SETD6_HUMAN
ID SETD6_HUMAN Reviewed; 473 AA.
AC Q8TBK2; A8K380; B5ME38; Q9H787;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=N-lysine methyltransferase SETD6;
DE EC=2.1.1.- {ECO:0000269|PubMed:21131967, ECO:0000269|PubMed:21515635, ECO:0000269|PubMed:23324626, ECO:0000269|PubMed:30189201};
DE AltName: Full=SET domain-containing protein 6;
GN Name=SETD6 {ECO:0000303|PubMed:21515635, ECO:0000312|HGNC:HGNC:26116};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-185
RP AND GLY-206.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP TYR-285.
RX PubMed=21131967; DOI=10.1038/ni.1968;
RA Levy D., Kuo A.J., Chang Y., Schaefer U., Kitson C., Cheung P., Espejo A.,
RA Zee B.M., Liu C.L., Tangsombatvisit S., Tennen R.I., Kuo A.Y., Tanjing S.,
RA Cheung R., Chua K.F., Utz P.J., Shi X., Prinjha R.K., Lee K., Garcia B.A.,
RA Bedford M.T., Tarakhovsky A., Cheng X., Gozani O.;
RT "Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity
RT of the histone methyltransferase GLP at chromatin to tonic repression of
RT NF-kappaB signaling.";
RL Nat. Immunol. 12:29-36(2011).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23324626; DOI=10.4161/epi.23416;
RA Binda O., Sevilla A., LeRoy G., Lemischka I.R., Garcia B.A., Richard S.;
RT "SETD6 monomethylates H2AZ on lysine 7 and is required for the maintenance
RT of embryonic stem cell self-renewal.";
RL Epigenetics 8:177-183(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, METHYLATION AT
RP LYS-39; LYS-179 AND LYS-372, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP MUTAGENESIS OF LYS-39; LYS-179; TYR-285 AND LYS-372.
RX PubMed=30189201; DOI=10.1016/j.jmb.2018.08.028;
RA Weil L.E., Shmidov Y., Kublanovsky M., Morgenstern D., Feldman M.,
RA Bitton R., Levy D.;
RT "Oligomerization and Auto-methylation of the Human Lysine Methyltransferase
RT SETD6.";
RL J. Mol. Biol. 430:4359-4368(2018).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASN-283.
RX PubMed=21515635; DOI=10.1093/nar/gkr256;
RA Chang Y., Levy D., Horton J.R., Peng J., Zhang X., Gozani O., Cheng X.;
RT "Structural basis of SETD6-mediated regulation of the NF-kB network via
RT methyl-lysine signaling.";
RL Nucleic Acids Res. 39:6380-6389(2011).
CC -!- FUNCTION: Protein-lysine N-methyltransferase. Monomethylates 'Lys-310'
CC of the RELA subunit of NF-kappa-B complex, leading to down-regulation
CC of NF-kappa-B transcription factor activity (PubMed:21131967,
CC PubMed:30189201, PubMed:21515635). Monomethylates 'Lys-8' of H2AZ
CC (H2AZK8me1) (PubMed:23324626). Required for the maintenance of
CC embryonic stem cell self-renewal (By similarity). Methylates PAK4.
CC {ECO:0000250|UniProtKB:Q9CWY3, ECO:0000269|PubMed:21131967,
CC ECO:0000269|PubMed:21515635, ECO:0000269|PubMed:23324626,
CC ECO:0000269|PubMed:30189201}.
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:0000269|PubMed:21131967, ECO:0000269|PubMed:21515635,
CC ECO:0000269|PubMed:23324626, ECO:0000269|PubMed:30189201};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737;
CC Evidence={ECO:0000305|PubMed:21131967, ECO:0000305|PubMed:21515635,
CC ECO:0000305|PubMed:23324626, ECO:0000305|PubMed:30189201};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(8)-[histone H2AZ] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(8)-[histone H2AZ] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:67808, Rhea:RHEA-COMP:17357, Rhea:RHEA-COMP:17358,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000269|PubMed:23324626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67809;
CC Evidence={ECO:0000305|PubMed:23324626};
CC -!- ACTIVITY REGULATION: Activated by automethylation.
CC {ECO:0000269|PubMed:30189201}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 10. {ECO:0000269|PubMed:21515635};
CC -!- SUBUNIT: Monomer, homodimer and homotrimer; these structures are
CC stabilized in the presence of S-adenosyl-L-methionine (SAM).
CC {ECO:0000269|PubMed:30189201}.
