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Lysine-specific demethylase 5D (EC 1.14.11.-) (Histocompatibility Y antigen) (H-Y) (Histone demethylase JARID1D) (Jumonji/ARID domain-containing protein 1D) (Protein SmcY)

 KDM5D_HUMAN             Reviewed;        1539 AA.
Q9BY66; A2RU19; A6H8V7; B7ZLX1; Q92509; Q92809; Q9HCU1;
24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
24-OCT-2001, sequence version 2.
25-OCT-2017, entry version 155.
RecName: Full=Lysine-specific demethylase 5D;
EC=1.14.11.-;
AltName: Full=Histocompatibility Y antigen;
Short=H-Y;
AltName: Full=Histone demethylase JARID1D;
AltName: Full=Jumonji/ARID domain-containing protein 1D;
AltName: Full=Protein SmcY;
Name=KDM5D; Synonyms=HY, HYA, JARID1D, KIAA0234, SMCY;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-1186.
PubMed=8841177; DOI=10.1038/ng1096-128;
Kent-First M.G., Maffitt M., Muallem A., Brisco P., Shultz J.,
Ekenberg S., Agulnik A.I., Agulnik S.I., Shramm D., Bavister B.,
Abdul-Mawgood A., Vandeberg J.;
"Gene sequence and evolutionary conservation of human SMCY.";
Nat. Genet. 14:128-129(1996).
[2]
ERRATUM.
Kent-First M.G., Maffitt M., Muallem A., Brisco P., Shultz J.,
Ekenberg S., Agulnik A.I., Agulnik S.I., Shramm D., Bavister B.,
Abdul-Mawgood A., Vandeberg J.;
Nat. Genet. 14:252-252(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Bone marrow;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=10861003; DOI=10.1073/pnas.97.13.7354;
Shen P., Wang F., Underhill P.A., Franco C., Yang W.-H., Roxas A.,
Sung R., Lin A.A., Hyman R.W., Vollrath D., Davis R.W.,
Cavalli-Sforza L.L., Oefner P.J.;
"Population genetic implications from sequence variation in four Y
chromosome genes.";
Proc. Natl. Acad. Sci. U.S.A. 97:7354-7359(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12815422; DOI=10.1038/nature01722;
Skaletsky H., Kuroda-Kawaguchi T., Minx P.J., Cordum H.S.,
Hillier L.W., Brown L.G., Repping S., Pyntikova T., Ali J., Bieri T.,
Chinwalla A., Delehaunty A., Delehaunty K., Du H., Fewell G.,
Fulton L., Fulton R., Graves T.A., Hou S.-F., Latrielle P.,
Leonard S., Mardis E., Maupin R., McPherson J., Miner T., Nash W.,
Nguyen C., Ozersky P., Pepin K., Rock S., Rohlfing T., Scott K.,
Schultz B., Strong C., Tin-Wollam A., Yang S.-P., Waterston R.H.,
Wilson R.K., Rozen S., Page D.C.;
"The male-specific region of the human Y chromosome is a mosaic of
discrete sequence classes.";
Nature 423:825-837(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-457 (ISOFORM 1).
PubMed=9060413; DOI=10.1007/s003359900372;
Agulnik A.I., Bishop C.E., Lerner J.L., Agulnik S.I., Solovyev V.V.;
"Analysis of mutation rates in the SMCY/SMCX genes shows that
mammalian evolution is male driven.";
Mamm. Genome 8:134-138(1997).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1340-1478.
TISSUE=Blood;
Poloumienko A., Blecher S.;
"Exon-intron structure of SMCX and SMCY genes in bovine and swine.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[10]
FUNCTION, COFACTOR, INTERACTION WITH PCGF6, AND MUTAGENESIS OF HIS-534
AND GLU-536.
PubMed=17320162; DOI=10.1016/j.cell.2007.02.004;
Lee M.G., Norman J., Shilatifard A., Shiekhattar R.;
"Physical and functional association of a trimethyl H3K4 demethylase
and Ring6a/MBLR, a polycomb-like protein.";
Cell 128:877-887(2007).
[11]
FUNCTION.
PubMed=17320160; DOI=10.1016/j.cell.2007.02.017;
Iwase S., Lan F., Bayliss P., de la Torre-Ubieta L., Huarte M.,
Qi H.H., Whetstine J.R., Bonni A., Roberts T.M., Shi Y.;
"The X-linked mental retardation gene SMCX/JARID1C defines a family of
histone H3 lysine 4 demethylases.";
Cell 128:1077-1088(2007).
