KAT6A_RAT
ID KAT6A_RAT Reviewed; 1998 AA.
AC Q5TKR9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Histone acetyltransferase KAT6A;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92794};
DE AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3;
DE Short=MYST-3;
DE AltName: Full=Monocytic leukemia zinc finger homolog;
DE AltName: Full=Monocytic leukemia zinc finger protein;
GN Name=Kat6a; Synonyms=Moz, Myst3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-1998.
RC STRAIN=Wistar;
RA Ohta K., Osada S., Nishikawa J., Nishihara T.;
RT "Cloning and characterization of a cDNA encoding histone acetyltransferase
RT MOZ (monocytic leukemia zinc finger protein) from rat.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-900, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Histone acetyltransferase that acetylates lysine residues in
CC histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex
CC which has a histone H3 acetyltransferase activity. May act as a
CC transcriptional coactivator for RUNX1 and RUNX2 (By similarity).
CC Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its
CC transcriptional activity via association with PML (By similarity).
CC {ECO:0000250|UniProtKB:Q92794}.
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:0000250|UniProtKB:Q92794};
CC -!- SUBUNIT: Component of the MOZ/MORF complex composed at least of ING5,
CC KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts
CC with RUNX1; phosphorylation of RUNX1 enhances the interaction.
CC Interacts with RUNX2. Interacts with p53/TP53. Interacts with PML and
CC this interaction positively regulates its acetylation activity towards
CC p53/TP53. {ECO:0000250|UniProtKB:Q92794}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92794}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q92794}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q92794}. Note=Recruited into PML body after DNA
CC damage. {ECO:0000250|UniProtKB:Q92794}.
CC -!- DOMAIN: The N-terminus is involved in transcriptional activation while
CC the C-terminus is involved in transcriptional repression.
CC {ECO:0000250}.
CC -!- PTM: Autoacetylated. Autoacetylation at Lys-602 is required for proper
CC function. {ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- PTM: Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction
CC with PML and negatively regulates its acetylation activity towards
CC p53/TP53. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; AABR03100194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB195309; BAD72833.1; -; mRNA.
DR RefSeq; NP_001094040.1; NM_001100570.2.
DR AlphaFoldDB; Q5TKR9; -.
DR BMRB; Q5TKR9; -.
DR SMR; Q5TKR9; -.
DR STRING; 10116.ENSRNOP00000037279; -.
DR CarbonylDB; Q5TKR9; -.
DR iPTMnet; Q5TKR9; -.
DR PhosphoSitePlus; Q5TKR9; -.
DR PaxDb; Q5TKR9; -.
DR PRIDE; Q5TKR9; -.
DR Ensembl; ENSRNOT00000078743; ENSRNOP00000071789; ENSRNOG00000025174.
DR GeneID; 306571; -.
DR KEGG; rno:306571; -.
DR UCSC; RGD:1304892; rat.
DR CTD; 7994; -.
DR RGD; 1304892; Kat6a.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00940000156962; -.
DR InParanoid; Q5TKR9; -.
DR OrthoDB; 629545at2759; -.
DR PhylomeDB; Q5TKR9; -.
DR TreeFam; TF106483; -.
DR Reactome; R-RNO-3214847; HATs acetylate histones.
DR Reactome; R-RNO-6804758; Regulation of TP53 Activity through Acetylation.
DR PRO; PR:Q5TKR9; -.
DR Proteomes; UP000002494; Chromosome 16.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISO:RGD.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0035909; P:aorta morphogenesis; ISO:RGD.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0035162; P:embryonic hemopoiesis; ISO:RGD.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
DR GO; GO:0016573; P:histone acetylation; ISS:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0030099; P:myeloid cell differentiation; ISS:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:RGD.
