ID U3IB34_ANAPP Unreviewed; 3782 AA.
AC U3IB34;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Histone-lysine N-methyltransferase {ECO:0000256|PIRNR:PIRNR010354};
DE EC=2.1.1.364 {ECO:0000256|PIRNR:PIRNR010354};
GN Name=KMT2A {ECO:0000313|Ensembl:ENSAPLP00000004456.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000004456.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000004456.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000004456.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000256|ARBA:ARBA00024515};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC Evidence={ECO:0000256|ARBA:ARBA00024515};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-
CC COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000256|PIRNR:PIRNR010354};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR010354}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. TRX/MLL
CC subfamily. {ECO:0000256|PIRNR:PIRNR010354}.
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DR STRING; 8840.ENSAPLP00000004456; -.
DR Ensembl; ENSAPLT00000005072.2; ENSAPLP00000004456.2; ENSAPLG00000004837.2.
DR GeneTree; ENSGT00940000160099; -.
DR HOGENOM; CLU_000208_2_0_1; -.
DR OMA; DTKMMEC; -.
DR Proteomes; UP000016666; Chromosome 25.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0071339; C:MLL1 complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0140945; F:histone H3K4 monomethyltransferase activity; IEA:RHEA.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0106363; F:protein-cysteine methyltransferase activity; IEA:Ensembl.
DR GO; GO:0045322; F:unmethylated CpG binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:Ensembl.
DR GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
DR GO; GO:0006306; P:DNA methylation; IEA:Ensembl.
DR GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR GO; GO:0045064; P:T-helper 2 cell differentiation; IEA:Ensembl.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:Ensembl.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR CDD; cd05493; Bromo_ALL-1; 1.
DR CDD; cd15693; ePHD_KMT2A; 1.
DR CDD; cd15588; PHD1_KMT2A; 1.
DR CDD; cd15590; PHD2_KMT2A; 1.
DR CDD; cd15592; PHD3_KMT2A; 1.
DR CDD; cd19170; SET_KMT2A_2B; 1.
DR Gene3D; 3.30.160.360; -; 2.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR047219; KMT2A_2B_SET.
DR InterPro; IPR041958; KMT2A_ePHD.
DR InterPro; IPR042023; KMT2A_PHD1.
DR InterPro; IPR042025; KMT2A_PHD2.
DR InterPro; IPR044133; KMT2A_PHD3.
DR InterPro; IPR016569; MeTrfase_trithorax.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR002857; Znf_CXXC.
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; PTHR45838:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE 2A; 1.
DR PANTHER; PTHR45838; HISTONE-LYSINE-N-METHYLTRANSFERASE 2 KMT2 FAMILY MEMBER; 1.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR Pfam; PF13771; zf-HC5HC2H; 1.
DR PIRSF; PIRSF010354; Methyltransferase_trithorax; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 4.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|PIRNR:PIRNR010354};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR010354-51};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR010354};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR010354};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR010354};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR010354};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR010354};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR010354};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR010354-51};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 945..993