CC -!- INTERACTION:
CC Q8TBK2; Q04207: Rela; Xeno; NbExp=4; IntAct=EBI-3863032, EBI-644400;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21131967}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TBK2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TBK2-2; Sequence=VSP_024093;
CC -!- PTM: Automethylated; Lys-39 and Lys-179 serve as the major
CC automethylation sites. {ECO:0000269|PubMed:30189201}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SETD6 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AK024801; BAB15011.1; -; mRNA.
DR EMBL; AK290495; BAF83184.1; -; mRNA.
DR EMBL; AC009118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022451; AAH22451.1; -; mRNA.
DR CCDS; CCDS10798.1; -. [Q8TBK2-2]
DR CCDS; CCDS54013.1; -. [Q8TBK2-1]
DR RefSeq; NP_001153777.1; NM_001160305.2. [Q8TBK2-1]
DR RefSeq; NP_079136.2; NM_024860.3. [Q8TBK2-2]
DR PDB; 3QXY; X-ray; 2.09 A; A/B=1-473.
DR PDB; 3RC0; X-ray; 2.19 A; A/B=1-473.
DR PDBsum; 3QXY; -.
DR PDBsum; 3RC0; -.
DR AlphaFoldDB; Q8TBK2; -.
DR SMR; Q8TBK2; -.
DR BioGRID; 122996; 58.
DR IntAct; Q8TBK2; 6.
DR MINT; Q8TBK2; -.
DR STRING; 9606.ENSP00000219315; -.
DR BindingDB; Q8TBK2; -.
DR iPTMnet; Q8TBK2; -.
DR PhosphoSitePlus; Q8TBK2; -.
DR BioMuta; SETD6; -.
DR DMDM; 308153495; -.
DR EPD; Q8TBK2; -.
DR jPOST; Q8TBK2; -.
DR MassIVE; Q8TBK2; -.
DR MaxQB; Q8TBK2; -.
DR PaxDb; Q8TBK2; -.
DR PeptideAtlas; Q8TBK2; -.
DR PRIDE; Q8TBK2; -.
DR ProteomicsDB; 74022; -. [Q8TBK2-1]
DR ProteomicsDB; 74023; -. [Q8TBK2-2]
DR Antibodypedia; 48742; 145 antibodies from 26 providers.
DR DNASU; 79918; -.
DR Ensembl; ENST00000219315.9; ENSP00000219315.5; ENSG00000103037.12. [Q8TBK2-1]
DR Ensembl; ENST00000310682.6; ENSP00000310082.2; ENSG00000103037.12. [Q8TBK2-2]
DR GeneID; 79918; -.
DR KEGG; hsa:79918; -.
DR MANE-Select; ENST00000219315.9; ENSP00000219315.5; NM_001160305.4; NP_001153777.1.
DR UCSC; uc002enr.4; human. [Q8TBK2-1]
DR CTD; 79918; -.
DR DisGeNET; 79918; -.
DR GeneCards; SETD6; -.
DR HGNC; HGNC:26116; SETD6.
DR HPA; ENSG00000103037; Low tissue specificity.
DR MIM; 616424; gene.
DR neXtProt; NX_Q8TBK2; -.
DR OpenTargets; ENSG00000103037; -.
DR PharmGKB; PA143485614; -.
DR VEuPathDB; HostDB:ENSG00000103037; -.
DR eggNOG; KOG1338; Eukaryota.
DR GeneTree; ENSGT00940000153577; -.
DR HOGENOM; CLU_017135_2_0_1; -.
DR InParanoid; Q8TBK2; -.
DR OMA; EYSADYL; -.
DR OrthoDB; 490654at2759; -.
DR PhylomeDB; Q8TBK2; -.
DR TreeFam; TF106399; -.
DR PathwayCommons; Q8TBK2; -.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR SignaLink; Q8TBK2; -.
DR BioGRID-ORCS; 79918; 15 hits in 1091 CRISPR screens.
DR ChiTaRS; SETD6; human.
DR GenomeRNAi; 79918; -.
DR Pharos; Q8TBK2; Tbio.
DR PRO; PR:Q8TBK2; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8TBK2; protein.
DR Bgee; ENSG00000103037; Expressed in secondary oocyte and 190 other tissues.
DR ExpressionAtlas; Q8TBK2; baseline and differential.
DR Genevisible; Q8TBK2; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR GO; GO:0034968; P:histone lysine methylation; IDA:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IDA:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
DR CDD; cd19178; SET_SETD6; 1.
DR Gene3D; 3.90.1420.10; -; 1.
DR InterPro; IPR011383; N-lys_methylase_SETD6.
DR InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044430; SETD6_SET.
DR Pfam; PF09273; Rubis-subs-bind; 1.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF011771; RMS1_SET; 1.
