55; Q9H1U6;
14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 2.
31-JAN-2018, entry version 131.
RecName: Full=Protein argonaute-3 {ECO:0000255|HAMAP-Rule:MF_03032};
Short=Argonaute3 {ECO:0000255|HAMAP-Rule:MF_03032};
Short=hAgo3;
AltName: Full=Argonaute RISC catalytic component 3;
AltName: Full=Eukaryotic translation initiation factor 2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
Short=eIF-2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
Short=eIF2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
Name=AGO3; Synonyms=EIF2C3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[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] (ISOFORM 2).
TISSUE=Leukocyte;
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]
SUBCELLULAR LOCATION.
PubMed=16081698; DOI=10.1126/science.1115079;
Pillai R.S., Bhattacharyya S.N., Artus C.G., Zoller T., Cougot N.,
Basyuk E., Bertrand E., Filipowicz W.;
"Inhibition of translational initiation by Let-7 MicroRNA in human
cells.";
Science 309:1573-1576(2005).
[6]
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).
[7]
INTERACTION WITH EIF4B; IMP8; PRMT5 AND TNRC6B.
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).
[8]
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).
[9]
FUNCTION, AND INTERACTION WITH EDC4.
PubMed=23064648; DOI=10.1038/nsmb.2400;
Hu Q., Tanasa B., Trabucchi M., Li W., Zhang J., Ohgi K.A., Rose D.W.,
Glass C.K., Rosenfeld M.G.;
"DICER- and AGO3-dependent generation of retinoic acid-induced DR2 Alu
RNAs regulates human stem cell proliferation.";
Nat. Struct. Mol. Biol. 19:1168-1175(2012).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds
to short RNAs such as microRNAs (miRNAs) and represses the
translation of mRNAs which are complementary to them. Lacks
endonuclease activity and does not appear to cleave target mRNAs.
Proposed to be involved in stabilization of small RNA derivates
(riRNA) derived from processed RNA polymerase III-transcribed Alu
repeats containing a DR2 retinoic acid response element (RARE) in
stem cells and in the subsequent riRNA-dependent degradation of a
subset of RNA polymerase II-transcribed coding mRNAs by recruiting
a mRNA decapping complex involving EDC4. {ECO:0000255|HAMAP-
Rule:MF_03032, ECO:0000269|PubMed:18771919,
ECO:0000269|PubMed:23064648}.
-!- SUBUNIT: Interacts with EIF4B, IMP8, PRMT5 and TNRC6B. Interacts
with APOBEC3F, APOBEC3G and APOBEC3H. Interacts with EDC4.
{ECO:0000255|HAMAP-Rule:MF_03032, ECO:0000269|PubMed:19167051,
ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23064648}.
-!- INTERACTION:
Q6P2E9:EDC4; NbExp=2; IntAct=EBI-2267883, EBI-1006038;
O15397:IPO8; NbExp=5; IntAct=EBI-2267883, EBI-358808;
P53041:PPP5C; NbExp=2; IntAct=EBI-2267883, EBI-716663;
Q8NDV7:TNRC6A; NbExp=3; IntAct=EBI-2267883, EBI-2269715;
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
Rule:MF_03032, ECO:0000269|PubMed:16081698}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H9G7-1; Sequence=Displayed;
Name=2;
IsoId=Q9H9G7-2; Sequence=VSP_041084;
-!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
{ECO:0000255|HAMAP-Rule:MF_03032}.
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EMBL; AK022827; BAB14262.1; -; mRNA.
EMBL; AL139286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC025769; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS399.1; -. [Q9H9G7-1]
CCDS; CCDS400.1; -. [Q9H9G7-2]
RefSeq; NP_079128.2; NM_024852.3. [Q9H9G7-1]
RefSeq; NP_803171.1; NM_177422.2. [Q9H9G7-2]
RefSeq; XP_005270632.1; XM_005270575.3. [Q9H9G7-1]
RefSeq; XP_011539184.1; XM_011540882.2. [Q9H9G7-2]
RefSeq; XP_016856012.1; XM_017000523.1. [Q9H9G7-1]
RefSeq; XP_016856013.1; XM_017000524.1. [Q9H9G7-2]
RefSeq; XP_016856014.1; XM_017000525.1. [Q9H9G7-2]
RefSeq; XP_016856015.1; XM_017000526.1. [Q9H9G7-2]
RefSeq; XP_016856016.1; XM_017000527.1. [Q9H9G7-2]
UniGene; Hs.657659; -.
PDB; 5VM9; X-ray; 3.28 A; A/C=1-860.
PDBsum; 5VM9; -.
ProteinModelPortal; Q9H9G7; -.
SMR; Q9H9G7; -.
BioGrid; 128177; 69.
DIP; DIP-54486N; -.
IntAct; Q9H9G7; 57.
STRING; 9606.ENSP00000362287; -.
iPTMnet; Q9H9G7; -.