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 1225..1276
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1273..1327
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1360..1421
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1497..1542
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1664..1772
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 1812..1868
FT /note="FYR N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51542"
FT DOMAIN 3479..3560
FT /note="FYR C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51543"
FT DOMAIN 3642..3758
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 3766..3782
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1876..1927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..1967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1980..2254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2278..2376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2440..2468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2534..2556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2746..2876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3012..3057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3311..3349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3405..3450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3598..3621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..373
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1641
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1892..1908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..1960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1983..2031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2038..2095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2121..2165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2166..2191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2198..2214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2215..2239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2320..2340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2347..2376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2540..2556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2746..2760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2826..2876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3311..3343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3407..3450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3652
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3654
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3696
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3719..3720
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3722
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3770
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3771
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3772
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3777
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
SQ SEQUENCE 3782 AA; 413203 MW; EF575632017311A0 CRC64;
MEKVKKKELK SGEKRRGRPP TLTSVKFKLS QVKGTSDIQK GSKEEKESLK KIKRSPSTTF
QQATKIKKLR TSKLSPLKSK FKPGAKLQIG RKSVQIVRRR GRPPSSERLK TSSTLVINSQ
LEKPQRIRKE KDGTPPLTKE EKTAVRQSPR RIKPVRIIPS TKRTDATIAK QLLQRAKKGA
QKKIEKEAAK LQGRKGRTQL KNIRQFIMPV VSAISSRIIK TPKRFIEDED YDPPIKISRL
ESTPNSRFSA TSCGSSEKSS AASQHSSQMS SDSSRSSSPS VDTSTDSQAS EEMQTLSEER
SNTPEVHTPL PVSQSPENDN SDRRNRRFSI TERSFGQRTA KKLSALPSVP QQQSSSSPPP
PLLTPPPPLQ PASSISDRTP WLMPPTIPLA SPFLPTSAAP MQEKRKSILR EPTFRWTSLK
HSRSEPQYFS SAKYAKEGLI RKPIFDNFRP PPLTPEDVGF ASGFSTPGAT APARLFSLHS
GTRFDMHKRS PLLRAPRFTP SEAHSRIFES VTLPSSVGRT TTGTAATGVS SRKRKRKVFS
