PRDM9_RAT
ID PRDM9_RAT Reviewed; 796 AA.
AC P0C6Y7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Histone-lysine N-methyltransferase PRDM9 {ECO:0000305};
DE AltName: Full=PR domain zinc finger protein 9;
DE AltName: Full=PR domain-containing protein 9;
DE AltName: Full=Protein-lysine N-methyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q96EQ9};
DE AltName: Full=[histone H3]-lysine36 N-trimethyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.359 {ECO:0000250|UniProtKB:Q96EQ9};
DE AltName: Full=[histone H3]-lysine4 N-trimethyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q96EQ9};
DE AltName: Full=[histone H3]-lysine9 N-trimethyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.355 {ECO:0000250|UniProtKB:Q96EQ9};
DE AltName: Full=[histone H4]-N-methyl-L-lysine20 N-methyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.362 {ECO:0000250|UniProtKB:Q96EQ9};
DE AltName: Full=[histone H4]-lysine20 N-methyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.361 {ECO:0000250|UniProtKB:Q96EQ9};
GN Name=Prdm9 {ECO:0000312|RGD:1305247};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone methyltransferase that sequentially mono-, di-, and
CC tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3
CC to produce respectively trimethylated 'Lys-4' (H3K4me3) and
CC trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in
CC meiotic prophase by determining hotspot localization thereby promoting
CC meiotic recombination. Can also methylate all four core histones with
CC H3 being the best substrate and the most highly modified. Is also able,
CC on one hand, to mono and di-methylate H4K20 and on other hand to
CC trimethylate H3K9 with the di-methylated H3K9 as the best substrate.
CC During meiotic prophase, binds specific DNA sequences through its zinc
CC finger domains thereby determining hotspot localization where it
CC promotes local H3K4me3 and H3K36me3 enrichment on the same nucleosomes
CC through its histone methyltransferase activity. Thereby promotes
CC double-stranded breaks (DSB) formation, at this subset of PRDM9-binding
CC sites, that initiates meiotic recombination for the proper meiotic
CC progression. During meiotic progression hotspot-bound PRDM9 interacts
CC with several complexes; in early leptonema binds CDYL and EHMT2
CC followed by EWSR1 and CXXC1 by the end of leptonema. EWSR1 joins PRDM9
CC with the chromosomal axis through REC8. In this way, controls the DSB
CC repair pathway, pairing of homologous chromosomes and sex body
CC formation. Moreover plays a central role in the transcriptional
CC activation of genes during early meiotic prophase thanks to H3K4me3 and
CC H3K36me3 enrichment that represents a specific tag for epigenetic
CC transcriptional activation. In addition performs automethylation.
CC Acetylation and phosphorylation of histone H3 attenuate or prevent
CC histone H3 methylation. {ECO:0000250|UniProtKB:Q96EQ9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+)
CC + N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54196, Rhea:RHEA-COMP:13053, Rhea:RHEA-COMP:13827,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54197;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000250|UniProtKB:Q9NQV7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60261;
CC Evidence={ECO:0000250|UniProtKB:Q9NQV7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC Evidence={ECO:0000250|UniProtKB:Q9NQV7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60325;
CC Evidence={ECO:0000250|UniProtKB:Q9NQV7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60277;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60345;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-
CC COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; EC=2.1.1.362;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC -!- SUBUNIT: Homodimer. Interacts with EHMT2 and CDYL; interaction only
CC takes place when PRDM9 is bound to hotspot DNA. Interacts with CXXC1;
CC this interaction does not link PRDM9-activated recombination hotspot
CC sites with DSB machinery and is not required for the hotspot
CC recognition pathway. Forms a complex with EWSR1, REC8, SYCP3 and SYCP1;
CC complex formation is dependent of phosphorylated form of REC8 and
CC requires PRDM9 bound to hotspot DNA; EWSR1 joins PRDM9 with the
CC chromosomal axis through REC8. {ECO:0000250|UniProtKB:Q96EQ9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96EQ9}.
CC Chromosome {ECO:0000250|UniProtKB:Q96EQ9}. Note=Localizes in nuclei of
CC pre-leptotene, leptotene, and early to mid-zygotene spermatocytes.
CC {ECO:0000250|UniProtKB:Q96EQ9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0C6Y7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0C6Y7-2; Sequence=VSP_036379, VSP_036380, VSP_036381;
CC -!- DOMAIN: The C2H2-type zinc fingers determine the hotspot localization
CC through its binding to specific DNA sequences. Variations in their
CC sequence affect affinity towards DNA-binding motif.
CC {ECO:0000250|UniProtKB:Q96EQ9}.
CC -!- PTM: Mono-methylated; automethylated. Tri-methylated; automethylated.
CC Mono-methylation is predominant; automethylation is lower and slower
CC than H3 peptide methylation and is in a highest S-adenosyl-L-methionine
CC concentration-dependent. There are two major sites for automethylation
CC at Lys-372 and Lys-378. Lysines can be simultaneously methylated, such
CC as Lys-372(me3)/Lys-376(me1), Lys-372(me1)/Lys-378(me1) and Lys-
CC 372(me1)/Lys-376(me1)/Lys-378(me1). Automethylation is an
CC intramolecular (cis) process. {ECO:0000250|UniProtKB:Q96EQ9}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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; CH474033; EDL99813.1; -; Genomic_DNA.
DR RefSeq; NP_001102373.2; NM_001108903.2. [P0C6Y7-1]
DR AlphaFoldDB; P0C6Y7; -.
DR SMR; P0C6Y7; -.
DR STRING; 10116.ENSRNOP00000060531; -.
DR PaxDb; P0C6Y7; -.
