AGO3_DROME
ID AGO3_DROME Reviewed; 867 AA.
AC Q7PLK0; A4GND8; A4GUJ7; A7YFW6; B6IDV1; B7FNN2; K7WKR9; K7XHY4;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein argonaute-3 {ECO:0000312|EMBL:EAA45981.3};
GN Name=AGO3; ORFNames=CG40300;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABO27430.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), FUNCTION, RNA-BINDING, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17346786; DOI=10.1016/j.cell.2007.01.043;
RA Brennecke J., Aravin A.A., Stark A., Dus M., Kellis M., Sachidanandam R.,
RA Hannon G.J.;
RT "Discrete small RNA-generating loci as master regulators of transposon
RT activity in Drosophila.";
RL Cell 128:1089-1103(2007).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABO26294.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM G), FUNCTION, RNA-BINDING, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17322028; DOI=10.1126/science.1140494;
RA Gunawardane L.S., Saito K., Nishida K.M., Miyoshi K., Kawamura Y.,
RA Nagami T., Siomi H., Siomi M.C.;
RT "A slicer-mediated mechanism for repeat-associated siRNA 5' end formation
RT in Drosophila.";
RL Science 315:1587-1590(2007).
RN [3] {ECO:0000312|EMBL:EAA45981.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000312|EMBL:ACJ13248.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACJ13248.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000312|EMBL:ACJ13248.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 68-861 (ISOFORM D).
RA Fablet M., Akkouche A., Braman V., Vieira C.;
RT "Variability in the piRNA pathway induces a variable load of transposable
RT elements in wild type strains of Drosophila simulans.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000312|EMBL:ABU63676.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 268-762.
RX PubMed=18201385; DOI=10.1186/gb-2008-9-1-r10;
RA Tomoyasu Y., Miller S.C., Tomita S., Schoppmeier M., Grossmann D.,
RA Bucher G.;
RT "Exploring systemic RNA interference in insects: a genome-wide survey for
RT RNAi genes in Tribolium.";
RL Genome Biol. 9:R10.1-R10.22(2008).
RN [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19395009; DOI=10.1016/j.cell.2009.04.027;
RA Li C., Vagin V.V., Lee S., Xu J., Ma S., Xi H., Seitz H., Horwich M.D.,
RA Syrzycka M., Honda B.M., Kittler E.L., Zapp M.L., Klattenhoff C.,
RA Schulz N., Theurkauf W.E., Weng Z., Zamore P.D.;
RT "Collapse of germline piRNAs in the absence of Argonaute3 reveals somatic
RT piRNAs in flies.";
RL Cell 137:509-521(2009).
RN [9] {ECO:0000305}
RP RNA-BINDING, INTERACTION WITH AUB AND TUD, AND METHYLATION AT ARG-4; ARG-68
RP AND ARG-70.
RX PubMed=19959991; DOI=10.1038/emboj.2009.365;
RA Nishida K.M., Okada T.N., Kawamura T., Mituyama T., Kawamura Y.,
RA Inagaki S., Huang H., Chen D., Kodama T., Siomi H., Siomi M.C.;
RT "Functional involvement of Tudor and dPRMT5 in the piRNA processing pathway
RT in Drosophila germlines.";
RL EMBO J. 28:3820-3831(2009).
RN [10] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND METHYLATION.
RX PubMed=19377467; DOI=10.1038/ncb1872;
RA Kirino Y., Kim N., de Planell-Saguer M., Khandros E., Chiorean S.,
RA Klein P.S., Rigoutsos I., Jongens T.A., Mourelatos Z.;
RT "Arginine methylation of Piwi proteins catalysed by dPRMT5 is required for
RT Ago3 and Aub stability.";
RL Nat. Cell Biol. 11:652-658(2009).
RN [11] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SMG; TWIN AND AUB, AND SUBCELLULAR LOCATION.
RX PubMed=20953170; DOI=10.1038/nature09465;
RA Rouget C., Papin C., Boureux A., Meunier A.C., Franco B., Robine N.,
RA Lai E.C., Pelisson A., Simonelig M.;
RT "Maternal mRNA deadenylation and decay by the piRNA pathway in the early
RT Drosophila embryo.";
RL Nature 467:1128-1132(2010).
