UTY_HUMAN
ID UTY_HUMAN Reviewed; 1347 AA.
AC O14607; A8K9Z3; E1U199; E1U1A0; F5H4V7; F8W8R7; O14608;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Histone demethylase UTY;
DE EC=1.14.11.68 {ECO:0000269|PubMed:24798337};
DE AltName: Full=Ubiquitously-transcribed TPR protein on the Y chromosome;
DE AltName: Full=Ubiquitously-transcribed Y chromosome tetratricopeptide repeat protein;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase UTY {ECO:0000305};
GN Name=UTY; Synonyms=KDM6C;
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 [MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=9381176; DOI=10.1126/science.278.5338.675;
RA Lahn B.T., Page D.C.;
RT "Functional coherence of the human Y chromosome.";
RL Science 278:675-680(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5).
RA Laaser I., Kolb H.J., Adamski J.;
RT "Characterization of the human UTY gene.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12815422; DOI=10.1038/nature01722;
RA Skaletsky H., Kuroda-Kawaguchi T., Minx P.J., Cordum H.S., Hillier L.W.,
RA Brown L.G., Repping S., Pyntikova T., Ali J., Bieri T., Chinwalla A.,
RA Delehaunty A., Delehaunty K., Du H., Fewell G., Fulton L., Fulton R.,
RA Graves T.A., Hou S.-F., Latrielle P., Leonard S., Mardis E., Maupin R.,
RA McPherson J., Miner T., Nash W., Nguyen C., Ozersky P., Pepin K., Rock S.,
RA Rohlfing T., Scott K., Schultz B., Strong C., Tin-Wollam A., Yang S.-P.,
RA Waterston R.H., Wilson R.K., Rozen S., Page D.C.;
RT "The male-specific region of the human Y chromosome is a mosaic of discrete
RT sequence classes.";
RL Nature 423:825-837(2003).
RN [5]
RP PROTEIN SEQUENCE OF 461-468.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 878-1347 IN COMPLEX WITH 2-OG AND
RP INHIBITOR, IRON-BINDING SITES, ZINC-BINDING SITES, FUNCTION, CATALYTIC
RP ACTIVITY, PHOSPHORYLATION AT THR-887, AND MUTAGENESIS OF HIS-1093; SER-1138
RP AND PRO-1214.
RX PubMed=24798337; DOI=10.1074/jbc.m114.555052;
RA Walport L.J., Hopkinson R.J., Vollmar M., Madden S.K., Gileadi C.,
RA Oppermann U., Schofield C.J., Johansson C.;
RT "Human UTY(KDM6C) is a male-specific N-methyl lysyl demethylase.";
RL J. Biol. Chem. 289:18302-18313(2014).
CC -!- FUNCTION: Male-specific histone demethylase that catalyzes
CC trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3. Has
CC relatively low lysine demethylase activity.
CC {ECO:0000269|PubMed:24798337}.
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:0000269|PubMed:24798337};
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 and TLE2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Long;
CC IsoId=O14607-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=O14607-2; Sequence=VSP_006556, VSP_036783;
CC Name=3;
CC IsoId=O14607-3; Sequence=VSP_036784;
CC Name=4;
CC IsoId=O14607-4; Sequence=VSP_045611;
CC Name=5;
CC IsoId=O14607-5; Sequence=VSP_045611, VSP_045612, VSP_045613;
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000305}.
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DR EMBL; AF000994; AAC51841.1; -; mRNA.
DR EMBL; AF000995; AAC51842.1; -; mRNA.
DR EMBL; AF000996; AAC51843.1; -; mRNA.
DR EMBL; DQ140389; ABA25870.1; -; mRNA.
DR EMBL; DQ140390; ABA25871.1; -; mRNA.
DR EMBL; AK292858; BAF85547.1; -; mRNA.
DR EMBL; AC005820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14783.1; -. [O14607-1]
DR CCDS; CCDS14784.1; -. [O14607-3]
DR CCDS; CCDS14785.1; -. [O14607-2]
DR CCDS; CCDS59184.1; -. [O14607-4]
DR CCDS; CCDS59185.1; -. [O14607-5]
DR PIR; T02214; T02214.
