ID AGO2_MOUSE Reviewed; 860 AA. AC Q8CJG0; A1A563; Q4VAB3; Q571J6; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 05-OCT-2016, entry version 126. DE RecName: Full=Protein argonaute-2 {ECO:0000255|HAMAP-Rule:MF_03031}; DE Short=Argonaute2 {ECO:0000255|HAMAP-Rule:MF_03031}; DE Short=mAgo2; DE EC=3.1.26.n2 {ECO:0000255|HAMAP-Rule:MF_03031}; DE AltName: Full=Argonaute RISC catalytic component 2; DE AltName: Full=Eukaryotic translation initiation factor 2C 2 {ECO:0000255|HAMAP-Rule:MF_03031}; DE Short=eIF-2C 2 {ECO:0000255|HAMAP-Rule:MF_03031}; DE Short=eIF2C 2 {ECO:0000255|HAMAP-Rule:MF_03031}; DE AltName: Full=Piwi/argonaute family protein meIF2C2; DE AltName: Full=Protein slicer {ECO:0000255|HAMAP-Rule:MF_03031}; GN Name=Ago2; Synonyms=Eif2c2, Kiaa4215; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12526743; DOI=10.1016/S0960-9822(02)01394-5; RA Doi N., Zenno S., Ueda R., Ohki-Hamazaki H., Ui-Tei K., Saigo K.; RT "Short-interfering-RNA-mediated gene silencing in mammalian cells RT requires Dicer and eIF2C translation initiation factors."; RL Curr. Biol. 13:41-46(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=B5/EGFP; TISSUE=Trophoblast stem cell; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-860. RC TISSUE=Embryonic tail; RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., RA Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene. RT The complete nucleotide sequences of mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=15284456; DOI=10.1126/science.1102513; RA Liu J., Carmell M.A., Rivas F.V., Marsden C.G., Thomson J.M., RA Song J.-J., Hammond S.M., Joshua-Tor L., Hannon G.J.; RT "Argonaute2 is the catalytic engine of mammalian RNAi."; RL Science 305:1437-1441(2004). RN [5] RP INTERACTION WITH DICER1 AND TARBP2. RX PubMed=16357216; DOI=10.1101/gad.1384005; RA Maniataki E., Mourelatos Z.; RT "A human, ATP-independent, RISC assembly machine fueled by pre- RT miRNA."; RL Genes Dev. 19:2979-2990(2005). RN [6] RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16800626; DOI=10.1021/bi060474w; RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., RA Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., RA Squier T.C., Bigelow D.J.; RT "Endogenously nitrated proteins in mouse brain: links to RT neurodegenerative disease."; RL Biochemistry 45:8009-8022(2006). RN [7] RP FUNCTION. RX PubMed=17626790; DOI=10.1101/gad.1565607; RA O'Carroll D., Mecklenbrauker I., Das P.P., Santana A., Koenig U., RA Enright A.J., Miska E.A., Tarakhovsky A.; RT "A Slicer-independent role for Argonaute 2 in hematopoiesis and the RT microRNA pathway."; RL Genes Dev. 21:1999-2004(2007). RN [8] RP FUNCTION. RX PubMed=19174539; DOI=10.1101/gad.1749809; RA Su H., Trombly M.I., Chen J., Wang X.; RT "Essential and overlapping functions for mammalian Argonautes in RT microRNA silencing."; RL Genes Dev. 23:304-317(2009). RN [9] RP INTERACTION WITH TRIM71. RX PubMed=19898466; DOI=10.1038/ncb1987; RA Rybak A., Fuchs H., Hadian K., Smirnova L., Wulczyn E.A., Michel G., RA Nitsch R., Krappmann D., Wulczyn F.G.; RT "The let-7 target gene mouse lin-41 is a stem cell specific E3 RT ubiquitin ligase for the miRNA pathway protein Ago2."; RL Nat. Cell Biol. 11:1411-1420(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, and Spleen; 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 RT expression."; RL Cell 