RN [12] {ECO:0000305}
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20980675; DOI=10.1261/rna.2270710;
RA Nagao A., Mituyama T., Huang H., Chen D., Siomi M.C., Siomi H.;
RT "Biogenesis pathways of piRNAs loaded onto AGO3 in the Drosophila testis.";
RL RNA 16:2503-2515(2010).
RN [13] {ECO:0000305}
RP INTERACTION WITH PAPI, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 68-ARG--ARG-72.
RX PubMed=21447556; DOI=10.1242/dev.059287;
RA Liu L., Qi H., Wang J., Lin H.;
RT "PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in
RT the nuage to silence transposition.";
RL Development 138:1863-1873(2011).
RN [14] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23559253; DOI=10.1126/science.1231965;
RA Perrat P.N., DasGupta S., Wang J., Theurkauf W., Weng Z., Rosbash M.,
RA Waddell S.;
RT "Transposition-driven genomic heterogeneity in the Drosophila brain.";
RL Science 340:91-95(2013).
CC -!- FUNCTION: Acts via the piwi-interacting RNA (piRNA) metabolic process,
CC which mediates the repression of transposable elements during meiosis
CC by forming complexes composed of piRNAs and Piwi proteins and governs
CC the methylation and subsequent repression of transposons. Directly
CC binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by
CC a Dicer-independent mechanism and are primarily derived from
CC transposons and other repeated sequence elements. Associates
CC predominantly with sense piRNAs that contain adenine at nucleotide 10,
CC but shows no preference for uridine at the 5' end. In testis, however,
CC associates with Su(Ste) and AT-chX-1 piRNAs mostly produced from
CC antisense precursors. Shows RNA cleavage activity. In the germline,
CC acts to amplify pools of antisense piRNAs, among others Su(Ste), AT-
CC chX-1 and roo, and to limit sense piRNA accumulation. Forms a complex
CC with smg, twin, aub and specific piRNAs that targets nos mRNA (and
CC probably other maternal mRNAS) for deadenylation promoting its decay
CC during early embryogenesis. Involved in transposon silencing in the
CC adult brain. {ECO:0000269|PubMed:17322028, ECO:0000269|PubMed:17346786,
CC ECO:0000269|PubMed:19395009, ECO:0000269|PubMed:20953170,
CC ECO:0000269|PubMed:20980675, ECO:0000269|PubMed:23559253}.
CC -!- SUBUNIT: Interacts with aub (PubMed:19959991). Interacts (when
CC methylated on arginine residues) with tud (PubMed:19959991). Forms a
CC complex with smg, twin, aub, nos mRNA and piRNAs that target the nos
CC 3'-untranslated region, in early embryos (PubMed:20953170). Interacts
CC (via the N-terminal region when symmetrically methylated on arginine
CC residues) with papi (via C-terminus); this interaction is RNA-
CC independent and may be required for AGO3 localization to the nuage
CC (PubMed:21447556). Interacts with TER94 and tral (PubMed:21447556).
CC {ECO:0000269|PubMed:19959991, ECO:0000269|PubMed:20953170,
CC ECO:0000269|PubMed:21447556}.
CC -!- INTERACTION:
CC Q7PLK0; Q9VQ91: papi; NbExp=6; IntAct=EBI-3431981, EBI-6915287;
CC Q7PLK0; P25823: tud; NbExp=5; IntAct=EBI-3431981, EBI-498741;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17322028,
CC ECO:0000269|PubMed:17346786, ECO:0000269|PubMed:19377467,
CC ECO:0000269|PubMed:19395009, ECO:0000269|PubMed:20953170,
CC ECO:0000269|PubMed:20980675, ECO:0000269|PubMed:21447556}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis. Also found in prominent but discrete foci in the germarium.
CC Unlike other nuage components, does not accumulate at the posterior
CC pole in oocytes and early embryos. In the cytoplasm of syncytial
CC embryos, accumulates in discrete foci. {ECO:0000269|PubMed:17322028,
CC ECO:0000269|PubMed:17346786, ECO:0000269|PubMed:19377467,
CC ECO:0000269|PubMed:19395009, ECO:0000269|PubMed:20953170,
CC ECO:0000269|PubMed:20980675, ECO:0000269|PubMed:21447556}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=D {ECO:0000269|PubMed:10731132, ECO:0000269|Ref.6}; Synonyms=E
CC {ECO:0000303|PubMed:10731132}, F {ECO:0000303|PubMed:10731132};
CC IsoId=Q7PLK0-1; Sequence=Displayed;
CC Name=G {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:17322028};
CC IsoId=Q7PLK0-2; Sequence=VSP_047355;
CC -!- TISSUE SPECIFICITY: In ovary, expressed in germline stem cells,
CC germline cyst cells, nurse cells and oocytes during early stages. Also
CC found in the somatic cap cells of the germarium. In testis, expressed
CC in germline stem cells, primary gonial cells and early spermatocytes.