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; ISS:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISO:RGD.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR031280; KAT6A.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615:SF26; PTHR10615:SF26; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Acyltransferase; Chromatin regulator;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1998
FT /note="Histone acetyltransferase KAT6A"
FT /id="PRO_0000051574"
FT DOMAIN 95..171
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 502..776
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 199..258
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 255..306
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 535..560
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 1..144
FT /note="Required for activation of RUNX1-1"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT REGION 52..166
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 72..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..662
FT /note="Interaction with PML"
FT /evidence="ECO:0000250"
FT REGION 312..662
FT /note="Interaction with RUNX1-1"
FT /evidence="ECO:0000250"
FT REGION 336..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..776
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 505..808
FT /note="Mediates interaction with BRPF1, required for
FT histone H3 acetyltransferase activity"
FT /evidence="ECO:0000250"
FT REGION 783..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1735
FT /note="Interaction with PML"
FT /evidence="ECO:0000250"
FT REGION 1510..1635
FT /note="Interaction with RUNX1-2"
FT /evidence="ECO:0000250"
FT REGION 1630..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1907..1942
FT /note="Required for activation of RUNX1-2"
FT /evidence="ECO:0000250"
FT COMPBIAS 798..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1028
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1171
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1313
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 678
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 643..647
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT BINDING 652..658
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT BINDING 682
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZ21"
FT MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 355
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 369
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 602
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZ21"
FT MOD_RES 815
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZ21"
FT MOD_RES 900
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 1006
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 1088
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 1089
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 835
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
SQ SEQUENCE 1998 AA; 223331 MW; 37092EED5475855D CRC64;
MVKLANPLYT QWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ LELSVKDGTI
LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQSVDWN KLLKRAFEGL AESGGSTLKS
IERFLKSQKD VSAACGGTAA SGFHQQLRLA IKRAVGHGRL LKDGPLYRLN TKAANAEGKE
GCESLSCLPP VSLLPHEKDK PVAEPIPICS FCLGTKEQNR EKKPEDLISC ADCGNSGHPS
CLKFSPELTV RVRALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQSTVSK GPFSKVRTGP
GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSSAPLK FNKKTKGLID GLTKFFTPSP
DGRKARGEAV DYSELRIRKK GNRKSSTSHW PTDNQDGWES KQESEERLFG SQEIMTERDM
ELFRDIQEQA LQKVGVTGPP DPQVRCPSVI EFGKYEIHTW YSSPYPQEYS RLPKLYLCEF
CLKYMKSRTI LQQHMKKCGW FHPPANEIYR KNNISVFEVD GNVSTIYCQN LCLLAKLFLD
HKTLYYDVEP FLFYVLTQND VKGCHLVGYF SKEKHCQQKY NVSCIMILPQ YQRKGYGRFL
IDFSYLLSKR EGQAGSPEKP LSDLGRLSYM AYWKSVILEC LYHQNDKQIS IKKLSKLTGV
CPQDITSTLH HLRMLDFRSD QFVIIRREKL IQDHMAKLQL NLRPVDVDPE CLRWTPVIVS
NSVVSEEEDE EADDGEKEEP QGQERELETR ERVGKSVSRE NKDQDSSSLI ESEKKPEVKE
LASSSRLSKQ ALVRDSLPAN SQPPRRGRCG RKNRKTQERF GDKDSKMLVG ETLSTSQEQY
GECEEKSAAS RERYTEVGEQ PAAPQAQADG NPDIPKGRFS ESADLWRGQL KKSPETLKCR
LPEGNDRLPC CYTDGDRAVF RGFSESSEEE EEPESPRSNS PPVLTKPTLK RKKPILHRRR
RVRKRKHHNS SVVTETISET TEVLDEPFED SDSERPMPRL EPTFEIEEEE EEEDENELFP
RGYFHCLSSQ DILRCQASSK RTASKDEEEE EEESDDADDT PVLKPVSLLR KCDVNSASLE
PDTSTPMKKK KGWPKGKSRK PIHWKKRPGR KPGFKLNQDI IAVSTQECIV EPIVPIKPGR
KPRTQESEEL VEVKEGLVEE RKEEMHTEAD EEAEEEEDAA SSDIRAMSPL DSSNSPDADP
KEPEAEEEEE KPLDDPRQSE EEPQELEEQE QEEEDEVTAE ANQNEDHDAD DEDDGHLDSL
KTKEPEGQPA REDGTEEPGT QESFLDASIQ DSRENAKDKD ETEADSEEEQ PSHEASVGSE
TMPGSEEDHE EDSNTKEELI ELKEEEEIPH SELDLETVQA VQSLTQEESS EHEGAYQDCE
ETLAACQTLQ SYTHTDEDPQ MSMVEDCHAS EHNSPISSIP SHPSQSVRSV SSPSMPALES
GYTQISPEQG SLSAPSMQNM ETSPMMDVPS VSDHSQQVVD SGFSDLGSIE STTENYENPS
SYDSTMGSSI CGNNSSQSSC SYGGLSSSSS LTQNSCVVTQ QMASMGNSCS MLQQNSVQPA
TNCNIKSPQT CVVERPPSNQ QPPPPPPPPP PPQQPQPQPQ QQAAPQPPPP QPQQQPPPPP
QQQPQPPPPP QQQPPLSQCS MNNSFTAAPM IMEIPESGGT GNISIYERIP GDFGAGSYSQ
PSATFSLAKL QQLTNTIMDP HAMPYSHSPA VTSYATSVSL SNTGLAQLAP SHPLAGTPQA
QATMTPPPNL APTTMNLTSP LLQCNMSATN IGIPHTQRLQ GQMPVKGHIS IRSKSAPLPS
ATAHQQQLYG RSPPAVAMQA GPRALAVQRG MNMGVNLMPT PAYNVNSMNM NTLNAMNSYR
MTQPMMNSSY HSNPAYMNQT AQYPMQMQMG MMGSQAYTQQ PMQPNPHGNM MYTGPSHHSY
MNAAGVPKQS LNGPYMRR