PhosphoSitePlus; Q9H9G7; -.
BioMuta; AGO3; -.
DMDM; 76803660; -.
EPD; Q9H9G7; -.
MaxQB; Q9H9G7; -.
PaxDb; Q9H9G7; -.
PeptideAtlas; Q9H9G7; -.
PRIDE; Q9H9G7; -.
DNASU; 192669; -.
Ensembl; ENST00000246314; ENSP00000246314; ENSG00000126070. [Q9H9G7-2]
Ensembl; ENST00000373191; ENSP00000362287; ENSG00000126070. [Q9H9G7-1]
GeneID; 192669; -.
KEGG; hsa:192669; -.
UCSC; uc001bzp.4; human. [Q9H9G7-1]
CTD; 192669; -.
DisGeNET; 192669; -.
EuPathDB; HostDB:ENSG00000126070.19; -.
GeneCards; AGO3; -.
HGNC; HGNC:18421; AGO3.
HPA; HPA048342; -.
HPA; HPA075436; -.
MIM; 607355; gene.
neXtProt; NX_Q9H9G7; -.
OpenTargets; ENSG00000126070; -.
PharmGKB; PA38329; -.
eggNOG; KOG1041; Eukaryota.
eggNOG; ENOG410XP07; LUCA.
GeneTree; ENSGT00760000119148; -.
HOGENOM; HOG000116043; -.
InParanoid; Q9H9G7; -.
KO; K11593; -.
OMA; QPANPQY; -.
OrthoDB; EOG091G020J; -.
PhylomeDB; Q9H9G7; -.
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-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.
GenomeRNAi; 192669; -.
PRO; PR:Q9H9G7; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000126070; -.
CleanEx; HS_EIF2C3; -.
ExpressionAtlas; Q9H9G7; baseline and differential.
Genevisible; Q9H9G7; HS.
GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0016442; C:RISC complex; IDA:BHF-UCL.
GO; GO:0070578; C:RISC-loading complex; IDA: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:0003727; F:single-stranded RNA binding; IDA:BHF-UCL.
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:0006402; P:mRNA catabolic process; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
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:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0072091; P:regulation of stem cell proliferation; IMP:UniProtKB.
GO; GO:0010501; P:RNA secondary structure unwinding; IDA:BHF-UCL.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
Gene3D; 3.30.420.10; -; 1.
HAMAP; MF_03032; AGO3; 1.
InterPro; IPR028603; AGO3.
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; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Phosphoprotein; Reference proteome; Ribonucleoprotein;
RNA-binding; RNA-mediated gene silencing; Translation regulation.
CHAIN 1 860 Protein argonaute-3.
/FTId=PRO_0000194061.
DOMAIN 236 349 PAZ. {ECO:0000255|HAMAP-Rule:MF_03032}.
DOMAIN 518 819 Piwi. {ECO:0000255|HAMAP-Rule:MF_03032}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 234 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041084.
CONFLICT 25 25 T -> A (in Ref. 1; BAB14262).
{ECO:0000305}.
STRAND 27 40 {ECO:0000244|PDB:5VM9}.
STRAND 47 52 {ECO:0000244|PDB:5VM9}.
HELIX 60 73 {ECO:0000244|PDB:5VM9}.
TURN 76 79 {ECO:0000244|PDB:5VM9}.
STRAND 88 96 {ECO:0000244|PDB:5VM9}.
STRAND 122 126 {ECO:0000244|PDB:5VM9}.
STRAND 128 132 {ECO:0000244|PDB:5VM9}.
HELIX 136 139 {ECO:0000244|PDB:5VM9}.
STRAND 141 143 {ECO:0000244|PDB:5VM9}.
HELIX 159 174 {ECO:0000244|PDB:5VM9}.
STRAND 181 184 {ECO:0000244|PDB:5VM9}.
STRAND 192 194 {ECO:0000244|PDB:5VM9}.
STRAND 197 210 {ECO:0000244|PDB:5VM9}.
STRAND 213 226 {ECO:0000244|PDB:5VM9}.
HELIX 231 238 {ECO:0000244|PDB:5VM9}.
HELIX 253 263 {ECO:0000244|PDB:5VM9}.
STRAND 267 271 {ECO:0000244|PDB:5VM9}.
STRAND 279 285 {ECO:0000244|PDB:5VM9}.
TURN 290 292 {ECO:0000244|PDB:5VM9}.
HELIX 309 315 {ECO:0000244|PDB:5VM9}.
STRAND 328 332 {ECO:0000244|PDB:5VM9}.
TURN 334 337 {ECO:0000244|PDB:5VM9}.
STRAND 338 342 {ECO:0000244|PDB:5VM9}.
STRAND 345 347 {ECO:0000244|PDB:5VM9}.
HELIX 359 369 {ECO:0000244|PDB:5VM9}.
HELIX 373 386 {ECO:0000244|PDB:5VM9}.
HELIX 389 391 {ECO:0000244|PDB:5VM9}.
