DPY21_CAEEL
ID DPY21_CAEEL Reviewed; 1641 AA.
AC Q9GRZ3;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Lysine-specific demethylase 9 {ECO:0000303|PubMed:28867287};
DE Short=KDM9 {ECO:0000303|PubMed:28867287};
DE EC=1.14.11.- {ECO:0000269|PubMed:28867287};
DE AltName: Full=Dosage compensation protein dpy-21 {ECO:0000305};
GN Name=dpy-21 {ECO:0000312|WormBase:Y59A8B.1a};
GN ORFNames=Y59A8B.1 {ECO:0000312|WormBase:Y59A8B.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=6537930; DOI=10.1093/genetics/106.1.29;
RA Meneely P.M., Wood W.B.;
RT "An autosomal gene that affects X chromosome expression and sex
RT determination in Caenorhabditis elegans.";
RL Genetics 106:29-44(1984).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=3779843; DOI=10.1016/0092-8674(86)90802-0;
RA Meyer B.J., Casson L.P.;
RT "Caenorhabditis elegans compensates for the difference in X chromosome
RT dosage between the sexes by regulating transcript levels.";
RL Cell 47:871-881(1986).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=3478715; DOI=10.1073/pnas.84.21.7600;
RA Donahue L.M., Quarantillo B.A., Wood W.B.;
RT "Molecular analysis of X chromosome dosage compensation in Caenorhabditis
RT elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7600-7604(1987).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SDC-3; DPY-27 AND DPY-26, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=14660541; DOI=10.1242/dev.00886;
RA Yonker S.A., Meyer B.J.;
RT "Recruitment of C. elegans dosage compensation proteins for gene-specific
RT versus chromosome-wide repression.";
RL Development 130:6519-6532(2003).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22393255; DOI=10.1128/mcb.06546-11;
RA Wells M.B., Snyder M.J., Custer L.M., Csankovszki G.;
RT "Caenorhabditis elegans dosage compensation regulates histone H4 chromatin
RT state on X chromosomes.";
RL Mol. Cell. Biol. 32:1710-1719(2012).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23028348; DOI=10.1371/journal.pgen.1002933;
RA Vielle A., Lang J., Dong Y., Ercan S., Kotwaliwale C., Rechtsteiner A.,
RA Appert A., Chen Q.B., Dose A., Egelhofer T., Kimura H., Stempor P.,
RA Dernburg A., Lieb J.D., Strome S., Ahringer J.;
RT "H4K20me1 contributes to downregulation of X-linked genes for C. elegans
RT dosage compensation.";
RL PLoS Genet. 8:E1002933-E1002933(2012).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SGK-1, AND DISRUPTION PHENOTYPE.
RX PubMed=23884442; DOI=10.1242/dev.094292;
RA Webster C.M., Wu L., Douglas D., Soukas A.A.;
RT "A non-canonical role for the C. elegans dosage compensation complex in
RT growth and metabolic regulation downstream of TOR complex 2.";
RL Development 140:3601-3612(2013).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26641248; DOI=10.1371/journal.pgen.1005698;
RA Kramer M., Kranz A.L., Su A., Winterkorn L.H., Albritton S.E., Ercan S.;
RT "Developmental dynamics of X-chromosome dosage compensation by the DCC and
RT H4K20me1 in C. elegans.";
RL PLoS Genet. 11:E1005698-E1005698(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1210-1617 IN COMPLEX WTH
RP ALPHA-KETOGLUTARATE AND IRON, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 1452-HIS--ASP-1454; HIS-1452 AND ASP-1454.
RX PubMed=28867287; DOI=10.1016/j.cell.2017.07.041;
RA Brejc K., Bian Q., Uzawa S., Wheeler B.S., Anderson E.C., King D.S.,
RA Kranzusch P.J., Preston C.G., Meyer B.J.;
RT "Dynamic Control of X Chromosome Conformation and Repression by a Histone
RT H4K20 Demethylase.";
RL Cell 171:E23-E23(2017).
