AGO4_HUMAN
ID AGO4_HUMAN Reviewed; 861 AA.
AC Q9HCK5; A7MD27;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein argonaute-4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE Short=Argonaute4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE Short=hAgo4;
DE AltName: Full=Argonaute RISC catalytic component 4;
DE AltName: Full=Eukaryotic translation initiation factor 2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE Short=eIF-2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
DE Short=eIF2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
GN Name=AGO4; Synonyms=EIF2C4, KIAA1567;
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].
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP ASSOCIATION WITH MIRNA.
RX PubMed=15260970; DOI=10.1016/j.molcel.2004.07.007;
RA Meister G., Landthaler M., Patkaniowska A., Dorsett Y., Teng G., Tuschl T.;
RT "Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs.";
RL Mol. Cell 15:185-197(2004).
RN [6]
RP FUNCTION.
RX PubMed=15337849; DOI=10.1261/rna.7131604;
RA Pillai R.S., Artus C.G., Filipowicz W.;
RT "Tethering of human Ago proteins to mRNA mimics the miRNA-mediated
RT repression of protein synthesis.";
RL RNA 10:1518-1525(2004).
RN [7]
RP INTERACTION WITH ZFP36.
RX PubMed=15766526; DOI=10.1016/j.cell.2004.12.038;
RA Jing Q., Huang S., Guth S., Zarubin T., Motoyama A., Chen J., Di Padova F.,
RA Lin S.C., Gram H., Han J.;
RT "Involvement of microRNA in AU-rich element-mediated mRNA instability.";
RL Cell 120:623-634(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16081698; DOI=10.1126/science.1115079;
RA Pillai R.S., Bhattacharyya S.N., Artus C.G., Zoller T., Cougot N.,
RA Basyuk E., Bertrand E., Filipowicz W.;
RT "Inhibition of translational initiation by Let-7 MicroRNA in human cells.";
RL Science 309:1573-1576(2005).
RN [9]
RP FUNCTION.
RX PubMed=18771919; DOI=10.1016/j.cub.2008.07.072;
RA Wu L., Fan J., Belasco J.G.;
RT "Importance of translation and nonnucleolytic ago proteins for on-target
RT RNA interference.";
RL Curr. Biol. 18:1327-1332(2008).
RN [10]
RP FUNCTION.
RX PubMed=18552826; DOI=10.1038/nsmb.1440;
RA Haussecker D., Cao D., Huang Y., Parameswaran P., Fire A.Z., Kay M.A.;
RT "Capped small RNAs and MOV10 in human hepatitis delta virus replication.";
RL Nat. Struct. Mol. Biol. 15:714-721(2008).
RN [11]
RP INTERACTION WITH EIF4B; IMP8; PRMT5; TNRC6A AND TNRC6B, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19167051; DOI=10.1016/j.cell.2008.12.023;
RA Weinmann L., Hoeck J., Ivacevic T., Ohrt T., Muetze J., Schwille P.,
RA Kremmer E., Benes V., Urlaub H., Meister G.;
RT "Importin 8 is a gene silencing factor that targets argonaute proteins to
RT distinct mRNAs.";
RL Cell 136:496-507(2009).
CC -!- FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to
CC short RNAs such as microRNAs (miRNAs) and represses the translation of
CC mRNAs which are complementary to them. Lacks endonuclease activity and
CC does not appear to cleave target mRNAs. Also required for RNA-directed
CC transcription and replication of the human hapatitis delta virus (HDV).
CC {ECO:0000255|HAMAP-Rule:MF_03033, ECO:0000269|PubMed:15337849,
CC ECO:0000269|PubMed:18552826, ECO:0000269|PubMed:18771919}.
CC -!- SUBUNIT: Interacts with EIF4B, IMP8, PRMT5, TNRC6A and TNRC6B
CC (PubMed:19167051). Interacts with ZFP36 (PubMed:15766526).
CC {ECO:0000255|HAMAP-Rule:MF_03033, ECO:0000269|PubMed:15766526,
CC ECO:0000269|PubMed:19167051}.
CC -!- INTERACTION:
CC Q9HCK5; O15397: IPO8; NbExp=3; IntAct=EBI-2269696, EBI-358808;
CC Q9HCK5; Q8NDV7: TNRC6A; NbExp=4; IntAct=EBI-2269696, EBI-2269715;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03033, ECO:0000269|PubMed:16081698,
CC ECO:0000269|PubMed:19167051}.
