ID DNMT1_BOVIN Reviewed; 1611 AA. AC Q24K09; Q6Y856; Q7YS60; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 08-NOV-2023, entry version 133. DE RecName: Full=DNA (cytosine-5)-methyltransferase 1; DE Short=Dnmt1; DE EC=2.1.1.37; GN Name=DNMT1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12971987; DOI=10.1016/s1567-133x(03)00121-2; RA Golding M.C., Westhusin M.E.; RT "Analysis of DNA (cytosine 5) methyltransferase mRNA sequence and RT expression in bovine preimplantation embryos, fetal and adult tissues."; RL Gene Expr. Patterns 3:551-558(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Lee P., Min K.S., Seong H.H., Park J.K., Lee Y.K., Kim S.W., Kim S.J., RA Lee H.G., Chung H.K., Chang Y.M., Chang W.K., Kwon M.; RT "Bovine (Bos taurus) cytosine-5-methyltransferase (Dnmt1) cDNA."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Hypothalamus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Methylates CpG residues. Preferentially methylates CC hemimethylated DNA. Associates with DNA replication sites in S phase CC maintaining the methylation pattern in the newly synthesized strand, CC that is essential for epigenetic inheritance. Associates with chromatin CC during G2 and M phases to maintain DNA methylation independently of CC replication. It is responsible for maintaining methylation patterns CC established in development. DNA methylation is coordinated with CC methylation of histones. Mediates transcriptional repression by direct CC binding to HDAC2. In association with DNMT3B and via the recruitment of CC CTCFL/BORIS, involved in activation of BAG1 gene expression by CC modulating dimethylation of promoter histone H3 at H3K4 and H3K9. CC Probably forms a corepressor complex required for activated KRAS- CC mediated promoter hypermethylation and transcriptional silencing of CC tumor suppressor genes (TSGs) or other tumor-related genes in CC colorectal cancer (CRC) cells. Also required to maintain a CC transcriptionally repressive state of genes in undifferentiated CC embryonic stem cells (ESCs). Associates at promoter regions of tumor CC suppressor genes (TSGs) leading to their gene silencing. Promotes tumor CC growth. {ECO:0000250|UniProtKB:P13864, ECO:0000250|UniProtKB:P26358}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5- CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10018}; CC -!- SUBUNIT: Homodimer. Forms a stable complex with E2F1, BB1 and HDAC1. CC Forms a complex with DMAP1 and HDAC2, with direct interaction. CC Interacts with the PRC2/EED-EZH2 complex. Probably part of a CC corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1. CC Interacts with UHRF1; promoting its recruitment to hemimethylated DNA. CC Interacts with USP7, promoting its deubiquitination. Interacts with CC PCNA. Interacts with MBD2 and MBD3. Interacts with DNMT3A and DNMT3B. CC Interacts with UBC9 (By similarity). Interacts with CSNK1D (By CC similarity). Interacts with HDAC1 (By similarity). Interacts with CC BAZ2A/TIP5 (By similarity). Interacts with SIRT7 (By similarity). CC Interacts with ZNF263; recruited to the SIX3 promoter along with other CC proteins involved in chromatin modification and transcriptional CC corepression where it contributes to transcriptional repression (By CC similarity). Interacts with L3MBTL3 and DCAF5; the interaction requires CC DNMT1 methylation at Lys-142 and is necessary to target DNMT1 for CC ubiquitination by the CRL4-DCAF5 E3 ubiquitin ligase complex and CC proteasomal degradation (By similarity). Interacts with PHF20L1; the CC interaction requires DNMT1 methylation at Lys-142 and protects DNMT1 CC from ubiquitination and proteasomal degradation (By similarity). CC {ECO:0000250|UniProtKB:P13864, ECO:0000250|UniProtKB:P26358}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- DOMAIN: The N-terminal part is required for homodimerization and acts CC as a regulatory domain. CC -!