CC -!- FUNCTION: Histone demethylase that specifically demethylates
CC dimethylated 'Lys-20' of histone H4 (H4K20me2), thereby modulating the
CC chromosome architecture (PubMed:28867287). Promotes chromatin
CC compaction by converting H4k20me2 to H4K20me1 leading to
CC transcriptional repression (PubMed:28867287). Required for X chromosome
CC dosage compensation by enriching H4K20me1 on X chromosomes and thereby
CC reducing X-linked gene transcription in hermaphrodites throughout
CC development (PubMed:14660541, PubMed:23028348, PubMed:3779843,
CC PubMed:3478715, PubMed:26641248, PubMed:22393255, PubMed:28867287). X
CC chromosome specificity is mediated by the recruitment through proteins
CC of the condensin-like dosage compensation complex (DCC)
CC (PubMed:14660541, PubMed:28867287). Required for the enrichment of
CC H4K20me1 on autosomes in meiotic germ cells leading to their compaction
CC in a DCC-independent mechanism (PubMed:28867287). Involved in 3-
CC dimensional chromosome organization by strengthening the borders of
CC topologically associating domains (PubMed:28867287). Involved in the
CC regulation of growth, fecundity and body fat metabolism downstream of
CC the TOR complex 2 and the protein kinase sgk-1 pathway
CC (PubMed:23884442). Also involved in male tail development
CC (PubMed:6537930). {ECO:0000269|PubMed:14660541,
CC ECO:0000269|PubMed:22393255, ECO:0000269|PubMed:23028348,
CC ECO:0000269|PubMed:23884442, ECO:0000269|PubMed:26641248,
CC ECO:0000269|PubMed:28867287, ECO:0000269|PubMed:3478715,
CC ECO:0000269|PubMed:3779843, ECO:0000269|PubMed:6537930}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:28867287};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:28867287};
CC -!- SUBUNIT: Interacts with the dosage compensation proteins dpy-27, dpy-26
CC and sdc-3; the interaction is probably involved in dpy-21 recruitment
CC to the X chromosomes in hermaphrodites (PubMed:14660541). Interacts
CC with the serine/threonine-protein kinase sgk-1 (PubMed:23884442).
CC {ECO:0000269|PubMed:14660541, ECO:0000269|PubMed:23884442}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14660541,
CC ECO:0000269|PubMed:28867287}. Chromosome {ECO:0000269|PubMed:14660541,
CC ECO:0000269|PubMed:28867287}. Note=Specifically localizes to the X
CC chromosomes around the 300- to 350-cell stage in hermaphrodite (XX) but
CC not in male (X0) embryos (PubMed:14660541, PubMed:28867287). Requires
CC sdc-2, sdc-3, dpy-26, dpy-27 and dpy-28 for X chromosome localization
CC (PubMed:14660541). Colocalizes with X chromosomes during interphase,
CC but is diffusely distributed during mitosis (PubMed:28867287).
CC Localizes to all autosomes but not to X chromosomes in pachytene nuclei
CC (PubMed:28867287). {ECO:0000269|PubMed:14660541,
CC ECO:0000269|PubMed:28867287}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, with highest
CC expression during embryogenesis. {ECO:0000269|PubMed:14660541}.
CC -!- DISRUPTION PHENOTYPE: Mutant hermaphrodites exhibit low larval
CC lethality, and survivors have a XX-specific shorter and stouter body
CC morphology and are egg-laying defective (PubMed:14660541,
CC PubMed:28867287). Leads to lethality in animals with three X
CC chromosomes and to intersex development in males with a sex-chromosome
CC to autosome (X:A) ratio higher than 0.65 (PubMed:6537930).
CC Overexpression of X-linked gene transcripts (PubMed:23028348,
CC PubMed:3478715, PubMed:26641248, PubMed:28867287). Increased binding of
CC the RNA Pol II large subunit ama-1 to promoters on the X chromosome
CC relative to autosomes (PubMed:26641248). Reduced levels of 'Lys-20'
CC monomethylation (H4K20me1) and an increase of 'Lys-20' trimethylation
CC (H4K20me3) and 'Lys-16' acetylation (H4K16ac) on histone H4 of
CC hermaphrodite X chromosomes (PubMed:23028348, PubMed:22393255,
CC PubMed:26641248, PubMed:28867287). Increased volume of the X chromosome
CC (PubMed:28867287). Suppresses the XO-specific lethality in a xol-1
CC mutant background, where the DCC is inappropriately activated
CC (PubMed:28867287). RNAi-mediated knockdown results in shortened
CC lifespan (PubMed:23884442). In a sinh-1 single or a rict-1;sgk-1 double
CC mutant background, suppresses the developmental delay phenotype
CC (PubMed:23884442). In a rict-1 mutant background, suppresses the
CC developmental delay, elevated body fat mass and low brood size, but
CC shortens the lifespan and decreases the body size (PubMed:23884442).
CC {ECO:0000269|PubMed:14660541, ECO:0000269|PubMed:22393255,
CC ECO:0000269|PubMed:23028348, ECO:0000269|PubMed:23884442,
CC ECO:0000269|PubMed:26641248, ECO:0000269|PubMed:28867287,
CC ECO:0000269|PubMed:3478715, ECO:0000269|PubMed:6537930}.
