ID I3L9U8_PIG Unreviewed; 2420 AA.
AC I3L9U8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=EP300 {ECO:0000313|Ensembl:ENSSSCP00000020812.3,
GN ECO:0000313|VGNC:VGNC:87720};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000020812.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000020812.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000020812.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000020812.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR SMR; I3L9U8; -.
DR STRING; 9823.ENSSSCP00000020812; -.
DR PaxDb; 9823-ENSSSCP00000020812; -.
DR Ensembl; ENSSSCT00000026332.3; ENSSSCP00000020812.3; ENSSSCG00000000068.5.
DR VGNC; VGNC:87720; EP300.
DR eggNOG; KOG1778; Eukaryota.
DR GeneTree; ENSGT00940000155497; -.
DR HOGENOM; CLU_000162_2_0_1; -.
DR InParanoid; I3L9U8; -.
DR TreeFam; TF101097; -.
DR Reactome; R-SSC-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-SSC-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-SSC-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR Reactome; R-SSC-3371568; Attenuation phase.
DR Reactome; R-SSC-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-SSC-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-SSC-5689901; Metalloprotease DUBs.
DR Reactome; R-SSC-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SSC-6782135; Dual incision in TC-NER.
DR Reactome; R-SSC-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SSC-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-SSC-6804760; Regulation of TP53 Activity through Methylation.
DR Reactome; R-SSC-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-SSC-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR Reactome; R-SSC-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-SSC-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-SSC-8941856; RUNX3 regulates NOTCH signaling.
DR Reactome; R-SSC-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-SSC-8951936; RUNX3 regulates p14-ARF.
DR Reactome; R-SSC-9018519; Estrogen-dependent gene expression.
DR Reactome; R-SSC-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-SSC-933541; TRAF6 mediated IRF7 activation.
DR Reactome; R-SSC-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR Reactome; R-SSC-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-SSC-9759194; Nuclear events mediated by NFE2L2.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000000068; Expressed in lung and 43 other cell types or tissues.
DR Genevisible; I3L9U8; SS.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0140033; F:acetylation-dependent protein binding; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0140069; F:histone butyryltransferase activity; IEA:Ensembl.
DR GO; GO:0140068; F:histone crotonyltransferase activity; IEA:Ensembl.
DR GO; GO:0044013; F:histone H2B acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0140908; F:histone H3K122 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043993; F:histone H3K18 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0044017; F:histone H3K27 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0010485; F:histone H4 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0120301; F:histone lactyltransferase activity; IEA:Ensembl.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IEA:Ensembl.
DR GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IEA:Ensembl.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IEA:Ensembl.
DR GO; GO:0061920; F:protein propionyltransferase activity; IEA:Ensembl.
DR GO; GO:0097677; F:STAT family protein binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0002209; P:behavioral defense response; IEA:Ensembl.
DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0071233; P:cellular response to leucine; IEA:Ensembl.
DR GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl.
DR GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:Ensembl.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030220; P:platelet formation; IEA:Ensembl.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006110; P:regulation of glycolytic process; IEA:Ensembl.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IEA:Ensembl.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0036268; P:swimming; IEA:Ensembl.
DR GO; GO:0001966; P:thigmotaxis; IEA:Ensembl.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:Ensembl.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd20910; NCBD_CREBBP-p300_like; 1.
DR CDD; cd15646; PHD_p300; 1.
DR CDD; cd15802; RING_CBP-p300; 1.