CC -!- PTM: Ubiquitinated on surface-exposed lysines by a SCF-like E3
CC ubiquitin-protein ligase complex containing ZSWIM8 during target-
CC directed microRNA degradation (TDMD), a process that mediates
CC degradation of microRNAs (miRNAs). Ubiquitination by the SCF-like E3
CC ubiquitin-protein ligase complex containing ZSWIM8 leads to its
CC subsequent degradation, thereby exposing miRNAs for degradation. ZSWIM8
CC recognizes and binds AGO4 when it is engaged with a TDMD target.
CC {ECO:0000250|UniProtKB:Q9UKV8}.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03033}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13393.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB046787; BAB13393.1; ALT_INIT; mRNA.
DR EMBL; AL359186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07400.1; -; Genomic_DNA.
DR EMBL; BC152450; AAI52451.1; -; mRNA.
DR CCDS; CCDS397.1; -.
DR RefSeq; NP_060099.2; NM_017629.3.
DR PDB; 6OON; X-ray; 1.90 A; A=1-861.
DR PDBsum; 6OON; -.
DR AlphaFoldDB; Q9HCK5; -.
DR SMR; Q9HCK5; -.
DR BioGRID; 128178; 221.
DR CORUM; Q9HCK5; -.
DR IntAct; Q9HCK5; 80.
DR MINT; Q9HCK5; -.
DR STRING; 9606.ENSP00000362306; -.
DR iPTMnet; Q9HCK5; -.
DR PhosphoSitePlus; Q9HCK5; -.
DR BioMuta; AGO4; -.
DR DMDM; 38372393; -.
DR EPD; Q9HCK5; -.
DR jPOST; Q9HCK5; -.
DR MassIVE; Q9HCK5; -.
DR MaxQB; Q9HCK5; -.
DR PaxDb; Q9HCK5; -.
DR PeptideAtlas; Q9HCK5; -.
DR PRIDE; Q9HCK5; -.
DR ProteomicsDB; 81747; -.
DR Antibodypedia; 31591; 172 antibodies from 28 providers.
DR DNASU; 192670; -.
DR Ensembl; ENST00000373210.4; ENSP00000362306.3; ENSG00000134698.11.
DR GeneID; 192670; -.
DR KEGG; hsa:192670; -.
DR MANE-Select; ENST00000373210.4; ENSP00000362306.3; NM_017629.4; NP_060099.2.
DR UCSC; uc001bzj.3; human.
DR CTD; 192670; -.
DR DisGeNET; 192670; -.
DR GeneCards; AGO4; -.
DR HGNC; HGNC:18424; AGO4.
DR HPA; ENSG00000134698; Low tissue specificity.
DR MIM; 607356; gene.
DR neXtProt; NX_Q9HCK5; -.
DR OpenTargets; ENSG00000134698; -.
DR PharmGKB; PA38330; -.
DR VEuPathDB; HostDB:ENSG00000134698; -.
DR eggNOG; KOG1041; Eukaryota.
DR GeneTree; ENSGT00940000158729; -.
DR HOGENOM; CLU_004544_4_3_1; -.
DR InParanoid; Q9HCK5; -.
DR OMA; VGANRHY; -.
DR OrthoDB; 159407at2759; -.
DR PhylomeDB; Q9HCK5; -.
DR TreeFam; TF101510; -.
DR PathwayCommons; Q9HCK5; -.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
DR Reactome; R-HSA-426496; Post-transcriptional silencing by small RNAs.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8943723; Regulation of PTEN mRNA translation.
DR Reactome; R-HSA-8948700; Competing endogenous RNAs (ceRNAs) regulate PTEN translation.
DR Reactome; R-HSA-8986944; Transcriptional Regulation by MECP2.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; Q9HCK5; -.
DR BioGRID-ORCS; 192670; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; AGO4; human.
DR GenomeRNAi; 192670; -.
DR Pharos; Q9HCK5; Tbio.
DR PRO; PR:Q9HCK5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9HCK5; protein.
DR Bgee; ENSG00000134698; Expressed in monocyte and 177 other tissues.
DR Genevisible; Q9HCK5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; IDA:BHF-UCL.
DR GO; GO:0070578; C:RISC-loading complex; IDA:BHF-UCL.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:BHF-UCL.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0035198; F:miRNA binding; IDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:BHF-UCL.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0007140; P:male meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0010586; P:miRNA metabolic process; IEA:Ensembl.
DR GO; GO:0035196; P:miRNA processing; IMP:BHF-UCL.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0031054; P:pre-miRNA processing; IDA:BHF-UCL.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:Ensembl.