CC -!- SIMILARITY: Belongs to the round spermatid basic protein 1 family.
CC {ECO:0000305}.
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DR EMBL; BX284605; CAC14406.1; -; Genomic_DNA.
DR RefSeq; NP_001024266.1; NM_001029095.2.
DR PDB; 5UQD; X-ray; 1.80 A; A=1210-1617.
DR PDBsum; 5UQD; -.
DR AlphaFoldDB; Q9GRZ3; -.
DR SMR; Q9GRZ3; -.
DR STRING; 6239.Y59A8B.1a; -.
DR EPD; Q9GRZ3; -.
DR PaxDb; Q9GRZ3; -.
DR PeptideAtlas; Q9GRZ3; -.
DR EnsemblMetazoa; Y59A8B.1a.1; Y59A8B.1a.1; WBGene00001080.
DR GeneID; 180176; -.
DR KEGG; cel:CELE_Y59A8B.1; -.
DR UCSC; Y59A8B.1a; c. elegans.
DR CTD; 180176; -.
DR WormBase; Y59A8B.1a; CE26205; WBGene00001080; dpy-21.
DR eggNOG; KOG4425; Eukaryota.
DR GeneTree; ENSGT00390000001969; -.
DR HOGENOM; CLU_242819_0_0_1; -.
DR InParanoid; Q9GRZ3; -.
DR OMA; AMDLYEP; -.
DR OrthoDB; 1310522at2759; -.
DR PRO; PR:Q9GRZ3; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001080; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000805; C:X chromosome; IDA:WormBase.
DR GO; GO:0035575; F:histone H4-methyl-lysine-20 demethylase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR026306; RSBN1/Dpy-21.
DR PANTHER; PTHR13354; PTHR13354; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Coiled coil; Dioxygenase; Iron; Metal-binding;
KW Nucleus; Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1641
FT /note="Lysine-specific demethylase 9"
FT /id="PRO_0000439455"
FT DOMAIN 1431..1625
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 388..443
FT /evidence="ECO:0000255"
FT COILED 947..979
FT /evidence="ECO:0000255"
FT COILED 1122..1186
FT /evidence="ECO:0000255"
FT COMPBIAS 11..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..804
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..885
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1449
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0007744|PDB:5UQD"
FT BINDING 1452
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:28867287,
FT ECO:0007744|PDB:5UQD"
FT BINDING 1454
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:28867287,
FT ECO:0007744|PDB:5UQD"
FT BINDING 1585
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0007744|PDB:5UQD"
FT BINDING 1593
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:28867287,
FT ECO:0007744|PDB:5UQD"
FT MUTAGEN 1452..1454
FT /note="HAD->AAA: In y622; loss of demethylase activity.
FT Sex-specific enrichment of H4K20me1 is abolished from X
FT chromosomes in XX adults and embryos. Elevated X-linked
FT gene transcription relative to autosomes. Leads to
FT increased X chromosome volume. Suppresses the X0-specific
FT lethality in a xol-1(y9) mutant background, where the DCC
FT is inappropriately activated."
FT /evidence="ECO:0000269|PubMed:28867287"
FT MUTAGEN 1452
FT /note="H->A: In y607; sex-specific enrichment of H4K20me1
FT is abolished from X chromosomes in XX adults and embryos.
FT Elevated X-linked gene transcription relative to autosomes.
FT Leads to increased X chromosome volume. Results in less
FT distinct chromosome organization and reduced boundary
FT strength of topologically associating domains (TADs). Loss
FT of H4K20me1 enrichment on autosomes and decompaction in
FT male and hermaphrodite meiotic germ cells. Suppresses the
FT X0-specific lethality in a xol-1 mutant background, where
FT the DCC is inappropriately activated."
FT /evidence="ECO:0000269|PubMed:28867287"
FT MUTAGEN 1454
FT /note="D->A: In y618; sex-specific enrichment of H4K20me1
FT is abolished from X chromosomes in XX adults and embryos.
FT Elevated X-linked gene transcription relative to autosomes.
FT Leads to increased X chromosome volume. Suppresses the X0-
FT specific lethality in a xol-1 mutant background, where the
FT DCC is inappropriately activated."