PIRSEPRSPS HSMRTRSGRL STSDLTTLTP QSSVSSSLTS ISVSSLATSA LNSTFTFPSH
SLTQSGESAE RSQRQRKQTS TPAEPFSSSS PAPLFPWFTP SPQTERGRNK DRATEELSKD
KDADKSVEKD KSREKDRERE KENKRESRKE KRRKGSEIQS SSALFPVGKM PKEKVVSEDV
AASSSAKKTA GRRKSTAIDP VADVSTAALV DTTAIKTKTS KKGRGGLDKS DLDLSPTVPS
LEKEKALRLS TPSSSTVKHS ASSISSMLAQ ADKLPMTDKR VASLLKKAKA QLYKIEKSKS
LKQADQPKAQ GQESDSSETS VRGPRIKHVC RRAAVALGRK RAVFPDDMPT LSALPWEERE
KILSSMGNDD KSSIAGSEEA EPLAPPIKPI KPVTRNKTQQ EPPVKKGRRS RRCGQCSGCQ
VPEDCGVCTN CLDKPKFGGR NIKKQCCKMR KCQNLQWMPS KAYLQKQAKA AKKKEKKSKT
NEKKESHSGK NQLDSGQKQT PPTILSREDN AIKKSSEPAR KPVEEKHEDG NSSTPLLEPK
QVPAPGARKT GKQTSQPVQL PPQPPSSGPL KKEAPKLTTS EPKKKQTPQP EIGTEQNKQK
KIAPRPTFPV KQKPKEKEKP PPISKPESST LNLLSTLTNG SSSKQKPPTD GVHRIRVDFK
EDCEVENVWE MGGLGIVTSV PITPRVVCFL CASSGHVEFV YCQVCCEPFH KFCLEESERP
LEDQLENWCC RRCKFCHVCG RQHQATKQLL ECNKCRNSYH PECLGPNYPT KPTKKKKVWI
CTKCVRCKSC GSTTPGKGWD AQWSHDFSLC HDCAKLFAKG NFCPLCDKCY DDDDYESKMM
QCGKCDRWVH SKCENLSDEM YEILSNLPES VAYTCINCTE QHPAEWRLAL EKELQVSLKQ
VLTALLNSRT TSHLLRYRQA AKPPDLNPET EESIPSRSSP EGPDPPVLTE VSKQEEQQPL
DLEGVKRKMD QGGYTSVLDF SDDIVKIIQA AINSDGGQPE VKKANSMVKS FFIRQMERVF
PWFSVKKSRF WEPNKVTSNS GMLPNAVLPP SLDHNYAQWQ EREENNRTEQ PPLMKKIIPA
PKPKGPGEPD SPTPLHPPTP PISSSDRSRE DSPELNPPPD VEDNRQCALC LKYGDDSAND
AGRLLYIGQN EWTHVNCALW SAEVFEDDDG SLKNVHMAVI RGKQLRCEFC QKSGATVGCC
LTSCTSNYHF MCSRAKNCVF LDDKKVYCQR HRDLIKGEVV PENGFEVLRR VFVDFEGISL
RRKFLSGLEP ENIHMMIGSM TIDCLGILND LSDCEDKLFP IGYQCSRVYW STTDARKRCV
YTCKIMECRP PVIEPDINST VEHDDNRTIA HSPVPLTETL SKDSRNAPEI VNPPSPDRPM
HSQTSSSCCY PLVSKGLRIR TPSYPSTQRS PGSRPLPSAG SPTPVTHEIV TVGDPLLSSG
LKSIGSRRHS TSSLSQQQSK LRMISPTRAG NTYSRHSVSS VSNTGSSSEH ELSVKNTDRF
VGSVNSGTTS APVQSCSTSS SSQKTAATSG SKTYQADASQ SSEVKHSSSS DLLAKSAPSK
GEKMKTLTSK DPDYSAHIFA SGGNSKMSTQ PNSSSGTETN VKIGTFQESS GSFSSKETIS
FQSLHQRGPR KDRDQHLEPV QPDKTALVDE MDVKTLKSAG VNSRSPAASE QAVSASRDRR
QKGKKLAKES FKEKHSLKSL ADPSQAVGSD EGNLKSEFGN QGLVTEQISQ RLCNNIPAEK
AGEKSPPSQG SSKGSAVPIE VASKESQAPR KRTVKVTLTP LKMENENQSK AAQQESDAEH
QSAGAELAAS SEPSSESPED NSVVQESPNK APAQESQNNA YENLPVQDNN LMLQDGTKAQ
EESSYKRRYP RRSARARSNM FFGLTPLYGV RSYGEEDIPF YSNSTGKKRG KRSAEGQVDG
ADDLSTSDED DLYYYNFTRT VVPSNTEERL ASHNLFREEE QCDLPKISQL DGVDDGTESD
TSVTATTRKV NQVTKRSGKE NGTENIKLDR TEETGEKVQV TKSPAVHKTD PKIDNCHSVS
RVKTQGQDSL EAQLSSLETG RRAHASTPSD KNLLDTFNTE LLKSDSDNNN SDDCGNILPS
DIMDFVLKNT PSMQALGESP ESSSSELLTL GEGLGLDSNR GKDMGLFEVF SQQLPTAEPV
DSSVSSSISA EEQFELPLEL PSDLSVLTTR SPTVPSQNHN RLAVISESSL SSSGERSILA
LPSTESGEKR VTVTEKSASS EGDTTLLSPG VDPSPEGHMT PDHFIQGHID AEHIASPPCG
PVEQGHGSNQ DLTRNSGTPG IQVPVSPTVP LQNQKYVPNS TDSPGPSQIS NAAVQTTPPH
LKPAAEKLLV VNQNMQPLYV LQTLPNGVTQ KIQLTPSVSS AQSVMETNAS VLGPMGSGLT
LTTGLNPSLP SSQSLFPPTS KGLLPMSHHQ HIHPFSTASQ TGFPPNIGSP SPGLLIGVQP
PPDPQLLVSE ASQRTDLGAT ASTPTAALGK KRPISRLQSR KNKKLAPSGT PSAIAPPDMV
SNMTLINFAP SQISNHPLDL GTIANSTSHR TVPNIIKRSK SGVMYFEQTS LLPQSGTAAA
VGTSPSVIGP DAGHLPTGPV SGLASSSSVL NVVSMQATAA PTTGGSVPSH VLGQSSVTLT
SPGLLGDLGS ISNLLIKASH QSLGLQEPHM TLPPGSGMFS QLGTSQTPST AAMTAASSIC
VLPSAQSMSM TVAQSSAEPE GSYQLQHMTQ LLASKTGIAS SQLDLGAASA TAQLSSFPQL
VDVPSSTGLE QNKVSSSVMH ASSASPGGSP SSGQQSASSS MLGPTKMKPK IKRIQPSLEK
GNGKKHKTSH LWAGSSEAHV PDRGAVAVPQ VSATRTPAVK ADVQDAASID QPSQKQCGQS
AGQMSVLAEP QSTQASANEQ ENAGSKAIEE EESTFSSPLM FWLQQEQKRK ECLGEKKPKK
GLVFEISSDD GFQICAESIE DAWKSLTDKV QEARSNARLK QLSFAGVNGL RMLGIIHDTV
VFLIEQLYGA KHCHNYKFRF HKPEEANEPP LNPHGSARAE VHLRKSAFDM FNFLASKHRQ
PPEYNPNDEE EEEVQLKSAR RATSMDLPMP MRFRHLKKTS KEAVGVYRSP IHGRGLFCKR
NIDAGEMVIE YSGNVIRSIL TDKREKYYDS KGIGCYMFRI DDSEVVDATM HGNAARFINH
SCEPNCYSRV INIDGQKHIV IFAMRKIYRG EELTYDYKFP IEDASNKLPC NCGAKKCRKF
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