- DOMAIN: The CXXC-type zinc finger specifically binds to unmethylated CC CpG dinucleotides, positioning the autoinhibitory linker between the CC DNA and the active site, thus providing a mechanism to ensure that only CC hemimethylated CpG dinucleotides undergo methylation. CC {ECO:0000250|UniProtKB:P26358}. CC -!- PTM: Sumoylated; sumoylation increases activity. CC {ECO:0000250|UniProtKB:P26358}. CC -!- PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates CC cell cycle G(2)/M transition. Deacetylation of Lys-1346 and Lys-1412 by CC SIRT1 increases methyltransferase activity. CC {ECO:0000250|UniProtKB:P26358}. CC -!- PTM: Phosphorylation of Ser-154 by CDKs is important for enzymatic CC activity and protein stability. Phosphorylation of Ser-143 by AKT1 CC prevents methylation by SETD7 therebye increasing DNMT1 stability. CC {ECO:0000250|UniProtKB:P26358}. CC -!- PTM: Methylation at Lys-142 by SETD7 is necessary for the regulation of CC DNMT1 proteasomal degradation. {ECO:0000250|UniProtKB:P26358}. CC -!- PTM: Ubiquitinated by UHRF1; interaction with USP7 counteracts CC ubiquitination by UHRF1 by promoting deubiquitination and preventing CC degradation by the proteasome. {ECO:0000250|UniProtKB:P13864}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE- CC ProRule:PRU01016}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY244709; AAP20551.1; -; mRNA. DR EMBL; AY173048; AAO44952.1; -; mRNA. DR EMBL; BC114063; AAI14064.1; -; mRNA. DR RefSeq; NP_872592.2; NM_182651.2. DR PDB; 6PZV; X-ray; 3.01 A; C/G=349-594. DR PDB; 7LMK; X-ray; 2.65 A; A/B/C/D=725-837, A/B/C/D=859-897. DR PDB; 7LMM; X-ray; 2.80 A; A/B/C/D=725-837, A/B/C/D=859-897. DR PDBsum; 6PZV; -. DR PDBsum; 7LMK; -. DR PDBsum; 7LMM; -. DR AlphaFoldDB; Q24K09; -. DR SMR; Q24K09; -. DR BioGRID; 158481; 1. DR STRING; 9913.ENSBTAP00000003549; -. DR REBASE; 7406; M.BtaDnmt1AP. DR PaxDb; 9913-ENSBTAP00000003549; -. DR GeneID; 281119; -. DR KEGG; bta:281119; -. DR CTD; 1786; -. DR eggNOG; ENOG502QPKK; Eukaryota. DR HOGENOM; CLU_003040_0_0_1; -. DR InParanoid; Q24K09; -. DR TreeFam; TF328926; -. DR BRENDA; 2.1.1.37; 908. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IBA:GO_Central. DR GO; GO:0044027; P:negative regulation of gene expression via CpG island methylation; ISS:UniProtKB. DR CDD; cd04760; BAH_Dnmt1_I; 1. DR CDD; cd04711; BAH_Dnmt1_II; 1. DR Gene3D; 1.10.10.2230; -; 1. DR Gene3D; 2.30.30.490; -; 2. DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR001025; BAH_dom. DR InterPro; IPR043151; BAH_sf. DR InterPro; IPR018117; C5_DNA_meth_AS. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR031303; C5_meth_CS. DR InterPro; IPR022702; Cytosine_MeTrfase1_RFD. DR InterPro; IPR010506; DMAP1-bd. DR InterPro; IPR017198; DNMT1-like. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR002857; Znf_CXXC. DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1. DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1. DR Pfam; PF01426; BAH; 2. DR Pfam; PF06464; DMAP_binding; 1. DR Pfam; PF00145; DNA_methylase; 1. DR Pfam; PF12047; DNMT1-RFD; 1. DR Pfam; PF02008; zf-CXXC; 1. DR PIRSF; PIRSF037404; DNMT1; 1. DR PRINTS; PR00105; C5METTRFRASE. DR SMART; SM00439; BAH; 2. DR SMART; SM01137; DMAP_binding; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51038; BAH; 2. DR PROSITE; PS00094; C5_MTASE_1; 1. DR PROSITE; PS00095; C5_MTASE_2; 1. DR PROSITE; PS51912; DMAP1_BIND; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. DR