CC No expression detected in the somatic hub cells at the apical tip of
CC the testis (at protein level). Expressed in neurons throughout the
CC adult brain and in the mushroom body subdivision in the peduncle. In
CC the mushroom body, expressed only in gamma and core alpha-beta neurons.
CC {ECO:0000269|PubMed:17322028, ECO:0000269|PubMed:17346786,
CC ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:20980675,
CC ECO:0000269|PubMed:23559253}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Expression is high in early
CC embryos but gradually decreases as development proceeds (at protein
CC level). {ECO:0000269|PubMed:17322028}.
CC -!- PTM: Symmetrically dimethylated on Arg-4, Arg-68 and Arg-70, most
CC likely by csul. {ECO:0000269|PubMed:19377467,
CC ECO:0000269|PubMed:19959991, ECO:0000303|PubMed:19959991}.
CC -!- DISRUPTION PHENOTYPE: Female sterility. Male semi-sterility accompanied
CC by production of Ste protein crystals in primary spermatocytes. Mutant
CC males fail to maintain germline stem cells.
CC {ECO:0000269|PubMed:19395009, ECO:0000269|PubMed:20980675}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Has been given the gene name AGO3 by FlyBase based on the
CC literature but is more similar to members of the Piwi subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACJ13248.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACK77640.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR EMBL; EF211827; ABO27430.1; -; mRNA.
DR EMBL; EF434174; ABO26294.1; -; mRNA.
DR EMBL; AE014296; ABI31274.2; -; Genomic_DNA.
DR EMBL; AE014296; ABI31275.2; -; Genomic_DNA.
DR EMBL; AE014296; ACZ94769.1; -; Genomic_DNA.
DR EMBL; AE014296; EAA45981.3; -; Genomic_DNA.
DR EMBL; BT050541; ACJ13248.1; ALT_INIT; mRNA.
DR EMBL; BT053722; ACK77640.1; ALT_SEQ; mRNA.
DR EMBL; JX656887; AFX62827.1; -; mRNA.
DR EMBL; JX656888; AFX62828.1; -; mRNA.
DR EMBL; EF688531; ABU63676.1; -; mRNA.
DR RefSeq; NP_001036627.2; NM_001043162.3. [Q7PLK0-1]
DR RefSeq; NP_001036628.2; NM_001043163.3. [Q7PLK0-1]
DR RefSeq; NP_001036629.2; NM_001043164.3. [Q7PLK0-1]
DR RefSeq; NP_001163498.1; NM_001170027.2. [Q7PLK0-2]
DR PDB; 7CFC; X-ray; 2.40 A; F/G/H/I=63-78.
DR PDBsum; 7CFC; -.
DR AlphaFoldDB; Q7PLK0; -.
DR SMR; Q7PLK0; -.
DR BioGRID; 78275; 18.
DR IntAct; Q7PLK0; 7.
DR MINT; Q7PLK0; -.
DR STRING; 7227.FBpp0289159; -.
DR PaxDb; Q7PLK0; -.
DR EnsemblMetazoa; FBtr0299880; FBpp0289158; FBgn0250816. [Q7PLK0-1]
DR EnsemblMetazoa; FBtr0299881; FBpp0289159; FBgn0250816. [Q7PLK0-1]
DR EnsemblMetazoa; FBtr0299882; FBpp0289160; FBgn0250816. [Q7PLK0-1]
DR EnsemblMetazoa; FBtr0301725; FBpp0290939; FBgn0250816. [Q7PLK0-2]
DR GeneID; 3355150; -.
DR KEGG; dme:Dmel_CG40300; -.
DR CTD; 192669; -.
DR FlyBase; FBgn0250816; AGO3.
DR VEuPathDB; VectorBase:FBgn0250816; -.
