KDM6B_MOUSE
ID KDM6B_MOUSE Reviewed; 1641 AA.
AC Q5NCY0; Q3UWY9; Q4VC26; Q6ZQD3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Lysine-specific demethylase 6B;
DE EC=1.14.11.68 {ECO:0000250|UniProtKB:O15054};
DE AltName: Full=JmjC domain-containing protein 3;
DE AltName: Full=Jumonji domain-containing protein 3;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase 6B {ECO:0000305};
GN Name=Kdm6b; Synonyms=Jmjd3, Kiaa0346;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 935-1641.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1138-1641.
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP INTERACTION WITH TLE1.
RX PubMed=9854018; DOI=10.1042/bj3370013;
RA Grbavec D., Lo R., Liu Y., Greenfield A., Stifani S.;
RT "Groucho/transducin-like enhancer of split (TLE) family members interact
RT with the yeast transcriptional co-repressor SSN6 and mammalian SSN6-related
RT proteins: implications for evolutionary conservation of transcription
RT repression mechanisms.";
RL Biochem. J. 337:13-17(1999).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=17825402; DOI=10.1016/j.cell.2007.08.019;
RA De Santa F., Totaro M.G., Prosperini E., Notarbartolo S., Testa G.,
RA Natoli G.;
RT "The histone H3 lysine-27 demethylase Jmjd3 links inflammation to
RT inhibition of polycomb-mediated gene silencing.";
RL Cell 130:1083-1094(2007).
RN [7]
RP FUNCTION, INTERACTION WITH TBX21; SMARCA4; SMARCC1 AND SMARCC2, AND
RP MUTAGENESIS OF HIS-1388; GLU-1390 AND HIS-1468.
RX PubMed=21095589; DOI=10.1016/j.molcel.2010.10.028;
RA Miller S.A., Mohn S.E., Weinmann A.S.;
RT "Jmjd3 and UTX play a demethylase-independent role in chromatin remodeling
RT to regulate T-box family member-dependent gene expression.";
RL Mol. Cell 40:594-605(2010).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-27'
CC of histone H3, thereby playing a central role in histone code.
CC Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a
CC central role in regulation of posterior development, by regulating HOX
CC gene expression. Involved in inflammatory response by participating in
CC macrophage differentiation in case of inflammation by regulating gene
CC expression and macrophage differentiation (PubMed:17825402). Plays a
CC demethylase-independent role in chromatin remodeling to regulate T-box
CC family member-dependent gene expression by acting as a link between T-
CC box factors and the SMARCA4-containing SWI/SNF remodeling complex
CC (PubMed:21095589). {ECO:0000269|PubMed:17825402,
CC ECO:0000269|PubMed:21095589}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224,
CC Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.68; Evidence={ECO:0000250|UniProtKB:O15054};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with TLE1 (PubMed:21095589). Component of the MLL4
CC complex, at least composed of KMT2B/MLL4, ASH2L, RBBP5, WDR5, and KDM6B
CC (By similarity). Interacts with TBX21, SMARCA4, SMARCC1 and SMARCC2
CC (PubMed:21095589). {ECO:0000250|UniProtKB:O15054,
CC ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:9854018}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- INDUCTION: By inflammatory stimuli; mediated by NF-kappa-B.
CC {ECO:0000269|PubMed:17825402}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE22775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AL596125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC075632; AAH75632.1; -; mRNA.
DR EMBL; AK129121; BAC97931.1; -; mRNA.
DR EMBL; AK136019; BAE22775.1; ALT_INIT; mRNA.
DR CCDS; CCDS24895.1; -.
DR RefSeq; NP_001017426.1; NM_001017426.1.
DR RefSeq; XP_006532961.1; XM_006532898.1.
DR RefSeq; XP_011247221.1; XM_011248919.2.
DR RefSeq; XP_011247222.1; XM_011248920.2.
DR RefSeq; XP_011247223.1; XM_011248921.1.
DR RefSeq; XP_011247224.1; XM_011248922.2.
DR RefSeq; XP_011247225.1; XM_011248923.1.
DR PDB; 4EYU; X-ray; 2.30 A; A/B=1155-1293, A/B=1321-1641.
DR PDB; 4EZ4; X-ray; 2.99 A; A/B=1155-1293, A/B=1321-1641.
DR PDB; 4EZH; X-ray; 2.52 A; A/B=1155-1293, A/B=1321-1641.
DR PDBsum; 4EYU; -.
DR PDBsum; 4EZ4; -.
DR PDBsum; 4EZH; -.
DR AlphaFoldDB; Q5NCY0; -.
DR SMR; Q5NCY0; -.
DR BioGRID; 229803; 10.
DR DIP; DIP-39160N; -.