DR RefSeq; NP_001245181.1; NM_001258252.1. [O14607-4]
DR RefSeq; NP_001245183.1; NM_001258254.1. [O14607-5]
DR RefSeq; NP_009056.3; NM_007125.4. [O14607-1]
DR RefSeq; NP_872600.1; NM_182659.1. [O14607-3]
DR RefSeq; NP_872601.1; NM_182660.1. [O14607-2]
DR PDB; 3ZLI; X-ray; 1.80 A; A/B=878-1347.
DR PDB; 3ZPO; X-ray; 2.00 A; A/B=878-1347.
DR PDB; 4UF0; X-ray; 1.78 A; A/B=878-1347.
DR PDB; 5A1L; X-ray; 2.00 A; A/B=878-1347.
DR PDB; 5FXV; X-ray; 1.91 A; A/B=878-1347.
DR PDB; 5FXW; X-ray; 2.09 A; A/B=878-1347.
DR PDB; 5FXX; X-ray; 1.99 A; A/B=878-1347.
DR PDB; 5FXZ; X-ray; 1.98 A; A/B=878-1347.
DR PDB; 5FY0; X-ray; 2.14 A; A/B=878-1347.
DR PDB; 5FY1; X-ray; 1.78 A; A/B=878-1347.
DR PDB; 5FY7; X-ray; 1.86 A; A/B=878-1347.
DR PDB; 5FYM; X-ray; 2.00 A; A/B=878-1347.
DR PDBsum; 3ZLI; -.
DR PDBsum; 3ZPO; -.
DR PDBsum; 4UF0; -.
DR PDBsum; 5A1L; -.
DR PDBsum; 5FXV; -.
DR PDBsum; 5FXW; -.
DR PDBsum; 5FXX; -.
DR PDBsum; 5FXZ; -.
DR PDBsum; 5FY0; -.
DR PDBsum; 5FY1; -.
DR PDBsum; 5FY7; -.
DR PDBsum; 5FYM; -.
DR AlphaFoldDB; O14607; -.
DR SMR; O14607; -.
DR BioGRID; 113247; 18.
DR DIP; DIP-48650N; -.
DR IntAct; O14607; 13.
DR MINT; O14607; -.
DR iPTMnet; O14607; -.
DR PhosphoSitePlus; O14607; -.
DR BioMuta; UTY; -.
DR EPD; O14607; -.
DR jPOST; O14607; -.
DR MassIVE; O14607; -.
DR MaxQB; O14607; -.
DR PaxDb; O14607; -.
DR PeptideAtlas; O14607; -.
DR PRIDE; O14607; -.
DR ProteomicsDB; 26687; -.
DR ProteomicsDB; 30194; -.
DR ProteomicsDB; 48111; -. [O14607-1]
DR ProteomicsDB; 48112; -. [O14607-2]
DR ProteomicsDB; 48113; -. [O14607-3]
DR TopDownProteomics; O14607-2; -. [O14607-2]
DR Antibodypedia; 21867; 154 antibodies from 23 providers.
DR DNASU; 7404; -.
DR Ensembl; ENST00000329134.9; ENSP00000330446.5; ENSG00000183878.16. [O14607-2]
DR Ensembl; ENST00000331397.8; ENSP00000328939.4; ENSG00000183878.16. [O14607-1]
DR Ensembl; ENST00000362096.8; ENSP00000355420.4; ENSG00000183878.16. [O14607-3]
DR Ensembl; ENST00000624098.3; ENSP00000485539.2; ENSG00000183878.16. [O14607-5]
DR Ensembl; ENST00000682913.1; ENSP00000507736.1; ENSG00000183878.16. [O14607-4]
DR GeneID; 7404; -.
DR KEGG; hsa:7404; -.
DR UCSC; uc004fsx.3; human. [O14607-1]
DR CTD; 7404; -.
DR DisGeNET; 7404; -.
DR GeneCards; UTY; -.
DR HGNC; HGNC:12638; UTY.
DR HPA; ENSG00000183878; Tissue enhanced (brain).
DR MIM; 400009; gene.
DR neXtProt; NX_O14607; -.
DR OpenTargets; ENSG00000183878; -.
DR PharmGKB; PA37263; -.
DR VEuPathDB; HostDB:ENSG00000183878; -.
DR GeneTree; ENSGT00940000155202; -.
DR HOGENOM; CLU_003187_1_0_1; -.
DR InParanoid; O14607; -.
DR OrthoDB; 268901at2759; -.
DR PhylomeDB; O14607; -.
DR TreeFam; TF317405; -.
DR BioCyc; MetaCyc:MON66-43915; -.