DR GO; GO:0070922; P:RISC complex assembly; IDA:BHF-UCL.
DR GO; GO:0010501; P:RNA secondary structure unwinding; IDA:BHF-UCL.
DR GO; GO:0007130; P:synaptonemal complex assembly; IEA:Ensembl.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_03033; AGO4; 1.
DR InterPro; IPR028604; AGO4.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR032472; ArgoL2.
DR InterPro; IPR032473; Argonaute_Mid_dom.
DR InterPro; IPR032474; Argonaute_N.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR045246; Piwi_ago-like.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF08699; ArgoL1; 1.
DR Pfam; PF16488; ArgoL2; 1.
DR Pfam; PF16487; ArgoMid; 1.
DR Pfam; PF16486; ArgoN; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM01163; DUF1785; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00950; Piwi; 1.
DR SUPFAM; SSF101690; SSF101690; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW RNA-binding; RNA-mediated gene silencing; Translation regulation;
KW Ubl conjugation.
FT CHAIN 1..861
FT /note="Protein argonaute-4"
FT /id="PRO_0000194063"
FT DOMAIN 225..338
FT /note="PAZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03033"
FT DOMAIN 509..820
FT /note="Piwi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03033"
FT REGION 825..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 25..38
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 43..54
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:6OON"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 117..129
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 146..163
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 186..198
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 200..215
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:6OON"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 384..388
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:6OON"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 456..472
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 493..503
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 520..529
FT /evidence="ECO:0007829|PDB:6OON"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 542..545
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 549..562
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 577..580
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 583..591
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 602..609
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 611..614
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 617..624
FT /evidence="ECO:0007829|PDB:6OON"
FT TURN 637..639
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 644..659
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 664..670
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 675..696
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 703..710
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 717..721
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:6OON"
FT TURN 727..730
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 736..738
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 740..743
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 749..753
FT /evidence="ECO:0007829|PDB:6OON"
FT STRAND 765..772
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 778..788
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 803..818
FT /evidence="ECO:0007829|PDB:6OON"
FT HELIX 841..847
FT /evidence="ECO:0007829|PDB:6OON"
FT TURN 852..856
FT /evidence="ECO:0007829|PDB:6OON"
SQ SEQUENCE 861 AA; 97097 MW; F236FF05047534C1 CRC64;
MEALGPGPPA SLFQPPRRPG LGTVGKPIRL LANHFQVQIP KIDVYHYDVD IKPEKRPRRV
NREVVDTMVR HFKMQIFGDR QPGYDGKRNM YTAHPLPIGR DRVDMEVTLP GEGKDQTFKV
SVQWVSVVSL QLLLEALAGH LNEVPDDSVQ ALDVITRHLP SMRYTPVGRS FFSPPEGYYH
PLGGGREVWF GFHQSVRPAM WNMMLNIDVS ATAFYRAQPI IEFMCEVLDI QNINEQTKPL
TDSQRVKFTK EIRGLKVEVT HCGQMKRKYR VCNVTRRPAS HQTFPLQLEN GQAMECTVAQ
YFKQKYSLQL KYPHLPCLQV GQEQKHTYLP LEVCNIVAGQ RCIKKLTDNQ TSTMIKATAR
SAPDRQEEIS RLVKSNSMVG GPDPYLKEFG IVVHNEMTEL TGRVLPAPML QYGGRNKTVA
TPNQGVWDMR GKQFYAGIEI KVWAVACFAP QKQCREDLLK SFTDQLRKIS KDAGMPIQGQ
PCFCKYAQGA DSVEPMFKHL KMTYVGLQLI VVILPGKTPV YAEVKRVGDT LLGMATQCVQ
VKNVVKTSPQ TLSNLCLKIN AKLGGINNVL VPHQRPSVFQ QPVIFLGADV THPPAGDGKK
PSIAAVVGSM DGHPSRYCAT VRVQTSRQEI SQELLYSQEV IQDLTNMVRE LLIQFYKSTR
FKPTRIIYYR GGVSEGQMKQ VAWPELIAIR KACISLEEDY RPGITYIVVQ KRHHTRLFCA
DKTERVGKSG NVPAGTTVDS TITHPSEFDF YLCSHAGIQG TSRPSHYQVL WDDNCFTADE
LQLLTYQLCH TYVRCTRSVS IPAPAYYARL VAFRARYHLV DKDHDSAEGS HVSGQSNGRD
PQALAKAVQI HHDTQHTMYF A