[12]
FUNCTION.
PubMed=17351630; DOI=10.1038/nsmb1217;
Eissenberg J.C., Lee M.G., Schneider J., Ilvarsonn A., Shiekhattar R.,
Shilatifard A.;
"The trithorax-group gene in Drosophila little imaginal discs encodes
a trimethylated histone H3 Lys4 demethylase.";
Nat. Struct. Mol. Biol. 14:344-346(2007).
[13]
INTERACTION WITH MSH5.
PubMed=18459961; DOI=10.1111/j.1365-2443.2008.01193.x;
Akimoto C., Kitagawa H., Matsumoto T., Kato S.;
"Spermatogenesis-specific association of SMCY and MSH5.";
Genes Cells 13:623-633(2008).
[14]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=26747897; DOI=10.1158/0008-5472.CAN-15-0906;
Li N., Dhar S.S., Chen T.Y., Kan P.Y., Wei Y., Kim J.H., Chan C.H.,
Lin H.K., Hung M.C., Lee M.G.;
"JARID1D is a suppressor and prognostic marker of prostate cancer
invasion and metastasis.";
Cancer Res. 76:831-843(2016).
[15]
BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND COFACTOR.
PubMed=27427228; DOI=10.1016/j.chembiol.2016.06.006;
Horton J.R., Liu X., Gale M., Wu L., Shanks J.R., Zhang X.,
Webber P.J., Bell J.S., Kales S.C., Mott B.T., Rai G., Jansen D.J.,
Henderson M.J., Urban D.J., Hall M.D., Simeonov A., Maloney D.J.,
Johns M.A., Fu H., Jadhav A., Vertino P.M., Yan Q., Cheng X.;
"Structural Basis for KDM5A Histone Lysine Demethylase Inhibition by
Diverse Compounds.";
Cell Chem. Biol. 23:769-781(2016).
[16]
FUNCTION, INTERACTION WITH ZMYND8, AND SUBCELLULAR LOCATION.
PubMed=27477906; DOI=10.1016/j.molcel.2016.06.035;
Li N., Li Y., Lv J., Zheng X., Wen H., Shen H., Zhu G., Chen T.Y.,
Dhar S.S., Kan P.Y., Wang Z., Shiekhattar R., Shi X., Lan F., Chen K.,
Li W., Li H., Lee M.G.;
"ZMYND8 reads the dual histone mark H3K4me1-H3K14ac to antagonize the
expression of metastasis-linked genes.";
Mol. Cell 63:470-484(2016).
[17]
FUNCTION, INTERACTION WITH AR, SUBCELLULAR LOCATION, AND INVOLVEMENT
IN DOCETAXEL SENSITIVITY.
PubMed=27185910; DOI=10.1073/pnas.1600420113;
Komura K., Jeong S.H., Hinohara K., Qu F., Wang X., Hiraki M.,
Azuma H., Lee G.S., Kantoff P.W., Sweeney C.J.;
"Resistance to docetaxel in prostate cancer is associated with
androgen receptor activation and loss of KDM5D expression.";
Proc. Natl. Acad. Sci. U.S.A. 113:6259-6264(2016).
[18]
STRUCTURE BY NMR OF 79-384.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the PHD domain and of the ARID domain of
JARID1D/SMCY protein.";
Submitted (APR-2008) to the PDB data bank.
-!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
4' of histone H3, thereby playing a central role in histone code.
Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36',
H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and
dimethylated but not monomethylated H3 'Lys-4'. May play a role in
spermatogenesis. Involved in transcriptional repression of diverse
metastasis-associated genes; in this function seems to cooperate
with ZMYND8. Suppresses prostate cancer cell invasion. Regulates
androgen receptor (AR) transcriptional activity by demethylating
H3K4me3 active transcription marks. {ECO:0000269|PubMed:17320160,
ECO:0000269|PubMed:17320162, ECO:0000269|PubMed:17351630,
ECO:0000269|PubMed:26747897, ECO:0000269|PubMed:27185910,
ECO:0000269|PubMed:27427228, ECO:0000269|PubMed:27477906}.
-!- COFACTOR:
Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
Evidence={ECO:0000269|PubMed:17320162};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:17320162};
Note=Binds 1 Fe(2+) ion per subunit.