DR CDD; cd02337; ZZ_CBP; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR Gene3D; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking domain; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF29; HISTONE ACETYLTRANSFERASE P300; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF09030; Creb_binding; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF06001; RING_CBP-p300; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00203}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 334..420
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 568..647
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1069..1141
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1289..1665
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1667..1715
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1730..1811
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 334..420
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1730..1811
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1522..1580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1835..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1991..2025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2097..2168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2191..2242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2273..2391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..851
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..903
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1550..1567
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1853..1895
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1913..1928
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1999..2025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2104..2118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2119..2168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2209..2242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2273..2316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2317..2348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2369..2391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2420 AA; 263899 MW; A76E8650E124A61B CRC64;
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD
ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQSMASQAQQ NSPGLGLINS
MVKSPMAQAG LTSPNMGMGT SGPNQGPTPS ATGMMNSPVN QPAMGMNTGM NAGMNPGMLA
AGNGQGMMPN QVMNGSIGAG RGRPNMQYPN PGLANAGNLM TEPLQQGSPQ MGGQTGLRGP
QPLKMGMMNN PNPYGSPYTQ NSGQQMGASG LGLQIPTKSV LPNSLSPFAM DKKAVPGGGM
PNMGQQQAPP PQVQQPGLVT PVAQGMGSGA HTADPEKRKL IQQQLVLLLH AHKCQRREQA
NGEVRQCNLP HCRTMKNVLN HMTHCQSGKS CQVAHCASSR QIISHWKNCT RHDCPVCLPL
KNAGDKRNQQ SILTGAPVGL GNTSSLGVGQ QSTPSLSTVS QIDPSSIERA YAALGLPYQV
NQMPTPPQVQ AKSQNQQSGQ SPQGMRPMSN MSASPMGVNG GVGVQTSNLL SDSMLHSAIN
SQNPMMSENA SVASLGPMPT AAQPSSTGIR KQWHEDITQD LRNHLVHKLV QAIFPTPDPA
ALKDRRMENL VAYARKVEGD MYESANNRAE YYHLLAEKIY KIQKELEEKR RTRLQKQNML
PSAASMVPVS MNPGPNMGQP QPGMTSNGPL PDPSVIRGSV PNQMMPRITP QPGLNQFGQM
SMPQPPIGPR QTSPLQHHGQ LAQPGTLNPP MGYGPRMQQP SSQSQFLPQA QFPAQGMNVT
NMPLAPSGGQ APVSQAQMSS SSCPVNSPIM PPGSQGSHIH CPPLPQPVLH QNSPSPVPSR
TPTPHHTPPS IGAQQPPATA IPAPVPTPPA MPPGPQSQAL HPPPRQTPTP PPTQLPPQVQ
PSLPAAPTAD QPQQQPLSQQ STAASVPTPT APLLPPQPAT PLSQPAVSIE GQVSNPPSTS
STEVNSQNIP EKQPSQEVKM EAKMEVDPPE PADTQPEDIP ETKAEDCKVE PTETEERGTE
LKAETKEEED QPSTSATQSS PAPGQSKKKI FKPDELRQAL MPTLEALYRQ DPESLPFRQP
VDPQLLGIPD YFDIVKSPMD LSTIKRKLDT GQYQEPWQYV DDIWLMFNNA WLYNRKTSRV
YKYCSKLSEV FEQEIDPVMQ SLGYCCGRKL EFSPQTLCCY GKQLCTIPRD ATYYSYQNRY
HFCEKCFNEI QGESVSLGDD PSQPQTTINK EQFSKRKNDT LDPELFVECT ECGRKMHQIC
VLHHEIIWPS GFVCDGCLKK TARTRKENKF SAKRLPSTRL GTFLENRVND FLRRQNHPES
GEVTVRVVHA SDKTVEVKPG MKARFVDSGE MAESFPYRTK ALFAFEEIDG VDLCFFGMHV
QEYGSDCPPP NQRRVYISYL DSVHFFRPKC LRTAVYHEIL IGYLEYVKKL GYTTGHIWAC
PPSEGDDYIF HCHPPDQKIP KPKRLQEWYK KMLDKAVSER IVHDYKDIFK QATEDRLTSA
KELPYFEGDF WPNVLEESIK ELEQEEEERK REENTSSEST DVTKGDSKNA KKKNNKKTSK
NKSSLSRGNK KKPGMPNVSN DLSQKLYATM EKHKEVFFVI RLIAGPAANS LPPIVDPDPL
IPCDLMDGRD AFLTLARDKH LEFSSLRRAQ WSTMCMLVEL HTQSQDRFVY TCNECKHHVE
TRWHCTVCED YDLCITCYNT KNHDHKMEKL GLGLDDESNN QQAAATQSPG DSRRLSIQRC
IQSLVHACQC RNANCSLPSC QKMKRVVQHT KGCKRKTNGG CPICKQLIAL CCYHAKHCQE
NKCPVPFCLN IKQKLRQQQL QHRLQQAQML RRRMASMQRT GVVGQQQGLP SPTPATPTTP
TGQQPATPQT PQPQPPSQPQ PTPPNSMPPY LPRTQAPGPV SQGKAAGQVT PPTPPQTAQP
PLPGPPPAAV EMAMQIQRAA ETQRQMAHVQ IFQRPIQHQM PQMPPMAPMG MNPPPMARGP
SGHLEPGMGP AGMQQQPPWA QGGLPQPQQL QSGMPRPAMM SVSQHGQPLN MAPQPGLGQV
GVSPLKPGTV SQQALQNLLR TLRSPSSPLQ QQQVLSILHA NPQLLAAFIK QRAAKYANSN
PQPLPGQPGM PQGQPGLQPP TMPGQQGVHS GPAMQNMNPL QAGVQRAGLP PQQPQQQLQP
PMGGVSPQAQ QMNVNHSTMP SQFRDILRRQ QMMQQQQQGA GPGIGPGMAN HNQFQQPQGV
GYAPQPQPQP QQRMQHHMQQ IQQGNMGQVG QLPQALGAEA GASLQAYQQR LLQQQMGSPA
QPNPMSPQQH MLPSQAQSPH LQGQQLPSLS NQVRSPQPVP SPRPQSQPPH SSPSPRMQPQ
PSPHHVSPQT SSPHPGLVAA PGNPMEQGHF ASPDQNTMLS QLASNPGMAN LHGASATDLG
LSTENSDLNS NLSQSTLDIH
//