143:1174-1189(2010). RN [11] RP INTERACTION WITH TRIM71. RX PubMed=22508726; DOI=10.1101/gad.187641.112; RA Chen J., Lai F., Niswander L.; RT "The ubiquitin ligase mLin41 temporally promotes neural progenitor RT cell maintenance through FGF signaling."; RL Genes Dev. 26:803-815(2012). RN [12] RP INTERACTION WITH TRIM71. RX PubMed=22735451; DOI=10.1038/ncomms1909; RA Chang H.M., Martinez N.J., Thornton J.E., Hagan J.P., Nguyen K.D., RA Gregory R.I.; RT "Trim71 cooperates with microRNAs to repress Cdkn1a expression and RT promote embryonic stem cell proliferation."; RL Nat. Commun. 3:923-923(2012). CC -!- FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the CC RNA-induced silencing complex (RISC). The 'minimal RISC' appears CC to include AGO2 bound to a short guide RNA such as a microRNA CC (miRNA) or short interfering RNA (siRNA). These guide RNAs direct CC RISC to complementary mRNAs that are targets for RISC-mediated CC gene silencing. The precise mechanism of gene silencing depends on CC the degree of complementarity between the miRNA or siRNA and its CC target. Binding of RISC to a perfectly complementary mRNA CC generally results in silencing due to endonucleolytic cleavage of CC the mRNA specifically by AGO2. Binding of RISC to a partially CC complementary mRNA results in silencing through inhibition of CC translation, and this is independent of endonuclease activity. May CC inhibit translation initiation by binding to the 7-methylguanosine CC cap, thereby preventing the recruitment of the translation CC initiation factor eIF4-E. May also inhibit translation initiation CC via interaction with EIF6, which itself binds to the 60S ribosomal CC subunit and prevents its association with the 40S ribosomal CC subunit. The inhibition of translational initiation leads to the CC accumulation of the affected mRNA in cytoplasmic processing bodies CC (P-bodies), where mRNA degradation may subsequently occur. In some CC cases RISC-mediated translational repression is also observed for CC miRNAs that perfectly match the 3' untranslated region (3'-UTR). CC Can also up-regulate the translation of specific mRNAs under CC certain growth conditions. Binds to the AU element of the 3'-UTR CC of the TNF (TNF-alpha) mRNA and up-regulates translation under CC conditions of serum starvation. Also required for transcriptional CC gene silencing (TGS), in which short RNAs known as antigene RNAs CC or agRNAs direct the transcriptional repression of complementary CC promoter regions. Regulates lymphoid and erythroid development and CC function, and this is independent of endonuclease activity. CC {ECO:0000255|HAMAP-Rule:MF_03031, ECO:0000269|PubMed:15284456, CC ECO:0000269|PubMed:17626790, ECO:0000269|PubMed:19174539}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_03031}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- SUBUNIT: Interacts with DICER1 through its Piwi domain and with CC TARBP2 during assembly of the RNA-induced silencing complex CC (RISC). Together, DICER1, AGO2 and TARBP2 constitute the trimeric CC RISC loading complex (RLC), or micro-RNA (miRNA) loading complex CC (miRLC). Within the RLC/miRLC, DICER1 and TARBP2 are required to CC process precursor miRNAs (pre-miRNAs) to mature miRNAs and then CC load them onto AGO2. AGO2 bound to the mature miRNA constitutes CC the minimal RISC and may subsequently dissociate