DR eggNOG; KOG1042; Eukaryota.
DR GeneTree; ENSGT00950000183200; -.
DR HOGENOM; CLU_008813_0_0_1; -.
DR InParanoid; Q7PLK0; -.
DR OMA; EGGLKLC; -.
DR PhylomeDB; Q7PLK0; -.
DR BioGRID-ORCS; 3355150; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 3355150; -.
DR PRO; PR:Q7PLK0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0250816; Expressed in cleaving embryo and 15 other tissues.
DR Genevisible; Q7PLK0; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:FlyBase.
DR GO; GO:0034584; F:piRNA binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0031047; P:gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:FlyBase.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:FlyBase.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 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; Alternative splicing; Cytoplasm; Developmental protein;
KW Methylation; Reference proteome; RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..867
FT /note="Protein argonaute-3"
FT /id="PRO_0000422914"
FT DOMAIN 286..402
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 566..853
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..289
FT /note="Interaction with papi"
FT /evidence="ECO:0000269|PubMed:21447556"
FT MOD_RES 4
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:19959991"
FT MOD_RES 68
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:19959991"
FT MOD_RES 70
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:19959991"
FT VAR_SEQ 840..867
FT /note="YAHKLAYLIGQSIQRDVAEALSEKLFYL -> VSHNYHLIFFKSTMITQDTI
FT NDFTRAL (in isoform G)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:17322028"
FT /id="VSP_047355"
FT MUTAGEN 68..72
FT /note="RGRAR->KGKAK: Abolishes binding to papi."
FT /evidence="ECO:0000269|PubMed:21447556"
FT CONFLICT 42
FT /note="G -> R (in Ref. 1; ABO27430)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="D -> G (in Ref. 6; AFX62827)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="V -> L (in Ref. 6; AFX62828)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="P -> L (in Ref. 6; AFX62828)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="S -> L (in Ref. 6; AFX62828)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="K -> R (in Ref. 6; AFX62828)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="E -> A (in Ref. 6; AFX62827)"
FT /evidence="ECO:0000305"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:7CFC"
SQ SEQUENCE 867 AA; 99129 MW; AE613D6C845F78BE CRC64;
MSGRGNLLSL FNKNAGNMGK SISSKDHEID SGLDFNNSES SGERLLSSHN IETDLITTLQ
HVNISVGRGR ARLIDTLKTD DHTSNQFITS ESKENITKKT KGPESEAIAS ENGLFFPDLI
YGSKGSSVNI YCNYLKLTTD ESKGVFNYEV RFFPPIDSVH LRIKYLNDHK DKLGGTKTFD
GNTLYLPILL PNKMTVFISK AEDVELQIRI LYKKKEEMRN CTQLYNILFD RVMKVLNYVK
FDRKQFDPSR PKIIPLAKLE VWPGYVTAVD EYKGGLMLCC DVSHRILCQK TVLEMLVDLY
QQNVEHYQES ARKMLVGNIV LTRYNNRTYK INDICFDQNP TCQFEIKTGC TSYVEYYKQY
HNINIKDVNQ PLIYSIKKSR GIPAERENLQ FCLIPELCYL TGLRDEVRSD NKLMREIATF
TRVSPNQRQM ALNKFYENVS NTPAAQEILN SWGLSLTNNS NKISGRQMDI EQIYFSKISV
SAGRSAEFSK HAVTNEMLKV VHLSKWIIIH LRNYRQAATS LLDNMKQACE SLGMNISNPT
MISLDHDRID AYIQALRRNI TMNTQMVVCI CHNRRDDRYA AIKKICCSEI PIPSQVINAK
TLQNDLKIRS VVQKIVLQMN CKLGGSLWTV KIPFKNVMIC GIDSYHDPSN RGNSVAAFVA
SINSSYSQWY SKAVVQTKRE EIVNGLSASF EIALKMYRKR NGKLPTNIII YRDGIGDGQL
YTCLNYEIPQ FEMVCGNRIK ISYIVVQKRI NTRIFSGSGI HLENPLPGTV VDQHITKSNM
YDFFLVSQLV RQGTVTPTHY VVLRDDCNYG PDIIQKLSYK LCFLYYNWAG TVRIPACCMY
AHKLAYLIGQ SIQRDVAEAL SEKLFYL