DR SUPFAM; SSF81822; SSF81822; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Methylation; Methyltransferase;
KW Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..473
FT /note="N-lysine methyltransferase SETD6"
FT /id="PRO_0000281889"
FT DOMAIN 60..286
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 73..75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21515635"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21515635"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21515635"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21515635"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21515635"
FT BINDING 251..252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21515635"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21515635"
FT BINDING 297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21515635"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21515635"
FT MOD_RES 39
FT /note="N6-methylated lysine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:30189201"
FT MOD_RES 179
FT /note="N6-methylated lysine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:30189201"
FT MOD_RES 372
FT /note="N6-methylated lysine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:30189201"
FT VAR_SEQ 40..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024093"
FT VARIANT 185
FT /note="R -> S (in dbSNP:rs17852020)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_064590"
FT VARIANT 206
FT /note="R -> G (in dbSNP:rs17852021)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_064591"
FT VARIANT 340
FT /note="D -> N (in dbSNP:rs11865588)"
FT /id="VAR_064592"
FT VARIANT 426
FT /note="T -> A (in dbSNP:rs34965375)"
FT /id="VAR_064593"
FT VARIANT 445
FT /note="A -> V (in dbSNP:rs36085499)"
FT /id="VAR_064594"
FT MUTAGEN 39
FT /note="K->R: Greatly decreases automethylation. Impairs the
FT methyltransferase activity toward RELA and PAK4; when
FT associated with Arg-179."
FT /evidence="ECO:0000269|PubMed:30189201"
FT MUTAGEN 179
FT /note="K->R: Abolishes automethylation. Impairs the
FT methyltransferase activity toward RELA and PAK4; when
FT associated with Arg-39."
FT /evidence="ECO:0000269|PubMed:30189201"
FT MUTAGEN 283
FT /note="N->A: Impairs the methyltransferase activity toward
FT RELA."
FT /evidence="ECO:0000269|PubMed:21515635"
FT MUTAGEN 283
FT /note="N->F: Decreases the methyltransferase activity
FT toward RELA."
FT /evidence="ECO:0000269|PubMed:21515635"
FT MUTAGEN 285
FT /note="Y->A: Abolishes methyltransferase activity. Greatly
FT decreases the stability of monomeric, homodimeric and
FT homotrimeric structures."
FT /evidence="ECO:0000269|PubMed:21131967,
FT ECO:0000269|PubMed:30189201"
FT MUTAGEN 372
FT /note="K->R: Has little effect on automethylation level."
FT /evidence="ECO:0000269|PubMed:30189201"
FT CONFLICT 102
FT /note="T -> A (in Ref. 1; BAF83184)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="S -> G (in Ref. 1; BAB15011)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="E -> V (in Ref. 1; BAB15011)"
FT /evidence="ECO:0000305"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:3QXY"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:3QXY"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:3QXY"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3QXY"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3RC0"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3QXY"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 173..190
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:3QXY"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:3QXY"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:3QXY"
FT STRAND 264..273
FT /evidence="ECO:0007829|PDB:3QXY"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:3QXY"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 329..344
FT /evidence="ECO:0007829|PDB:3QXY"
FT STRAND 353..363
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 364..375
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:3QXY"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 410..424
FT /evidence="ECO:0007829|PDB:3QXY"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 431..439
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 441..446
FT /evidence="ECO:0007829|PDB:3QXY"
FT HELIX 449..471
FT /evidence="ECO:0007829|PDB:3QXY"
SQ SEQUENCE 473 AA; 53189 MW; 3BFC08F0FACEAACC CRC64;
MATQAKRPRV AGPVDGGDLD PVACFLSWCR RVGLELSPKV SERAGGRRTR GGARAALTSP
PAQVAVSRQG TVAGYGMVAR ESVQAGELLF VVPRAALLSQ HTCSIGGLLE RERVALQSQS
GWVPLLLALL HELQAPASRW RPYFALWPEL GRLEHPMFWP EEERRCLLQG TGVPEAVEKD
LANIRSEYQS IVLPFMEAHP DLFSLRVRSL ELYHQLVALV MAYSFQEPLE EEEDEKEPNS
PVMVPAADIL NHLANHNANL EYSANCLRMV ATQPIPKGHE IFNTYGQMAN WQLIHMYGFV
EPYPDNTDDT ADIQMVTVRE AALQGTKTEA ERHLVYERWD FLCKLEMVGE EGAFVIGREE
VLTEEELTTT LKVLCMPAEE FRELKDQDGG GDDKREEGSL TITNIPKLKA SWRQLLQNSV
LLTLQTYATD LKTDQGLLSN KEVYAKLSWR EQQALQVRYG QKMILHQLLE LTS