PROSITE; PS51058; ZF_CXXC; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Chromatin regulator; DNA-binding; KW Isopeptide bond; Metal-binding; Methylation; Methyltransferase; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Repressor; KW S-adenosyl-L-methionine; Transcription; Transcription regulation; KW Transferase; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..1611 FT /note="DNA (cytosine-5)-methyltransferase 1" FT /id="PRO_0000239845" FT DOMAIN 16..109 FT /note="DMAP1-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260" FT DOMAIN 752..877 FT /note="BAH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT DOMAIN 969..1097 FT /note="BAH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT REPEAT 1106..1107 FT /note="1" FT REPEAT 1108..1109 FT /note="2" FT REPEAT 1110..1111 FT /note="3" FT REPEAT 1112..1113 FT /note="4" FT REPEAT 1114..1115 FT /note="5; approximate" FT DOMAIN 1136..1595 FT /note="SAM-dependent MTase C5-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016" FT ZN_FING 643..689 FT /note="CXXC-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT REGION 1..334 FT /note="Interaction with the PRC2/EED-EZH2 complex" FT /evidence="ECO:0000250" FT REGION 1..148 FT /note="Interaction with DNMT3A" FT /evidence="ECO:0000250" FT REGION 1..120 FT /note="Interaction with DMAP1" FT /evidence="ECO:0000250" FT REGION 123..328 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 149..216 FT /note="Interaction with DNMT3B" FT /evidence="ECO:0000250" FT REGION 163..174 FT /note="Interaction with PCNA" FT /evidence="ECO:0000250" FT REGION 306..603 FT /note="Interaction with the PRC2/EED-EZH2 complex" FT /evidence="ECO:0000250" FT REGION 329..548 FT /note="DNA replication foci-targeting sequence" FT /evidence="ECO:0000250" FT REGION 594..614 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 690..751 FT /note="Autoinhibitory linker" FT REGION 695..726 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1091..1126 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1106..1115 FT /note="5 X 2 AA tandem repeats of K-G" FT REGION 1118..1611 FT /note="Interaction with the PRC2/EED-EZH2 complex" FT /evidence="ECO:0000250" FT REGION 1136..1611 FT /note="Catalytic" FT /evidence="ECO:0000250" FT MOTIF 177..204 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 150..171 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 174..210 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 224..328 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1223 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016, FT ECO:0000255|PROSITE-ProRule:PRU10018" FT BINDING 351 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 354 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 412 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 416 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 650 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 653 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 656 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 661 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 664 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 667 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 683 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 688 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509" FT BINDING 1143 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P13864" FT BINDING 1147..1148 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P13864" FT BINDING 1165..1166 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P26358" FT BINDING 1187..1188 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P13864" FT BINDING 1188 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P26358" FT