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Database: UniProt
Entry: U3IB34_ANAPP
LinkDB: U3IB34_ANAPP
Original site: U3IB34_ANAPP 
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
     LN
//
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