DR Ensembl; ENSRNOT00000066370; ENSRNOP00000060531; ENSRNOG00000021493. [P0C6Y7-1]
DR GeneID; 365155; -.
DR KEGG; rno:365155; -.
DR UCSC; RGD:1305247; rat. [P0C6Y7-1]
DR CTD; 56979; -.
DR RGD; 1305247; Prdm9.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG2461; Eukaryota.
DR GeneTree; ENSGT00940000158211; -.
DR HOGENOM; CLU_002678_32_0_1; -.
DR InParanoid; P0C6Y7; -.
DR OMA; RSCNDKT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P0C6Y7; -.
DR TreeFam; TF338096; -.
DR Reactome; R-RNO-3214841; PKMTs methylate histone lysines.
DR PRO; PR:P0C6Y7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000021493; Expressed in liver and 19 other tissues.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISS:UniProtKB.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0010844; F:recombination hotspot binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; ISS:UniProtKB.
DR GO; GO:0007292; P:female gamete generation; ISS:UniProtKB.
DR GO; GO:0097676; P:histone H3-K36 dimethylation; ISS:UniProtKB.
DR GO; GO:0097198; P:histone H3-K36 trimethylation; ISS:UniProtKB.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; ISS:UniProtKB.
DR GO; GO:0051568; P:histone H3-K4 methylation; ISS:UniProtKB.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; ISS:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB.
DR GO; GO:0051567; P:histone H3-K9 methylation; ISS:UniProtKB.
DR GO; GO:0034968; P:histone lysine methylation; ISS:UniProtKB.
DR GO; GO:0016571; P:histone methylation; ISO:RGD.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISS:UniProtKB.
DR GO; GO:0048232; P:male gamete generation; ISS:UniProtKB.
DR GO; GO:0006311; P:meiotic gene conversion; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1905516; P:positive regulation of fertilization; ISS:UniProtKB.
DR GO; GO:2001255; P:positive regulation of histone H3-K36 trimethylation; ISS:UniProtKB.
DR GO; GO:1905437; P:positive regulation of histone H3-K4 trimethylation; ISS:UniProtKB.
DR GO; GO:0060903; P:positive regulation of meiosis I; ISO:RGD.
DR GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd19193; PR-SET_PRDM7_9; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR003655; aKRAB.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR044417; PRDM7_9_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019041; SSXRD_motif.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF09514; SSXRD; 1.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50806; KRAB_RELATED; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 3: Inferred from homology;
KW Activator; Alternative splicing; Chromatin regulator; Chromosome;
KW DNA-binding; Meiosis; Metal-binding; Methylation; Methyltransferase;
KW Nucleus; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..796
FT /note="Histone-lysine N-methyltransferase PRDM9"
FT /id="PRO_0000363961"
FT DOMAIN 27..90
FT /note="KRAB-related"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00120"
FT DOMAIN 248..362
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 392..415
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 522..540
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 546..568
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 574..596
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 602..624
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 630..652
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 658..680
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 686..708
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 714..736
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 742..764
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 770..792
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 260..262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 292..298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 295
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 324..325
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 716
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 719
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 732
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 736
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 744
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 747
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 760
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 764
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 772
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 775
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 788
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 792
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT MOD_RES 372
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT MOD_RES 372
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT MOD_RES 376
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT MOD_RES 378
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036379"
FT VAR_SEQ 386..408
FT /note="ELRTEIHPCFLCSLAFSSQKFLT -> GGYHYDSLKEKEKMDFSLRIFIF
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036380"
FT VAR_SEQ 409..796
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036381"
SQ SEQUENCE 796 AA; 92579 MW; 7FB5104B805F87D9 CRC64;
MSRTMNTNKP EENSTEGDAG KLEWKPKVKD EFKDISIYFS KEEWAEMGEW EKIRYRNVKR
NYKMLISIGL RAPRPAFMCY QRQAIKPQIN DNEDSDEEWT PKQQVSSPWV PFRVKHSKQQ
KETPRMPLSD KSSVKEVFGI ENLLNTSGSE HAQKPVCSPE EGNTSGQHFG KKLKLRRKNV
EVNRYRLRER KDLAYEEVSE PQDDDYLYCE KCQNFFIDSC PNHGPPVFVK DSVVDRGHPN
HSVLSLPPGL RIGPSGIPEA GLGVWNEASD LPVGLHFGPY KGQITEDEEA ANSGYSWLIT
KGRNCYEYVD GQDESQANWM RYVNCARDDE EQNLVAFQYH RKIFYRTCRV IRPGRELLVW
YGDEYGQELG IKWGSKMKKG FTAGRELRTE IHPCFLCSLA FSSQKFLTQH VEWNHRTEIF
PGASARINPK PGDPCPDQLQ EHFDSQNKND KASNEVKRKS KPRHKWTRQR ISTAFSSTLK
EQMRSEESKR TVEEELRTGQ TTNIEDTAKS FIASETSRIE RQCGQCFSDK SNVSEHQRTH
TGEKPYICRE CGRGFSQKSD LIKHQRTHTE EKPYICRECG RGFTQKSDLI KHQRTHTEEK
PYICRECGRG FTQKSDLIKH QRTHTGEKPY ICRECGRGFT QKSDLIKHQR THTEEKPYIC
RECGRGFTQK SSLIRHQRTH TGEKPYICRE CGLGFTQKSN LIRHLRTHTG EKPYICRECG
LGFTRKSNLI QHQRTHTGEK PYICRECGQG LTWKSSLIQH QRTHTGEKPY ICRECGRGFT
WKSSLIQHQR THTVEK