BINDING 1574 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P26358" FT BINDING 1576 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P13864" FT SITE 507 FT /note="Important for activity" FT /evidence="ECO:0000250" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P13864" FT MOD_RES 70 FT /note="N6,N6-dimethyllysine; by EHMT2" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 133 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 137 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 141 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P13864" FT MOD_RES 142 FT /note="N6-methyllysine; by SETD7" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 143 FT /note="Phosphoserine; by PKB/AKT1" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 154 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 160 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 166 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 188 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 257 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 310 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 392 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 396 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 507 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P13864" FT MOD_RES 547 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 711 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 729 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 746 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 875 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 888 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 954 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 958 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 972 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 1051 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 1108 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 1110 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 1112 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 1114 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 1118 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13864" FT MOD_RES 1346 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT MOD_RES 1412 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26358" FT CROSSLNK 257 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P26358" FT CROSSLNK 1605 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P26358" FT CONFLICT 655 FT /note="I -> V (in Ref. 2; AAO44952)" FT /evidence="ECO:0000305" FT CONFLICT 716 FT /note="H -> R (in Ref. 2; AAO44952)" FT /evidence="ECO:0000305" FT CONFLICT 777 FT /note="T -> A (in Ref. 2; AAO44952)" FT /evidence="ECO:0000305" FT CONFLICT 1176 FT /note="L -> F (in Ref. 1; AAP20551)" FT /evidence="ECO:0000305" FT CONFLICT 1186 FT /note="E -> K (in Ref. 1; AAP20551)" FT /evidence="ECO:0000305" FT CONFLICT 1192 FT /note="L -> V (in Ref. 1; AAP20551)" FT /evidence="ECO:0000305" FT CONFLICT 1209 FT /note="P -> L (in Ref. 1; AAP20551)" FT /evidence="ECO:0000305" FT CONFLICT 1287 FT /note="M -> R (in Ref. 1; AAP20551)" FT /evidence="ECO:0000305" FT CONFLICT 1387 FT /note="G -> R (in Ref. 1; AAP20551)" FT /evidence="ECO:0000305" FT CONFLICT 1405 FT /note="I -> T (in Ref. 2; AAO44952)" FT /evidence="ECO:0000305" FT CONFLICT 1466 FT /note="S -> T (in Ref. 2; AAO44952)" FT /evidence="ECO:0000305" FT TURN 352..354 FT /evidence="ECO:0007829|PDB:6PZV" FT STRAND 357..359 FT /evidence="ECO:0007829|PDB:6PZV" FT HELIX 375..378 FT /evidence="ECO:0007829|PDB:6PZV" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:6PZV" FT STRAND 402..411 FT /evidence="ECO:0007829|PDB:6PZV" FT STRAND 415..417 FT /evidence="ECO:0007829|PDB:6PZV" FT STRAND 420..423 FT /evidence="ECO:0007829|PDB:6PZV" FT TURN 424..428 FT /evidence="ECO:0007829|PDB:6PZV" FT STRAND 432..438 FT /evidence="ECO:0007829|PDB:6PZV" FT STRAND 450..456 FT /evidence="ECO:0007829|PDB:6PZV" FT STRAND 460..465 FT /evidence="ECO:0007829|PDB:6PZV" FT STRAND 474..478 FT /evidence="ECO:0007829|PDB:6PZV" FT STRAND 483..486 FT /evidence="ECO:0007829|PDB:6PZV" FT TURN 491..493 FT /evidence="ECO:0007829|PDB:6PZV" FT HELIX 494..516 FT /evidence="ECO:0007829|PDB:6PZV" FT HELIX 522..531 FT /evidence="ECO:0007829|PDB:6PZV" FT HELIX 536..538 FT /evidence="ECO:0007829|PDB:6PZV" FT HELIX 545..549 FT /evidence="ECO:0007829|PDB:6PZV" FT HELIX 552..564 FT /evidence="ECO:0007829|PDB:6PZV" FT HELIX 577..586 FT /evidence="ECO:0007829|PDB:6PZV" FT STRAND 728..733 FT /evidence="ECO:0007829|PDB:7LMK" FT STRAND 735..737 FT /evidence="ECO:0007829|PDB:7LMK" FT STRAND 739..749 FT /evidence="ECO:0007829|PDB:7LMK" FT STRAND 752..755 FT /evidence="ECO:0007829|PDB:7LMK" FT STRAND 759..762 FT /evidence="ECO:0007829|PDB:7LMK" FT STRAND 772..782 FT /evidence="ECO:0007829|PDB:7LMK" FT TURN 783..785 FT /evidence="ECO:0007829|PDB:7LMK" FT STRAND 786..795 FT /evidence="ECO:0007829|PDB:7LMK" FT HELIX 797..799 FT /evidence="ECO:0007829|PDB:7LMK" FT STRAND 812..821 FT /evidence="ECO:0007829|PDB:7LMK" FT HELIX 822..824 FT /evidence="ECO:0007829|PDB:7LMK" FT STRAND 825..829 FT /evidence="ECO:0007829|PDB:7LMK" FT STRAND 865..867 FT /evidence="ECO:0007829|PDB:7LMK" FT TURN 868..871 FT /evidence="ECO:0007829|PDB:7LMK" FT STRAND 872..875 FT /evidence="ECO:0007829|PDB:7LMK" FT TURN 883..885 FT /evidence="ECO:0007829|PDB:7LMK" FT HELIX 886..888 FT /evidence="ECO:0007829|PDB:7LMK" FT HELIX 891..896 FT /evidence="ECO:0007829|PDB:7LMK" SQ SEQUENCE 1611 AA; 182842 MW; A7F0D9B24A18771C CRC64; MPARTAPARV PALASRAFSL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLRTEIKNQ LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGAHAFS REANGCLENG SQTSGEDCRV VMAEKGKPPK PVSRLYTPRR SKSDGETKSE VSSSPRITRK TTRQTTITSH FPRGPAKRKP EEEPEKVKSD DSVDEEKDQE EKRRRVTSRE RVAGLLPAEE PGRVRPGTHM EEEGRDDKEE KRLRSQTKEP TPKHKAKEEP DRDVRPGGAQ AEMNEGEDKD EKRHRSQPKD LASKRRPEEK EPERVKPQVS DEKDEDEKEE KRRRTTYREL TEKKMTRTKI AVVSKTNPPK CTECLQYLDD PELRYEQHPP DAVEEIQILT NERLSIFDAN ESGFESYEDL PQHKLTCFSV YCKRGHLCPI DTGLIEKDVE LLFSGSAKPI YEDDPSPEGG INGKNFGPIN EWWIAGFDGG EKALLGFSTS FAEYILMDPS PEYAPLFSVM QEKIYISKIV VEFLQSNPDS TYEDLINKIE TTVPPCMLNL NRFTEDSLLR HAQFVVEQVE SYDRAGDSDE QPIFLSPCMR DLIKLAGVTL GKRRAERRQT IRQPAKEKDK GPTKATTTKL VYQIFDTFFA EQIEKDDKED KENAFKRRRC GVCEICQQPE CGKCKACKDM VKFGGSGRSK QACQKRRCPN MAMKEADDDE EVDDNIPEMP SPKKMHQGKK KKQNKNRISW VGDAVKTDGK KSYYKKVCID SETLEVGDCV SVIPDDSSKP LYLARVTALW EDSSNGQMFH AHWFCAGTDT VLGATSDPLE LFLVDECEDM QLSYIHSKVQ VIYKAPSENW AMEGGVDPEA LMSEDDGKTY FYQLWYDQDY ARFESPPKTQ PTEDNKYKFC ASCARLAEMR QKEIPRVVEQ LQDLEGRVLY SLATKNGVQY RVGDGVYLPP EAFTFNIKLS SPVKRPRKEP VDEALYPEHY RKYSDYIKGS NLDAPEPYRI GRIKEIFCSK KSNGRPNETD IKIRVNKFYR PENTHKSTPA SYHADINLLY WSDEEAVVDF KAVQGRCTVE YGEDLPQCLQ DFSAGGPDRF YFLEAYNAKS KSFEDPPNHA RSTGNKGKGK GKGKNRTKSQ TCEPSELETE IKLPKLRTLD VFSGCGGLSE GFHQAGISET LWAIEMWDPA AQAFRLNNPG STVFTEDCNV LLKLVMAGEV TNSRGQKLPQ KGDVEMLCGG PPCQGFSGMN RFNSRTYSKF KNSLVVSFLS YCDYYRPRYF LLENVRNFVS FKRSMVLKLT LRCLVRMGYQ CTFGVLQAGQ YGVAQTRRRA IILAAAPGEP LPLFPEPLHV FAPRACQLSV VVDDKKFVSN ITRLSSGPFR TITVRDTMSD LPEIRNGASA LEISYNGEPQ SWFQRQLRGS QYQPILRDHI CKDMSALVAA RMRHIPLAPG SDWRDLPNIE VRLSDGTLAR KLRYNYHDKK NGCSSSGALR GVCSCVEGKP CEPAARQFNT LIPWCLPHTG NRHNHWAGLY GRLEWDGFFS TTVTNPEPMG KQGRVLHPEQ HRVVSVRECA RSQGFPDTYR LFGNILDKHR QVGNAVPPPL AKAIGLEIKR CMLAKARESA SAKIKEEAAK D //