DR IntAct; Q5NCY0; 5.
DR STRING; 10090.ENSMUSP00000091620; -.
DR iPTMnet; Q5NCY0; -.
DR PhosphoSitePlus; Q5NCY0; -.
DR EPD; Q5NCY0; -.
DR MaxQB; Q5NCY0; -.
DR PaxDb; Q5NCY0; -.
DR PeptideAtlas; Q5NCY0; -.
DR PRIDE; Q5NCY0; -.
DR ProteomicsDB; 263525; -.
DR Antibodypedia; 24405; 370 antibodies from 33 providers.
DR DNASU; 216850; -.
DR Ensembl; ENSMUST00000094077; ENSMUSP00000091620; ENSMUSG00000018476.
DR GeneID; 216850; -.
DR KEGG; mmu:216850; -.
DR UCSC; uc007jqd.1; mouse.
DR CTD; 23135; -.
DR MGI; MGI:2448492; Kdm6b.
DR VEuPathDB; HostDB:ENSMUSG00000018476; -.
DR eggNOG; KOG1124; Eukaryota.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000160414; -.
DR HOGENOM; CLU_001909_0_0_1; -.
DR InParanoid; Q5NCY0; -.
DR OMA; LHGDVWG; -.
DR OrthoDB; 268901at2759; -.
DR PhylomeDB; Q5NCY0; -.
DR TreeFam; TF317405; -.
DR BRENDA; 1.14.11.68; 3474.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 216850; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Kdm6b; mouse.
DR PRO; PR:Q5NCY0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5NCY0; protein.
DR Bgee; ENSMUSG00000018476; Expressed in internal carotid artery and 222 other tissues.
DR Genevisible; Q5NCY0; MM.
DR GO; GO:0044666; C:MLL3/4 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:BHF-UCL.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0045446; P:endothelial cell differentiation; IMP:BHF-UCL.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0016577; P:histone demethylation; IMP:MGI.
DR GO; GO:0071557; P:histone H3-K27 demethylation; IDA:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0048333; P:mesodermal cell differentiation; IMP:BHF-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR029518; KDM6B.
DR PANTHER; PTHR14017:SF5; PTHR14017:SF5; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Dioxygenase; Inflammatory response;
KW Iron; Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..1641
FT /note="Lysine-specific demethylase 6B"
FT /id="PRO_0000292008"
FT DOMAIN 1337..1500
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 42..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..490
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..529
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..610
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..664
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..909
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..990
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1067
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1388
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 1390
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 1468
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1573
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1576
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15054"
FT CROSSLNK 1107
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15054"
FT MUTAGEN 1388
FT /note="H->A: No loss of its ability to regulate TBX21-
FT dependent gene expression or its ability to interact with
FT SMARCA4; when associated with A-1390 and A-1468."
FT /evidence="ECO:0000269|PubMed:21095589"
FT MUTAGEN 1390
FT /note="E->A: No loss of its ability to regulate TBX21-
FT dependent gene expression or its ability to interact with
FT SMARCA4; when associated with A-1388 and A-1468."
FT /evidence="ECO:0000269|PubMed:21095589"
FT MUTAGEN 1468
FT /note="H->A: No loss of its ability to regulate TBX21-
FT dependent gene expression or its ability to interact with
FT SMARCA4; when associated with A-1388 and A-1390."
