KAT8_MOUSE
ID KAT8_MOUSE Reviewed; 458 AA.
AC Q9D1P2; Q3UIY0; Q8BJ69; Q8BJ76; Q8CI73;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Histone acetyltransferase KAT8;
DE EC=2.3.1.48 {ECO:0000269|PubMed:31794431};
DE AltName: Full=Lysine acetyltransferase 8;
DE AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1;
DE Short=MYST-1;
GN Name=Kat8; Synonyms=Mof, Myst1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Amnion, Embryo, Head, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP INTERACTION WITH MSL1 AND NELFD.
RX PubMed=17335777; DOI=10.1016/j.bbrc.2007.02.073;
RA Dmitriev R.I., Korneenko T.V., Bessonov A.A., Shakhparonov M.I.,
RA Modyanov N.N., Pestov N.B.;
RT "Characterization of hampin/MSL1 as a node in the nuclear interactome.";
RL Biochem. Biophys. Res. Commun. 355:1051-1057(2007).
RN [4]
RP INTERACTION WITH MSL1.
RX PubMed=21217699; DOI=10.1038/nsmb.1960;
RA Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S.,
RA Akhtar A.;
RT "Structural basis for MOF and MSL3 recruitment into the dosage compensation
RT complex by MSL1.";
RL Nat. Struct. Mol. Biol. 18:142-149(2011).
RN [5]
RP STRUCTURE BY NMR OF 50-169 (ISOFORM 1).
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the Tudor domain from mouse hypothetical protein
RT homologous to histone acetyltransferase.";
RL Submitted (MAY-2004) to the PDB data bank.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=31794431; DOI=10.1172/jci131145;
RA Li L., Ghorbani M., Weisz-Hubshman M., Rousseau J., Thiffault I.,
RA Schnur R.E., Breen C., Oegema R., Weiss M.M., Waisfisz Q., Welner S.,
RA Kingston H., Hills J.A., Boon E.M., Basel-Salmon L., Konen O.,
RA Goldberg-Stern H., Bazak L., Tzur S., Jin J., Bi X., Bruccoleri M.,
RA McWalter K., Cho M.T., Scarano M., Schaefer G.B., Brooks S.S., Hughes S.S.,
RA van Gassen K.L.I., van Hagen J.M., Pandita T.K., Agrawal P.B.,
RA Campeau P.M., Yang X.J.;
RT "Lysine acetyltransferase 8 is involved in cerebral development and
RT syndromic intellectual disability.";
RL J. Clin. Invest. 130:1431-1445(2020).
CC -!- FUNCTION: Histone acetyltransferase which may be involved in
CC transcriptional activation (PubMed:31794431). May influence the
CC function of ATM. As part of the MSL complex it is involved in
CC acetylation of nucleosomal histone H4 producing specifically H4K16ac
CC (Probable). As part of the NSL complex it may be involved in
CC acetylation of nucleosomal histone H4 on several lysine residues. That
CC activity is less specific than the one of the MSL complex. Can also
CC acetylate TP53/p53 at 'Lys-120' (By similarity).
CC {ECO:0000250|UniProtKB:Q9H7Z6, ECO:0000269|PubMed:31794431,
CC ECO:0000305|PubMed:31794431}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:31794431};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000305|PubMed:31794431};
CC -!- SUBUNIT: Component of a multisubunit histone acetyltransferase complex
CC (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1
CC (By similarity). Component of the NSL complex at least composed of
CC MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and
CC HCFC1 (By similarity). Interacts with KANSL1; the interaction is direct
CC (By similarity). Component of some MLL1/MLL complex, at least composed
CC of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as
CC well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C,
CC KANSL1, LAS1L, MAX, MCRS1, MGA, MOF/KAT8, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10 (By similarity). Interacts with the chromodomain of MORF4L1/MRG15
CC (By similarity). Interacts with ATM (via its Tudor-knot domain) (By
CC similarity). Interacts with MSL1; the interaction is direct
CC (PubMed:21217699, PubMed:17335777). Interacts with MSL3 (By
CC similarity). Interacts with NELFD (PubMed:17335777).
CC {ECO:0000250|UniProtKB:Q9H7Z6, ECO:0000269|PubMed:17335777,
CC ECO:0000269|PubMed:21217699}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:31794431}. Chromosome
CC {ECO:0000305|PubMed:31794431}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D1P2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D1P2-2; Sequence=VSP_014580, VSP_014581;
CC -!- PTM: Autoacetylation at Lys-274 is required for binding histone H4 with
CC high affinity and for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- DISRUPTION PHENOTYPE: Cerebrum-specific knockout of the gene resulted
CC in impaired postnatal growth, hyperactive behavior, and early death.
CC Analysis of mutant mice at various stages of embryonic development
CC showed cerebral hypoplasia with defects in neocortical lamination,
CC abnormal neuronal differentiation with decreased neuronal progenitor
CC cells, and aberrant neuronal migration. These defects were associated
CC with impaired cell proliferation, increased apoptosis, defective
CC neurosphere formation in vitro, and decreased H4K16 propionylation and
CC acetylation in the cerebrocortical neuroepithelium.
CC {ECO:0000269|PubMed:31794431}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25539.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK003264; BAB22680.1; -; mRNA.
DR EMBL; AK018002; BAC25539.1; ALT_FRAME; mRNA.
DR EMBL; AK029350; BAC26411.1; -; mRNA.
DR EMBL; AK146710; BAE27376.1; -; mRNA.
DR EMBL; BC036284; AAH36284.1; -; mRNA.
