ID A0A2K6D401_MACNE Unreviewed; 3271 AA.
AC A0A2K6D401;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:ENSMNEP00000030636.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000030636.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000030636.1}
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 Ensembl; ENSMNET00000055054.1; ENSMNEP00000030636.1; ENSMNEG00000038754.1.
DR GeneTree; ENSGT00940000160099; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000038754; Expressed in lymph node and 12 other cell types or tissues.
DR GO; GO:0035097; C:histone methyltransferase complex; IEA:InterPro.
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:0045322; F:unmethylated CpG binding; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; 6.10.250.2390; -; 1.
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; 3.
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:UP000233120};
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 449..497
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 733..784
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 781..835
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 868..929
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1005..1050
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1172..1280
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 3131..3247
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 3255..3271
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1577..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1675..1762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1780..1920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1949..1976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2015..2086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2104..2123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2265..2366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2464..2547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2766..2788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2802..2909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2921..2945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3087..3110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..58
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..619
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1704..1720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1721..1747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1828..1862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1869..1896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2023..2048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2049..2086
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2313..2366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2464..2485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2497..2524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2532..2547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2802..2832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2865..2908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3185
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3208..3209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
SQ SEQUENCE 3271 AA; 355694 MW; 7F2FB4FFB38523F8 CRC64;
MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG PGAPPSPPAV
AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS SGPALLRVGP GFDAALQVSA