{ECO:0000269|PubMed:17320162};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=10 uM for 2-oxoglutarate {ECO:0000269|PubMed:27427228};
KM=6.2 uM for histone H3K4me3 {ECO:0000269|PubMed:27427228};
Note=Kcat are 2.6 min(-1) and 3.0 min(-1) for 2-oxoglutarate and
histone H3K4me3, respectively. {ECO:0000269|PubMed:27427228};
-!- SUBUNIT: Interacts with PCGF6, MSH5, ZMYND8, AR.
{ECO:0000269|PubMed:17320162, ECO:0000269|PubMed:18459961,
ECO:0000269|PubMed:27185910, ECO:0000269|PubMed:27477906}.
-!- INTERACTION:
P10275:AR; NbExp=2; IntAct=EBI-1246860, EBI-608057;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27185910,
ECO:0000269|PubMed:27477906, ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9BY66-1; Sequence=Displayed;
Name=2;
IsoId=Q9BY66-2; Sequence=VSP_000317;
Name=3;
IsoId=Q9BY66-3; Sequence=VSP_043320;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expression is highly down-regulated in
metastatic prostate tumors. {ECO:0000269|PubMed:26747897}.
-!- DOMAIN: The JmjC domain is required for enzymatic activity.
-!- MISCELLANEOUS: Involved in sensitivity to docetaxel.
{ECO:0000269|PubMed:27185910}.
-!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA13241.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U52191; AAC50806.1; -; mRNA.
EMBL; D87072; BAA13241.2; ALT_INIT; mRNA.
EMBL; AF273841; AAG00951.1; -; Genomic_DNA.
EMBL; AC010889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471202; EAW54663.1; -; Genomic_DNA.
EMBL; BC132721; AAI32722.1; -; mRNA.
EMBL; BC144102; AAI44103.1; -; mRNA.
EMBL; BC146767; AAI46768.1; -; mRNA.
EMBL; U52365; AAC51135.1; -; mRNA.
EMBL; AF134849; AAK27839.1; -; Genomic_DNA.
CCDS; CCDS14794.1; -. [Q9BY66-1]
CCDS; CCDS55554.1; -. [Q9BY66-2]
CCDS; CCDS55555.1; -. [Q9BY66-3]
RefSeq; NP_001140177.1; NM_001146705.1. [Q9BY66-3]
RefSeq; NP_001140178.1; NM_001146706.1. [Q9BY66-2]
RefSeq; NP_004644.2; NM_004653.4. [Q9BY66-1]
UniGene; Hs.80358; -.
PDB; 2E6R; NMR; -; A=306-384.
PDB; 2YQE; NMR; -; A=79-171.
PDBsum; 2E6R; -.
PDBsum; 2YQE; -.
ProteinModelPortal; Q9BY66; -.
SMR; Q9BY66; -.
BioGrid; 113891; 2.
IntAct; Q9BY66; 2.
STRING; 9606.ENSP00000444293; -.
BindingDB; Q9BY66; -.
DrugBank; DB00126; Vitamin C.
iPTMnet; Q9BY66; -.
PhosphoSitePlus; Q9BY66; -.
BioMuta; KDM5D; -.
DMDM; 17368706; -.
MaxQB; Q9BY66; -.
PaxDb; Q9BY66; -.
PeptideAtlas; Q9BY66; -.
PRIDE; Q9BY66; -.
Ensembl; ENST00000317961; ENSP00000322408; ENSG00000012817. [Q9BY66-1]
Ensembl; ENST00000382806; ENSP00000372256; ENSG00000012817. [Q9BY66-2]
Ensembl; ENST00000541639; ENSP00000444293; ENSG00000012817. [Q9BY66-3]
GeneID; 8284; -.
KEGG; hsa:8284; -.
UCSC; uc004fug.4; human. [Q9BY66-1]
CTD; 8284; -.
DisGeNET; 8284; -.
EuPathDB; HostDB:ENSG00000012817.15; -.
GeneCards; KDM5D; -.
GeneReviews; KDM5D; -.
HGNC; HGNC:11115; KDM5D.
HPA; HPA049086; -.
HPA; HPA060807; -.
MIM; 426000; gene.
neXtProt; NX_Q9BY66; -.
OpenTargets; ENSG00000012817; -.