DR PathwayCommons; O14607; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR SignaLink; O14607; -.
DR BioGRID-ORCS; 7404; 19 hits in 718 CRISPR screens.
DR ChiTaRS; UTY; human.
DR GeneWiki; UTY_(gene); -.
DR GenomeRNAi; 7404; -.
DR Pharos; O14607; Tbio.
DR PRO; PR:O14607; -.
DR Proteomes; UP000005640; Chromosome Y.
DR RNAct; O14607; protein.
DR Bgee; ENSG00000183878; Expressed in corpus callosum and 158 other tissues.
DR ExpressionAtlas; O14607; baseline and differential.
DR Genevisible; O14607; HS.
DR GO; GO:0044666; C:MLL3/4 complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
DR GO; GO:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; IBA:GO_Central.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0071557; P:histone H3-K27 demethylation; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Dioxygenase;
KW Direct protein sequencing; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Zinc.
FT CHAIN 1..1347
FT /note="Histone demethylase UTY"
FT /id="PRO_0000106411"
FT REPEAT 90..123
FT /note="TPR 1"
FT REPEAT 127..160
FT /note="TPR 2"
FT REPEAT 167..196
FT /note="TPR 3"
FT REPEAT 202..235
FT /note="TPR 4"
FT REPEAT 247..280
FT /note="TPR 5"
FT REPEAT 281..314
FT /note="TPR 6"
FT REPEAT 315..348
FT /note="TPR 7"
FT REPEAT 349..382
FT /note="TPR 8"
FT DOMAIN 1042..1205
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 571..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1093
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:24798337"
FT BINDING 1095
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:24798337"
FT BINDING 1173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:24798337"
FT BINDING 1278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24798337"
FT BINDING 1281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24798337"
FT BINDING 1305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24798337"
FT BINDING 1308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24798337"
FT MOD_RES 887
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24798337"
FT VAR_SEQ 394
FT /note="L -> LQAQLCNLPQSSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQ
FT (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_045611"
FT VAR_SEQ 465..588
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_045612"
FT VAR_SEQ 996..1079
FT /note="EENEKRTQHKDHSDNESTSSENSGRRRKGPFKTIKFGTNIDLSDNKKWKLQL
FT HELTKLPAFARVVSAGNLLTHVGHTILGMNTV -> AGMQWCDLSSLQPPPPGFKRFSH
FT LSLPNSWNYRHLPSCPTNFCIFVETGFHHVGQACLELLTSGGLLASASQSAGITGVSHH
FT AR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9381176"
FT /id="VSP_006556"
FT VAR_SEQ 1080..1347
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9381176"
FT /id="VSP_036783"
FT VAR_SEQ 1241..1347
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9381176"
FT /id="VSP_036784"
FT VAR_SEQ 1283..1339
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_045613"
FT MUTAGEN 1093
FT /note="H->A: Abolishes lysine demethylase activity."
FT /evidence="ECO:0000269|PubMed:24798337"
FT MUTAGEN 1138
FT /note="S->G: No effect on lysine demethylase activity."
FT /evidence="ECO:0000269|PubMed:24798337"
FT MUTAGEN 1214
FT /note="P->I: Significantly higher lysine demethylase
FT activity."