HELIX 393 397 {ECO:0000244|PDB:5VM9}.
STRAND 407 413 {ECO:0000244|PDB:5VM9}.
TURN 423 425 {ECO:0000244|PDB:5VM9}.
STRAND 452 456 {ECO:0000244|PDB:5VM9}.
TURN 460 462 {ECO:0000244|PDB:5VM9}.
HELIX 465 481 {ECO:0000244|PDB:5VM9}.
STRAND 491 495 {ECO:0000244|PDB:5VM9}.
STRAND 498 501 {ECO:0000244|PDB:5VM9}.
HELIX 502 512 {ECO:0000244|PDB:5VM9}.
STRAND 518 523 {ECO:0000244|PDB:5VM9}.
HELIX 529 539 {ECO:0000244|PDB:5VM9}.
HELIX 550 554 {ECO:0000244|PDB:5VM9}.
HELIX 558 571 {ECO:0000244|PDB:5VM9}.
HELIX 581 583 {ECO:0000244|PDB:5VM9}.
HELIX 586 589 {ECO:0000244|PDB:5VM9}.
STRAND 592 600 {ECO:0000244|PDB:5VM9}.
STRAND 611 618 {ECO:0000244|PDB:5VM9}.
STRAND 620 623 {ECO:0000244|PDB:5VM9}.
STRAND 626 633 {ECO:0000244|PDB:5VM9}.
HELIX 643 657 {ECO:0000244|PDB:5VM9}.
STRAND 658 660 {ECO:0000244|PDB:5VM9}.
STRAND 664 669 {ECO:0000244|PDB:5VM9}.
HELIX 677 692 {ECO:0000244|PDB:5VM9}.
TURN 693 695 {ECO:0000244|PDB:5VM9}.
STRAND 702 707 {ECO:0000244|PDB:5VM9}.
STRAND 716 719 {ECO:0000244|PDB:5VM9}.
TURN 721 723 {ECO:0000244|PDB:5VM9}.
TURN 726 729 {ECO:0000244|PDB:5VM9}.
STRAND 735 737 {ECO:0000244|PDB:5VM9}.
STRAND 739 742 {ECO:0000244|PDB:5VM9}.
STRAND 744 752 {ECO:0000244|PDB:5VM9}.
STRAND 764 771 {ECO:0000244|PDB:5VM9}.
HELIX 777 788 {ECO:0000244|PDB:5VM9}.
STRAND 792 796 {ECO:0000244|PDB:5VM9}.
HELIX 802 812 {ECO:0000244|PDB:5VM9}.
HELIX 815 818 {ECO:0000244|PDB:5VM9}.
HELIX 839 845 {ECO:0000244|PDB:5VM9}.
HELIX 851 853 {ECO:0000244|PDB:5VM9}.
SEQUENCE 860 AA; 97360 MW; 6FF1277995E5322E CRC64;
MEIGSAGPAG AQPLLMVPRR PGYGTMGKPI KLLANCFQVE IPKIDVYLYE VDIKPDKCPR
RVNREVVDSM VQHFKVTIFG DRRPVYDGKR SLYTANPLPV ATTGVDLDVT LPGEGGKDRP
FKVSIKFVSR VSWHLLHEVL TGRTLPEPLE LDKPISTNPV HAVDVVLRHL PSMKYTPVGR
SFFSAPEGYD HPLGGGREVW FGFHQSVRPA MWKMMLNIDV SATAFYKAQP VIQFMCEVLD
IHNIDEQPRP LTDSHRVKFT KEIKGLKVEV THCGTMRRKY RVCNVTRRPA SHQTFPLQLE
NGQTVERTVA QYFREKYTLQ LKYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN
QTSTMIKATA RSAPDRQEEI SRLVRSANYE TDPFVQEFQF KVRDEMAHVT GRVLPAPMLQ
YGGRNRTVAT PSHGVWDMRG KQFHTGVEIK MWAIACFATQ RQCREEILKG FTDQLRKISK
DAGMPIQGQP CFCKYAQGAD SVEPMFRHLK NTYSGLQLII VILPGKTPVY AEVKRVGDTL
LGMATQCVQV KNVIKTSPQT LSNLCLKINV KLGGINNILV PHQRPSVFQQ PVIFLGADVT
HPPAGDGKKP SIAAVVGSMD AHPSRYCATV RVQRPRQEII QDLASMVREL LIQFYKSTRF
KPTRIIFYRD GVSEGQFRQV LYYELLAIRE ACISLEKDYQ PGITYIVVQK RHHTRLFCAD
RTERVGRSGN IPAGTTVDTD ITHPYEFDFY LCSHAGIQGT SRPSHYHVLW DDNCFTADEL
QLLTYQLCHT YVRCTRSVSI PAPAYYAHLV AFRARYHLVD KEHDSAEGSH VSGQSNGRDP
QALAKAVQIH QDTLRTMYFA


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