from DICER1 and CC TARBP2. Note however that the term RISC has also been used to CC describe the trimeric RLC/miRLC. The formation of RISC complexes CC containing siRNAs rather than miRNAs appears to occur CC independently of DICER1 (PubMed:16357216). Interacts with AGO1. CC Also interacts with DDB1, DDX5, DDX6, DDX20, DHX30, DHX36, DDX47, CC DHX9, ELAVL, FXR1, GEMIN4, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, CC PABPC1, PRMT5, P4HA1, P4HB, RBM4, SART3, TNRC6A, TNRC6B, UPF1 and CC YBX1. Interacts with the P-body components DCP1A and XRN1. CC Associates with polysomes and messenger ribonucleoproteins CC (mNRPs). Interacts with RBM4; the interaction is modulated under CC stress-induced conditions, occurs under both cell proliferation CC and differentiation conditions and in an RNA- and phosphorylation- CC independent manner. Interacts with LIMD1, WTIP and AJUBA (By CC similarity). Interacts with TRIM71 (PubMed:19898466, CC PubMed:22508726, PubMed:22735451). Interacts with APOBEC3G in an CC RNA-dependent manner. Interacts with APOBEC3A, APOBEC3C, APOBEC3F CC and APOBEC3H. Interacts with DICER1, TARBP2, EIF6, MOV10 and RPL7A CC (60S ribosome subunit); they form a large RNA-induced silencing CC complex (RISC). Interacts with FMR1. {ECO:0000255|HAMAP- CC Rule:MF_03031, ECO:0000269|PubMed:16357216, CC ECO:0000269|PubMed:19898466, ECO:0000269|PubMed:22508726, CC ECO:0000269|PubMed:22735451}. CC -!- INTERACTION: CC Q9UPY3:DICER1 (xeno); NbExp=2; IntAct=EBI-528299, EBI-395506; CC Q4VGL6:Rc3h1; NbExp=2; IntAct=EBI-528299, EBI-2366263; CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP- CC Rule:MF_03031}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03031}. CC Note=Translational repression of mRNAs results in their CC recruitment to P-bodies. Translocation to the nucleus requires CC IMP8. {ECO:0000255|HAMAP-Rule:MF_03031}. CC -!- TISSUE SPECIFICITY: Ubiquitous expression in 9.5 day embryos with CC highest levels in forebrain, heart, limb buds, and branchial CC arches. {ECO:0000269|PubMed:15284456}. CC -!- DOMAIN: The Piwi domain may perform RNA cleavage by a mechanism CC similar to that of RNase H. However, while RNase H utilizes a CC triad of Asp-Asp-Glu (DDE) for metal ion coordination, this CC protein appears to utilize a triad of Asp-Asp-His (DDH). CC {ECO:0000255|HAMAP-Rule:MF_03031}. CC -!- PTM: Hydroxylated. 4-hydroxylation appears to enhance protein CC stability but is not required for miRNA-binding or endonuclease CC activity. {ECO:0000255|HAMAP-Rule:MF_03031}. CC -!- DISRUPTION PHENOTYPE: Embryonic death with a strong defect in CC neural tube closure and apparent cardiac failure. CC {ECO:0000269|PubMed:15284456}. CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily. CC {ECO:0000255|HAMAP-Rule:MF_03031}. CC -!- SIMILARITY: Contains 1 PAZ domain. {ECO:0000255|HAMAP- CC Rule:MF_03031}. CC -!- SIMILARITY: Contains 1 Piwi domain. {ECO:0000255|HAMAP- CC Rule:MF_03031}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH96465.