DR CCDS; CCDS21885.1; -. [Q9D1P2-1]
DR RefSeq; NP_080646.1; NM_026370.1. [Q9D1P2-1]
DR PDB; 1WGS; NMR; -; A=50-169.
DR PDBsum; 1WGS; -.
DR AlphaFoldDB; Q9D1P2; -.
DR BMRB; Q9D1P2; -.
DR SMR; Q9D1P2; -.
DR BioGRID; 212433; 35.
DR ComplexPortal; CPX-859; MSL histone acetyltransferase complex.
DR ComplexPortal; CPX-875; NSL histone acetyltransferase complex.
DR IntAct; Q9D1P2; 32.
DR MINT; Q9D1P2; -.
DR STRING; 10090.ENSMUSP00000033070; -.
DR iPTMnet; Q9D1P2; -.
DR PhosphoSitePlus; Q9D1P2; -.
DR EPD; Q9D1P2; -.
DR jPOST; Q9D1P2; -.
DR MaxQB; Q9D1P2; -.
DR PaxDb; Q9D1P2; -.
DR PeptideAtlas; Q9D1P2; -.
DR PRIDE; Q9D1P2; -.
DR ProteomicsDB; 269179; -. [Q9D1P2-1]
DR ProteomicsDB; 269180; -. [Q9D1P2-2]
DR Antibodypedia; 27640; 305 antibodies from 38 providers.
DR DNASU; 67773; -.
DR Ensembl; ENSMUST00000033070; ENSMUSP00000033070; ENSMUSG00000030801. [Q9D1P2-1]
DR GeneID; 67773; -.
DR KEGG; mmu:67773; -.
DR UCSC; uc009jxg.1; mouse. [Q9D1P2-2]
DR UCSC; uc009jxh.1; mouse. [Q9D1P2-1]
DR CTD; 84148; -.
DR MGI; MGI:1915023; Kat8.
DR VEuPathDB; HostDB:ENSMUSG00000030801; -.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00940000159512; -.
DR HOGENOM; CLU_011815_2_1_1; -.
DR InParanoid; Q9D1P2; -.
DR OMA; MNMVKYW; -.
DR OrthoDB; 629545at2759; -.
DR PhylomeDB; Q9D1P2; -.
DR TreeFam; TF317619; -.
DR BRENDA; 2.3.1.48; 3474.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 67773; 27 hits in 71 CRISPR screens.
DR ChiTaRS; Kat8; mouse.
DR EvolutionaryTrace; Q9D1P2; -.
DR PRO; PR:Q9D1P2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D1P2; protein.
DR Bgee; ENSMUSG00000030801; Expressed in seminiferous tubule of testis and 227 other tissues.
DR ExpressionAtlas; Q9D1P2; baseline and differential.
DR Genevisible; Q9D1P2; MM.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0072487; C:MSL complex; ISS:UniProtKB.
DR GO; GO:0044545; C:NSL complex; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0046972; F:histone acetyltransferase activity (H4-K16 specific); IMP:UniProtKB.
DR GO; GO:0043995; F:histone acetyltransferase activity (H4-K5 specific); ISS:UniProtKB.
DR GO; GO:0043996; F:histone acetyltransferase activity (H4-K8 specific); ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; ISO:MGI.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IMP:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0030099; P:myeloid cell differentiation; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IDA:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR037906; KAT8.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR PANTHER; PTHR10615:SF82; PTHR10615:SF82; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Acyltransferase;
KW Alternative splicing; Chromatin regulator; Chromosome; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT CHAIN 2..458
FT /note="Histone acetyltransferase KAT8"
FT /id="PRO_0000051567"
FT DOMAIN 55..110
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 174..447
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 207..232
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..458
FT /note="Sufficient for interaction with KANSL1"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT ACT_SITE 350
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 317..319
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 324..330
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 354
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 363
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 432
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI06"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI06"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 274
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT VAR_SEQ 155..194
FT /note="TYAEMDPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYF -> VLAPPFSG
FT PSQQSHSNSHVKAGSMPGFFSRLFTYEKILSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014580"
FT VAR_SEQ 195..458
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014581"
FT CONFLICT 385
FT /note="L -> F (in Ref. 2; AAH36284)"
FT /evidence="ECO:0000305"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1WGS"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1WGS"
FT STRAND 69..81
FT /evidence="ECO:0007829|PDB:1WGS"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:1WGS"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1WGS"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1WGS"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1WGS"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1WGS"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1WGS"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1WGS"
SQ SEQUENCE 458 AA; 52574 MW; FA25E0C8D7E46CEC CRC64;
MAAQGATAAV AATTSGTVGE GEPGPGENAA VEGPARSPGR VSPPTPARGE PEVTVEIGET
YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL DEWVDKNRLA LTKTVKDAVQ
KNSEKYLSEL AEQPERKITR NQKRKHDEIN HVQKTYAEMD PTTAALEKEH EAITKVKYVD
KIHIGNYEID AWYFSPFPED YGKQPKLWLC EYCLKYMKFE KSYRFHLGQC QWRQPPGKEI
YRKSNISVYE VDGKDHKIYC QNLCLLAKLF LDHKTLYFDV EPFVFYILTE VDRQGAHIVG
YFSKEKESPD GNNVACILTL PPYQRRGYGK FLIAFSYELS KLESTVGSPE KPLSDLGKLS
YRSYWSWVLL EILRDFRGTL SIKDLSQMTS ITQNDIISTL QSLNMVKYWK GQHVICVTPK
LVEEHLKSAQ YKKPPITVDS VCLKWAPPKH KQVKLSKK