PharmGKB; PA35965; -.
eggNOG; KOG1246; Eukaryota.
eggNOG; ENOG410XR9J; LUCA.
GeneTree; ENSGT00530000063118; -.
HOGENOM; HOG000290719; -.
InParanoid; Q9BY66; -.
KO; K11446; -.
OMA; CILAECK; -.
OrthoDB; EOG091G0RFR; -.
PhylomeDB; Q9BY66; -.
TreeFam; TF106476; -.
Reactome; R-HSA-3214842; HDMs demethylate histones.
ChiTaRS; KDM5D; human.
EvolutionaryTrace; Q9BY66; -.
GeneWiki; JARID1D; -.
GenomeRNAi; 8284; -.
PRO; PR:Q9BY66; -.
Proteomes; UP000005640; Chromosome Y.
Bgee; ENSG00000012817; -.
CleanEx; HS_JARID1D; -.
ExpressionAtlas; Q9BY66; baseline and differential.
Genevisible; Q9BY66; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0050681; F:androgen receptor binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
GO; GO:0032453; F:histone demethylase activity (H3-K4 specific); IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro.
GO; GO:0034720; P:histone H3-K4 demethylation; IDA:MGI.
GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0002457; P:T cell antigen processing and presentation; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.150.60; -; 1.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR001606; ARID_dom.
InterPro; IPR036431; ARID_dom_sf.
InterPro; IPR003347; JmjC_dom.
InterPro; IPR003349; JmjN.
InterPro; IPR013637; Lys_sp_deMease-like_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR004198; Znf_C5HC2.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF01388; ARID; 1.
Pfam; PF02373; JmjC; 1.
Pfam; PF02375; JmjN; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF08429; PLU-1; 1.
Pfam; PF02928; zf-C5HC2; 1.
SMART; SM00501; BRIGHT; 1.
SMART; SM00558; JmjC; 1.
SMART; SM00545; JmjN; 1.
SMART; SM00249; PHD; 2.
SUPFAM; SSF46774; SSF46774; 1.
SUPFAM; SSF57903; SSF57903; 2.
PROSITE; PS51011; ARID; 1.
PROSITE; PS51184; JMJC; 1.
PROSITE; PS51183; JMJN; 1.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus;
Oxidoreductase; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 1539 Lysine-specific demethylase 5D.
/FTId=PRO_0000200588.
DOMAIN 14 55 JmjN. {ECO:0000255|PROSITE-
ProRule:PRU00537}.
DOMAIN 79 169 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
DOMAIN 458 624 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
ZN_FING 316 362 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 697 749 C5HC2. {ECO:0000250|UniProtKB:P29375}.
ZN_FING 1174 1235 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
METAL 504 504 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 506 506 Iron; catalytic.
{ECO:0000250|UniProtKB:P29375}.
METAL 592 592 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
BINDING 430 430 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
BINDING 512 512 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
BINDING 514 514 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
BINDING 522 522 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
VAR_SEQ 118 174 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9039502}.
/FTId=VSP_000317.
VAR_SEQ 457 457 K -> KRQSLTVLTRLISSFWAQAVLPPWPPKVLGLQ (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043320.
VARIANT 1186 1186 V -> L (in dbSNP:rs1050807).
{ECO:0000269|PubMed:8841177}.
/FTId=VAR_032991.
MUTAGEN 534 534 H->A: Abolishes enzymatic activity; when
associated with A-536.
{ECO:0000269|PubMed:17320162}.
MUTAGEN 536 536 E->A: Abolishes enzymatic activity; when
associated with A-534.
{ECO:0000269|PubMed:17320162}.
CONFLICT 327 327 D -> N (in Ref. 1; AAC50806 and 8;
AAC51135). {ECO:0000305}.
CONFLICT 1285 1285 S -> F (in Ref. 1; AAC50806).
{ECO:0000305}.
CONFLICT 1352 1352 P -> L (in Ref. 9; AAK27839).
{ECO:0000305}.
CONFLICT 1391 1391 D -> G (in Ref. 1; AAC50806).
{ECO:0000305}.
HELIX 81 96 {ECO:0000244|PDB:2YQE}.
STRAND 106 109 {ECO:0000244|PDB:2YQE}.
HELIX 112 122 {ECO:0000244|PDB:2YQE}.
HELIX 125 130 {ECO:0000244|PDB:2YQE}.