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB081472; BAC15767.1; -; mRNA. DR EMBL; BC096465; AAH96465.1; ALT_INIT; mRNA. DR EMBL; BC128379; AAI28380.1; -; mRNA. DR EMBL; BC129922; AAI29923.1; -; mRNA. DR EMBL; AK220193; BAD90378.1; -; mRNA. DR CCDS; CCDS37098.1; -. DR RefSeq; NP_694818.3; NM_153178.4. DR UniGene; Mm.23095; -. DR UniGene; Mm.391971; -. DR UniGene; Mm.440409; -. DR UniGene; Mm.476931; -. DR UniGene; Mm.486474; -. DR UniGene; Mm.490340; -. DR ProteinModelPortal; Q8CJG0; -. DR SMR; Q8CJG0; 223-390. DR BioGrid; 232092; 7. DR DIP; DIP-35014N; -. DR IntAct; Q8CJG0; 51. DR STRING; 10090.ENSMUSP00000042207; -. DR iPTMnet; Q8CJG0; -. DR PhosphoSite; Q8CJG0; -. DR EPD; Q8CJG0; -. DR MaxQB; Q8CJG0; -. DR PaxDb; Q8CJG0; -. DR PeptideAtlas; Q8CJG0; -. DR PRIDE; Q8CJG0; -. DR Ensembl; ENSMUST00000044113; ENSMUSP00000042207; ENSMUSG00000036698. DR GeneID; 239528; -. DR KEGG; mmu:239528; -. DR UCSC; uc007wbu.2; mouse. DR CTD; 27161; -. DR MGI; MGI:2446632; Ago2. DR eggNOG; KOG1041; Eukaryota. DR eggNOG; ENOG410XP07; LUCA. DR GeneTree; ENSGT00760000119148; -. DR HOGENOM; HOG000116043; -. DR HOVERGEN; HBG006101; -. DR InParanoid; Q8CJG0; -. DR KO; K11593; -. DR OMA; IPGYAFK; -. DR OrthoDB; EOG091G020J; -. DR TreeFam; TF101510; -. DR Reactome; R-MMU-203927; MicroRNA (miRNA) biogenesis. DR Reactome; R-MMU-426486; Small interfering RNA (siRNA) biogenesis. DR Reactome; R-MMU-426496; Post-transcriptional silencing by small RNAs. DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs. DR PRO; PR:Q8CJG0; -. DR Proteomes; UP000000589; Chromosome 15. DR Bgee; ENSMUSG00000036698; -. DR CleanEx; MM_EIF2C2; -. DR Genevisible; Q8CJG0; MM. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0000932; C:cytoplasmic mRNA processing body; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0030425; C:dendrite; IDA:MGI. DR GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0035068; C:micro-ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005844; C:polysome; ISS:UniProtKB. DR GO; GO:0016442; C:RISC complex; IDA:BHF-UCL. DR GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB. DR GO; GO:0001047; F:core promoter binding; ISO:MGI. DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI. DR GO; GO:0004521; F:endoribonuclease activity; IDA:MGI. DR GO; GO:0090624; F:endoribonuclease activity, cleaving miRNA-paired mRNA; ISO:MGI. DR GO; GO:0070551; F:endoribonuclease activity, cleaving siRNA-paired mRNA; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035198; F:miRNA binding; IDA:MGI. DR GO; GO:0003729; F:mRNA binding; IDA:MGI. DR GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI. DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI. DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:MGI. DR GO; GO:0000993; F:RNA polymerase II core binding; ISO:MGI. DR GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI. DR GO; GO:0035197; F:siRNA binding; ISS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB. DR GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; ISO:MGI. DR GO; GO:0035278; P:miRNA mediated inhibition of translation; ISS:UniProtKB. DR GO; GO:0010586; P:miRNA metabolic process; IDA:MGI. DR GO; GO:0035279; P:mRNA cleavage involved in gene silencing by miRNA; ISS:UniProtKB. DR GO; GO:0090625; P:mRNA cleavage involved in gene silencing by siRNA; ISO:MGI. DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI. DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:UniProtKB. DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB. DR GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:MGI. DR GO; GO:0010501; P:RNA secondary structure unwinding; ISO:MGI. DR GO; GO:0035087; P:siRNA loading onto RISC involved in RNA interference; ISO:MGI. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_03031; AGO2; 1. DR InterPro; IPR028602; AGO2. 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; IPR003165; Piwi. DR InterPro; IPR012337; RNaseH-like_dom. 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 Complete proteome; Cytoplasm; Developmental protein; Differentiation; KW Endonuclease; Hydrolase; Hydroxylation; Magnesium; Manganese; KW Metal-binding; Nitration; Nuclease; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; Ribonucleoprotein; RNA-binding; KW RNA-mediated gene silencing; Transcription; Transcription regulation; KW Translation regulation. FT CHAIN 1 860 Protein argonaute-2. FT /FTId=PRO_0000194058. FT DOMAIN 236 349 PAZ. {ECO:0000255|HAMAP-Rule:MF_03031}. FT DOMAIN 518 819 Piwi. {ECO:0000255|HAMAP-Rule:MF_03031}. FT REGION 312 317 Interaction with guide RNA. FT {ECO:0000250}. FT REGION 525 567 Interaction with guide RNA. FT {ECO:0000250}. FT REGION 588 591 Interaction with GW182 family members. FT {ECO:0000255}. FT REGION 651 661 Interaction with GW182 family members. FT {ECO:0000255}. FT REGION 710 711 Interaction with guide RNA. FT {ECO:0000250}. FT REGION 754 762 Interaction with guide RNA. FT {ECO:0000250}. FT REGION 791 813 Interaction with guide RNA. FT {ECO:0000250}. FT METAL 598 598 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_03031}. FT METAL 670 670 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_03031}. FT METAL 808 808 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_03031}. FT MOD_RES 2 2 Nitrated tyrosine. FT {ECO:0000244|PubMed:16800626}. FT MOD_RES 388 388 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9UKV8}. FT MOD_RES 701 701 4-hydroxyproline. {ECO:0000255|HAMAP- FT Rule:MF_03031}. FT MOD_RES 825 825 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H9G7}. FT MOD_RES 829 829 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9UKV8}. FT CONFLICT 65 65 E -> G (in Ref. 2; AAH96465). FT {ECO:0000305}. FT CONFLICT 67 67 C -> R (in Ref. 1; BAC15767). FT {ECO:0000305}. FT CONFLICT 129 129 F -> L (in Ref. 1; BAC15767). FT {ECO:0000305}. FT CONFLICT 360 360 N -> D (in Ref. 1; BAC15767). FT {ECO:0000305}. FT CONFLICT 563 563 N -> D (in Ref. 2; AAH96465). FT {ECO:0000305}. FT CONFLICT 711 711 R -> P (in Ref. 2; AAH96465). FT {ECO:0000305}. FT CONFLICT 761 761 S -> G (in Ref. 1; BAC15767). FT {ECO:0000305}. SQ SEQUENCE 860 AA; 97304 MW; A4E13C633846062C CRC64; MYSGAGPVLA SPAPTTSPIP GYAFKPPPRP DFGTTGRTIK LQANFFEMDI PKIDIYHYEL DIKPEKCPRR VNREIVEHMV QHFKTQIFGD RKPVFDGRKN LYTAMPLPIG RDKVELEVTL PGEGKDRIFK VSIKWVSCVS LQALHDALSG RLPSVPFETI QALDVVMRHL PSMRYTPVGR SFFTASEGCS NPLGGGREVW FGFHQSVRPS LWKMMLNIDV SATAFYKAQP VIEFVCEVLD FKSIEEQQKP LTDSQRVKFT KEIKGLKVEI THCGQMKRKY RVCNVTRRPA SHQTFPLQQE SGQTVECTVA QYFKDRHKLV LRYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN QTSTMIRATA RSAPDRQEEI SKLMRSASFN TDPYVREFGI MVKDEMTDVT GRVLQPPSIL YGGRNKAIAT PVQGVWDMRN KQFHTGIEIK VWAIACFAPQ RQCTEVHLKS FTEQLRKISR DAGMPIQGQP CFCKYAQGAD SVEPMFRHLK NTYAGLQLVV VILPGKTPVY AEVKRVGDTV LGMATQCVQM KNVQRTTPQT LSNLCLKINV KLGGVNNILL PQGRPPVFQQ PVIFLGADVT HPPAGDGKKP SIAAVVGSMD AHPNRYCATV RVQQHRQEII QDLAAMVREL LIQFYKSTRF KPTRIIFYRD GVSEGQFQQV LHHELLAIRE ACIKLEKDYQ PGITFIVVQK RHHTRLFCTD KNERVGKSGN IPAGTTVDTK ITHPTEFDFY LCSHAGIQGT SRPSHYHVLW DDNRFSSDEL QILTYQLCHT YVRCTRSVSI PAPAYYAHLV AFRARYHLVD KEHDSAEGSH TSGQSNGRDH QALAKAVQVH QDTLRTMYFA //