FT /evidence="ECO:0000269|PubMed:21095589"
FT CONFLICT 172
FT /note="P -> S (in Ref. 2; AAH75632)"
FT /evidence="ECO:0000305"
FT CONFLICT 965
FT /note="A -> T (in Ref. 3; BAC97931)"
FT /evidence="ECO:0000305"
FT CONFLICT 1290
FT /note="L -> LQ (in Ref. 3; BAC97931)"
FT /evidence="ECO:0000305"
FT HELIX 1160..1162
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1170..1172
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1176..1179
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1185..1187
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1191..1195
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1197..1203
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1209..1214
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1216..1220
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1224..1227
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1229..1236
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1240..1247
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1260..1262
FT /evidence="ECO:0007829|PDB:4EZ4"
FT STRAND 1269..1274
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1275..1295
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1323..1331
FT /evidence="ECO:0007829|PDB:4EYU"
FT TURN 1335..1338
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1339..1344
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1345..1347
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1350..1352
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1353..1355
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1360..1363
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1364..1366
FT /evidence="ECO:0007829|PDB:4EYU"
FT TURN 1369..1371
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1375..1379
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1384..1388
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1391..1393
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1395..1404
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1406..1411
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1413..1415
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1416..1425
FT /evidence="ECO:0007829|PDB:4EYU"
FT TURN 1430..1432
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1439..1444
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1450..1454
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1459..1462
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1467..1483
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1488..1503
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1512..1522
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1528..1553
FT /evidence="ECO:0007829|PDB:4EYU"
FT TURN 1554..1556
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1559..1561
FT /evidence="ECO:0007829|PDB:4EYU"
FT TURN 1574..1576
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1582..1588
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1596..1599
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1601..1607
FT /evidence="ECO:0007829|PDB:4EYU"
FT STRAND 1615..1620
FT /evidence="ECO:0007829|PDB:4EYU"
FT HELIX 1622..1631
FT /evidence="ECO:0007829|PDB:4EYU"
SQ SEQUENCE 1641 AA; 176355 MW; 6CBE3620998427EA CRC64;
MHRAVDPPGA RSAREAFALG GLSCAGAWSS CPPHPPPRSS WLPGGRCSAS VGQPPLSAPL
PPSHGSSSGH PNKPYYAPGT PTPRPLHGKL ESLHGCVQAL LREPAQPGLW EQLGQLYESE
HDSEEAVCCY HRALRYGGSF AELGPRIGRL QQAQLWNFHA GSCQHRAKVL PPLEQVWNLL
HLEHKRNYGA KRGGPPVKRS AEPPVVQPMP PAALSGPSGE EGLSPGGKRR RGCSSEQAGL
PPGLPLPPPP PPPPPPPPPP PPPPPPLPGL AISPPFQLTK PGLWNTLHGD AWGPERKGSA
PPERQEQRHS MPHSYPYPAP AYSAHPPSHR LVPNTPLGPG PRPPGAESHG CLPATRPPGS
DLRESRVQRS RMDSSVSPAA STACVPYAPS RPPGLPGTSS SSSSSSSSNN TGLRGVEPSP
GIPGADHYQN PALEISPHQA RLGPSAHSSR KPFLTAPAAT PHLSLPPGTP SSPPPPCPRL
LRPPPPPAWM KGSACRAARE DGEILGELFF GAEGPPRPPP PPLPHRDGFL GPPNPRFSVG
TQDSHNPPIP PTTTSSSSSS NSHSSSPTGP VPFPPPSYLA RSIDPLPRPS SPTLSPQDPP
LPPLTLALPP APPSSCHQNT SGSFRRSESP RPRVSFPKTP EVGQGPPPGP VSKAPQPVPP
GVGELPARGP RLFDFPPTPL EDQFEEPAEF KILPDGLANI MKMLDESIRK EEEQQQQQEA
GVAPPPPLKE PFASLQPPFP SDTAPATTTA APTTATTTTT TTTTTTQEEE KKPPPALPPP
PPLAKFPPPP QPQPPPPPPA SPASLLKSLA SVLEGQKYCY RGTGAAVSTR PGSVPATQYS
PSPASGATAP PPTSVAPSAQ GSPKPSVSSS SQFSTSGGPW AREHRAGEEP APGPVTPAQL
PPPLPLPPAR SESEVLEEIS RACETLVERV GRSAINPVDT ADPVDSGTEP QPPPAQAKEE
SGGVAVAAAG PGSGKRRQKE HRRHRRACRD SVGRRPREGR AKAKAKAPKE KSRRVLGNLD
LQSEEIQGRE KARPDVGGVS KVKTPTAPAP PPAPAPAAQP TPPSAPVPGK KTREEAPGPP
GVSRADMLKL RSLSEGPPKE LKIRLIKVES GDKETFIASE VEERRLRMAD LTISHCAADV
MRASKNAKVK GKFRESYLSP AQSVKPKINT EEKLPREKLN PPTPSIYLES KRDAFSPVLL
QFCTDPRNPI TVIRGLAGSL RLNLGLFSTK TLVEASGEHT VEVRTQVQQP SDENWDLTGT
RQIWPCESSR SHTTIAKYAQ YQASSFQESL QEERESEDEE SEEPDSTTGT SPSSAPDPKN
HHIIKFGTNI DLSDAKRWKP QLQELLKLPA FMRVTSTGNM LSHVGHTILG MNTVQLYMKV
PGSRTPGHQE NNNFCSVNIN IGPGDCEWFA VHEHYWETIS AFCDRHGVDY LTGSWWPILD
DLYASNIPVY RFVQRPGDLV WINAGTVHWV QATGWCNNIA WNVGPLTAYQ YQLALERYEW
NEVKNVKSIV PMIHVSWNVA RTVKISDPDL FKMIKFCLLQ SMKHCQVQRE SLVRAGKKIA
YQGRVKDEPA YYCNECDVEV FNILFVTSEN GSRNTYLVHC EGCARRRSAG LQGVVVLEQY
RTEELAQAYD AFTLAPASTS R