TURN 131 133 {ECO:0000244|PDB:2YQE}.
HELIX 134 140 {ECO:0000244|PDB:2YQE}.
HELIX 149 159 {ECO:0000244|PDB:2YQE}.
HELIX 161 167 {ECO:0000244|PDB:2YQE}.
STRAND 318 320 {ECO:0000244|PDB:2E6R}.
HELIX 324 328 {ECO:0000244|PDB:2E6R}.
TURN 333 335 {ECO:0000244|PDB:2E6R}.
STRAND 341 346 {ECO:0000244|PDB:2E6R}.
HELIX 359 366 {ECO:0000244|PDB:2E6R}.
SEQUENCE 1539 AA; 174073 MW; E58DAE374E3BD7AA CRC64;
MEPGCDEFLP PPECPVFEPS WAEFQDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV
DNFRFTPRVQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERKIL DLYSLSKIVI
EEGGYEAICK DRRWARVAQR LHYPPGKNIG SLLRSHYERI IYPYEMFQSG ANHVQCNTHP
FDNEVKDKEY KPHSIPLRQS VQPSKFSSYS RRAKRLQPDP EPTEEDIEKH PELKKLQIYG
PGPKMMGLGL MAKDKDKTVH KKVTCPPTVT VKDEQSGGGN VSSTLLKQHL SLEPCTKTTM
QLRKNHSSAQ FIDSYICQVC SRGDEDDKLL FCDGCDDNYH IFCLLPPLPE IPRGIWRCPK
CILAECKQPP EAFGFEQATQ EYSLQSFGEM ADSFKSDYFN MPVHMVPTEL VEKEFWRLVS
SIEEDVTVEY GADIHSKEFG SGFPVSNSKQ NLSPEEKEYA TSGWNLNVMP VLDQSVLCHI
NADISGMKVP WLYVGMVFSA FCWHIEDHWS YSINYLHWGE PKTWYGVPSL AAEHLEEVMK
MLTPELFDSQ PDLLHQLVTL MNPNTLMSHG VPVVRTNQCA GEFVITFPRA YHSGFNQGYN
FAEAVNFCTA DWLPAGRQCI EHYRRLRRYC VFSHEELICK MAAFPETLDL NLAVAVHKEM
FIMVQEERRL RKALLEKGVT EAEREAFELL PDDERQCIKC KTTCFLSALA CYDCPDGLVC
LSHINDLCKC SSSRQYLRYR YTLDELPTML HKLKIRAESF DTWANKVRVA LEVEDGRKRS
FEELRALESE ARERRFPNSE LLQRLKNCLS EVEACIAQVL GLVSGQVARM DTPQLTLTEL
RVLLEQMGSL PCAMHQIGDV KDVLEQVEAY QAEAREALAT LPSSPGLLRS LLERGQQLGV
EVPEAHQLQQ QVEQAQWLDE VKQALAPSAH RGSLVIMQGL LVMGAKIASS PSVDKARAEL
QELLTIAERW EEKAHFCLEA RQKHPPATLE AIIRETENIP VHLPNIQALK EALTKAQAWI
ADVDEIQNGD HYPCLDDLEG LVAVGRDLPV GLEELRQLEL QVLTAHSWRE KASKTFLKKN
SCYTLLEVLC PCADAGSDST KRSRWMEKAL GLYQCDTELL GLSAQDLRDP GSVIVAFKEG
EQKEKEGILQ LRRTNSAKPS PLAPSLMASS PTSICVCGQV PAGVGVLQCD LCQDWFHGQC
VSVPHLLTSP KPSLTSSPLL AWWEWDTKFL CPLCMRSRRP RLETILALLV ALQRLPVRLP
EGEALQCLTE RAIGWQDRAR KALASEDVTA LLRQLAELRQ QLQAKPRPEE ASVYTSATAC
DPIREGSGNN ISKVQGLLEN GDSVTSPENM APGKGSDLEL LSSLLPQLTG PVLELPEAIR
APLEELMMEG DLLEVTLDEN HSIWQLLQAG QPPDLDRIRT LLELEKFEHQ GSRTRSRALE
RRRRRQKVDQ GRNVENLVQQ ELQSKRARSS GIMSQVGREE EHYQEKADRE NMFLTPSTDH
SPFLKGNQNS LQHKDSGSSA ACPSLMPLLQ LSYSDEQQL


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