AIGTNLRRFR AVFGESGGGG GSGELTTQIP CSWRTKGHIH DKKTEPFRLL AWSWCLNDEQ
FLGFGSDEEV RVRSPTRSPS VKTSPRKPRG RPRSGSDRNS AILSDPSVFS PLNKSETKSG
DKIKKKDSKS IEKKRGRPPT FPGVKIKITH GKDISELPKG NKEDNLKKIK RTPSATFQQA
TKIKKLRAGS MLAQADKLPM TDKRVASLLK KAKAQLCKIE KSKSLKQTDQ PKAQGQESDS
SETSVRGPRI KHVCRRAAVA LGRKRAVFPD DMPTLSALPW EEREKILSSM GNDDKSSIAG
SEDAEPLAPP IKPIKPVTRN KAPQEPPVKK GRRSRRCGQC PGCQVPEDCG VCTNCLDKPK
FGGRNIKKQC CKMRKCQNLQ WMPSKAYLQK QAKAVKKKEK KSKTSEKKES KESSVVKNVV
DSSQKPTPSA REDPAPKKSS SEPPPRKPVE EKSEEGNVSA PGPESKQATI PASRKSSKQV
SQPAPVIPPQ PPTTGPPRKE VPKTTPSEPK KKQPPPPESG PEQSKQKKVA PRPSIPVKQK
PKEKEKPPPV NKQENAGTLN ILSTLSNGNS SKQKIPADGV HRIRVDFKED CEAENVWEMG
GLGILTSVPI TPRVVCFLCA SSGHVEFVYC QVCCEPFHKF CLEENERPLE DQLENWCCRR
CKFCHVCGRQ HQATKQLLEC NKCRNSYHPE CLGPNYPTKP TKKKKVWICT KCVRCKSCGS
TTPGKGWDAQ WSHDFSLCHD CAKLFAKGNF CPLCDKCYDD DDYESKMMQC GKCDRWVHSK
CENLSDEMYE ILSNLPESVA YTCVNCTERH PAEWRLALEK ELQISLKQVL TALLNSRTTS
HLLRYRQAAK PPDLNPETEE SIPSRSSPEG PDPPVLTEVS KQDDQQPLDL EGVKRKMDQG
NYTSVLEFSD DIVKIIQAAI NSDGGQPEIK KANSMVKSFF IRQMERVFPW FSVKKSRFWE
PNKVSSNSGM LPNAVLPPSL DHNYAQWQER EENSHTEQPP LMKKIIPAPK PKGPGEPDSP
TPLHPPTPPI LSTDRSREDS PELNPPPGIE DNRQCALCLT YGDDSANDAG RLLYIGQNEW
THVNCALWSA EVFEDDDGSL KNVHMAVIRG KQLRCEFCQK PGATVGCCLT SCTSNYHFMC
SRAKNCVFLD DKKVYCQRHR DLIKGEVVPE NGFEVFRRVF VDFEGISLRR KFLNGLEPEN
IHMMIGSMTI DCLGILNDLS DCEDKLFPIG YQCSRVYWST TDARKRCVYT CKIVECRPPV
VEPDINSTVE HDENRTIAHS PTSFTESSSK ENQNTAEIIS PPSPDRPPHS QTSGSCYYHV
ISKVPRIRTP SYSPTQRSPG CRPLPSAGSP TPTTHEIVTV GDPLLSSGLR SIGSRRHSTS
SLSPQRSKLR IMSPMRTGNT YSRNNVSSVS TIGTATDLES SAKAVDHVLG PLNSSTSLGQ
NTSTSSNLQR TVVTVGNKNS HLDGSSSSEM KQSSASDLAS KSSSLKGEKT KVLSSKSSEG
SAHNVTYPGI PKLTPQVHNT TSRELNVSKI GSFAEPSSVS FSSKEALSFP HLHLRGQRND
RDQHTDSTQS ANPSPDEDTE VKTLKLSGMS NRSSIINEHM GSSSRDRRQK GKKSCKETFK
EKHSSKSFLE PGQVTTGEEG NLKPEFMDEV LTPEYMGQRP CNNVSSDKIG DKGLSMPGVP
KAPPMQVEGS AKELQAPRKR TVKVTLTPLK MENESQSKNT LKESSPASPL QIESTSPPEP
ISASENPADG PVAQPSPNNT SCQDSQSNNY QNLPVQDRNL MLPDGPKPQE DGSFKRRYPR
RSARARSNMF FGLTPLYGVR SYGEEDIPFY SSSTGKKRGK RSAEGQVDGA DDLSTSDEDD
LYYYNFTRTV ISSGGEERLA SHNLFREEEQ CDLPKISQLD GVDDGTESDT SVTATTRKSS
QIPKRNGKEN GTENLKIDRP EDAGEKEHVI KSSVGHKNEP KMDNCHSVSR VKTQGQDSLE
AQLSSLESSR RVHTSTPSDK NLLDTYNTEL LKSDSDNNNS DDCGNILPSD IMDFVLKNTP
SMQALGESPE SSSSELLNLG EGLGLDSNRE KDMGLFEVFS QQLPTTEPVD SSVSSSISAE
EQFELPLELP SDLSVLTTRS PTVPSQNPSR LAVISDSGEK RVTITEKSVA SSEGDPALLS
PGVDPTPEGH MTPDHFIQGH MDADHISSPP CGSVEQGHGN NQDLTRNSST PGLQVPVSPT
VPIQNQKYVP NSTDSPGPSQ ISNAAVQTTP PHLKPATEKL IVVNQNMQPL YVLQTLPNGV
TQKIQLTSSV SSTPSVMETN TSVLGPMGSG LTLTTGLNPS LPTSQSLFPS ASKGLLPMSH
HQHLHSFPTA TQSSFPPNIS SPPSGLLIGV QPPPDPQLLV SESSQRTDLS TTVATPSSGL
KKRPISRLQT RKNKKLAPSS TPSNIAPSDV VSNMTLINFT PSQLPNHPNL LDLGSLNTSS
HRTVPNIIKR SKSSIMYFEP APLLPQSVGG TAATASGTST ISQDTSHLTS GSVSGLASSS
SVLNVVSMQT TTTPTSSAPV PGHVTLTNPR LLGTPDIGSI SNLLIKASQQ SLGIQDQPVA
LPPSSGMFPQ LGTSQTPSTA AMTAASSICV LPSTQTTGVT AASPSGEADE HYQLQHVNQL
LASKTGIHSS QRDLDSASGP QVSNFTQTVD APNSVGLEQN KALSSAVQAS STSPGGSPSS
PSSGQRSASP SVPGPTKPKP KTKRFQLPLD KGNGKKHKVS HLRTSSSEAH IPDQEATSLT
SGTGTPGAEA EQQDTANVEQ SSQKECGQPA GQVAVLPEVQ VTQNPANEQE STEPKTVEEE
ESNFSSPLML WLQQEQKRKE SITEKKPKKG LVFEISSDDG FQICAESIED AWKSLTDKVQ
EARSNARLKQ LSFAGVNGLR MLGILHDAVV FLIEQLSGAK HCRNYKFRFH KPEEANEPPL
NPHGSARAEV HLRKSAFDMF NFLASKHRQP PEYNPNDEEE EEVQLKSARR ATSMDLPMPM
RFRHLKKTSK EAVGVYRSPI HGRGLFCKRN IDAGEMVIEY AGNVIRSIQT DKREKYYDSK
GIGCYMFRID DSEVVDATMH GNAARFINHS CEPNCYSRVI NIDGQKHIVI FAMRKIYRGE
ELTYDYKFPI EDASNKLPCN CGAKKCRKFL N
//