FT /evidence="ECO:0000269|PubMed:24798337"
FT CONFLICT 81
FT /note="I -> L (in Ref. 2; ABA25871)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="G -> R (in Ref. 2; ABA25870)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="D -> G (in Ref. 2; ABA25870)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="Y -> C (in Ref. 2; ABA25871)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="V -> A (in Ref. 2; ABA25870)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="F -> S (in Ref. 3; BAF85547)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="I -> V (in Ref. 2; ABA25870)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="Y -> H (in Ref. 2; ABA25870)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="L -> P (in Ref. 2; ABA25870)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="I -> T (in Ref. 3; BAF85547)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="A -> V (in Ref. 2; ABA25870)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="S -> R (in Ref. 2; ABA25871)"
FT /evidence="ECO:0000305"
FT CONFLICT 1177
FT /note="A -> T (in Ref. 1; AAC51841/AAC51842)"
FT /evidence="ECO:0000305"
FT HELIX 881..883
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 889..891
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 895..899
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 901..908
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 913..918
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 920..924
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 928..931
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 933..940
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 944..951
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 963..966
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 972..978
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 979..997
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1028..1036
FT /evidence="ECO:0007829|PDB:4UF0"
FT TURN 1040..1042
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1044..1049
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1050..1052
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1055..1057
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1058..1060
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1065..1068
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1069..1071
FT /evidence="ECO:0007829|PDB:5FY0"
FT TURN 1074..1076
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1080..1084
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1089..1093
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1096..1098
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1100..1109
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1111..1116
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1118..1120
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1121..1130
FT /evidence="ECO:0007829|PDB:4UF0"
FT TURN 1135..1137
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1144..1149
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1155..1159
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1164..1167
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1172..1188
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1190..1192
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1193..1208
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1217..1227
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1233..1259
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1264..1266
FT /evidence="ECO:0007829|PDB:4UF0"
FT TURN 1279..1281
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1287..1292
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1293..1297
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1306..1312
FT /evidence="ECO:0007829|PDB:4UF0"
FT STRAND 1319..1325
FT /evidence="ECO:0007829|PDB:4UF0"
FT HELIX 1327..1335
FT /evidence="ECO:0007829|PDB:4UF0"
SQ SEQUENCE 1347 AA; 149548 MW; D83B8CAB861BCE60 CRC64;
MKSCAVSLTT AAVAFGDEAK KMAEGKASRE SEEESVSLTV EEREALGGMD SRLFGFVRLH
EDGARTKTLL GKAVRCYESL ILKAEGKVES DFFCQLGHFN LLLEDYSKAL SAYQRYYSLQ
ADYWKNAAFL YGLGLVYFYY NAFHWAIKAF QDVLYVDPSF CRAKEIHLRL GLMFKVNTDY
KSSLKHFQLA LIDCNPCTLS NAEIQFHIAH LYETQRKYHS AKEAYEQLLQ TENLPAQVKA
TVLQQLGWMH HNMDLVGDKA TKESYAIQYL QKSLEADPNS GQSWYFLGRC YSSIGKVQDA
FISYRQSIDK SEASADTWCS IGVLYQQQNQ PMDALQAYIC AVQLDHGHAA AWMDLGTLYE
SCNQPQDAIK CYLNAARSKR CSNTSTLAAR IKFLQNGSDN WNGGQSLSHH PVQQVYSLCL
TPQKLQHLEQ LRANRDNLNP AQKHQLEQLE SQFVLMQQMR HKEVAQVRTT GIHNGAITDS
SLPTNSVSNR QPHGALTRVS SVSQPGVRPA CVEKLLSSGA FSAGCIPCGT SKILGSTDTI
LLGSNCIAGS ESNGNVPYLQ QNTHTLPHNH TDLNSSTEEP WRKQLSNSAQ GLHKSQSSCL
SGPNEEQPLF STGSAQYHQA TSTGIKKANE HLTLPSNSVP QGDADSHLSC HTATSGGQQG
IMFTKESKPS KNRSLVPETS RHTGDTSNGC ADVKGLSNHV HQLIADAVSS PNHGDSPNLL
IADNPQLSAL LIGKANGNVG TGTCDKVNNI HPAVHTKTDH SVASSPSSAI STATPSPKST
EQRSINSVTS LNSPHSGLHT VNGEGLGKSQ SSTKVDLPLA SHRSTSQILP SMSVSICPSS
TEVLKACRNP GKNGLSNSCI LLDKCPPPRP PTSPYPPLPK DKLNPPTPSI YLENKRDAFF
PPLHQFCTNP KNPVTVIRGL AGALKLDLGL FSTKTLVEAN NEHMVEVRTQ LLQPADENWD
PTGTKKIWRC ESNRSHTTIA KYAQYQASSF QESLREENEK RTQHKDHSDN ESTSSENSGR
RRKGPFKTIK FGTNIDLSDN KKWKLQLHEL TKLPAFARVV SAGNLLTHVG HTILGMNTVQ
LYMKVPGSRT PGHQENNNFC SVNINIGPGD CEWFVVPEDY WGVLNDFCEK NNLNFLMSSW
WPNLEDLYEA NVPVYRFIQR PGDLVWINAG TVHWVQAVGW CNNIAWNVGP LTACQYKLAV
ERYEWNKLKS VKSPVPMVHL SWNMARNIKV SDPKLFEMIK YCLLKILKQY QTLREALVAA
GKEVIWHGRT NDEPAHYCSI CEVEVFNLLF VTNESNTQKT YIVHCHDCAR KTSKSLENFV
VLEQYKMEDL IQVYDQFTLA LSLSSSS