FT /evidence="ECO:0000269|PubMed:28867287"
FT HELIX 1210..1222
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1232..1235
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1239..1242
FT /evidence="ECO:0007829|PDB:5UQD"
FT TURN 1244..1246
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1249..1254
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1255..1258
FT /evidence="ECO:0007829|PDB:5UQD"
FT TURN 1259..1261
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1264..1278
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1285..1287
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1289..1294
FT /evidence="ECO:0007829|PDB:5UQD"
FT TURN 1295..1299
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1303..1310
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1315..1319
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1327..1331
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1332..1342
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1347..1350
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1353..1358
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1371..1378
FT /evidence="ECO:0007829|PDB:5UQD"
FT TURN 1381..1383
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1384..1386
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1403..1405
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1408..1412
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1415..1418
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1443..1445
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1448..1452
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1498..1505
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1519..1521
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1524..1531
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1533..1535
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1536..1542
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1551..1553
FT /evidence="ECO:0007829|PDB:5UQD"
FT HELIX 1561..1568
FT /evidence="ECO:0007829|PDB:5UQD"
FT TURN 1569..1571
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1574..1580
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1584..1587
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1593..1597
FT /evidence="ECO:0007829|PDB:5UQD"
FT STRAND 1601..1608
FT /evidence="ECO:0007829|PDB:5UQD"
SQ SEQUENCE 1641 AA; 181928 MW; F6C38533AA158D1D CRC64;
MRSTTFDKNS GAPEEPRRPR GPRTPDGEPT EANERPCSSS SSLSNDSFVP APQGPQNGHT
SSSHDNDYSE YRPRRGPKTP PLPPPDEPVK QQQQQQPIVA PYSYYPTYGS STGYPYPYPT
MMMPQQGIPG PSQHPATPSY YIQHPPPPSM SNGAPYYPHM NPSPYYQPRP NYVTQPPAPI
IPPPQPPVMT ASAAAAAYRD RLPPPPPKPP MPDLRTKEPI GIRSWNGSGI PPPPILPPVA
CLSSTMSPGM LRSPVPRERF NSVESNGSFS LHPPPPVPPP AKKPLNMDVR ELLNGAHQTT
VESVKKDPPA PQPRPRPIPV PPTTSYNSSF CGLLPPPPVP PDLRASAASA AASPPMVQDA
SFSSVLTPKT KAPEKIPSPP ATVTSSTDSL EHMQRKRKKQ QETEEQEKAA KKAKRHQEER
ERQKIEAEKR KKAILEEAAK VTRPPAEKKP PVVVEETIRA VPFVFKQEMP LPFVLAAAAA
AAKEPETRPE PRPEPKQNGY HVKQAEPLQA EPPQNGYRLA AAQALQHEPR QASEPLQNVQ
PEPSKQASEL VQNGYAAPQE PRRATPPPEP LRNELPKHSD LLNVSKPSEP AEPPKPSDAP
REPEVAAAEA VIPEPSPAVS VEEPPRREER AASMAGIPPP PPTSSRHSPV PRREDRAEFM
ARSTPPAPGK DRKSLGGRMA MWRNKKNKTA SMVGPPEPKE LPAVVEVEAI VEPVVEDQPE
PVVSEELKPT EPEPVEPEPM EVEPVVAKEV VEEVVEEVVE TQEPWVPLSE CSRSSSLELL
AELPPPPRAS EPPPPPPPPV ATAPVPASME EDEIIDIETI DEITSTSTKK PEKVEKIKKA
PVVTKAALKM VGRPKKTPGR RRKKDRGASP SPSPSPPPPP ETTLTPIVLP RKKQRIEKKK
LTPPPPQQAP VTSHTPPPVE QLMSRKKQIM MEHSSLDHIQ FKLIEIELAA KRRKAEAAAK
AAAAVEQKDE KAEEVENRET PPGPSTSMRS SSLHTPNTSE EDEVIFVEPS TLEKPERRNG
TTEERVMTAD QRAMFDAKIE EARRSRMSTR DCSVVSTLGP VKSKASQRLH DIIEGKEELE
DSMDDPTNNN GTLAGILYPM RSERAESVSS NHRSEGAGGS MSLKHHLARK NELKEEANVA
RRSEILKAVV KRQREIGVPT TLMSKSAIEL VEEDEKERKN HKNNKTLSHP DYVRSKNEAE
KAEFHGKGGT MRITNRNLKM LTRQFDLPKM SSRFRKFVRI RRHPNGMATI ISCDYNQIKQ
HLGPNEMKHF ERQFVRLGFA ENNGVPLFAI GVMENAAEAL HDQFEWLAKN SPNTQVKVGS
LTNKQFIETM PMKKYYESAM ETLDMGTFRF GPLMSLSMVG TKNEEAGGNF KEMLDALNAA
PFLGPIMPWG DFSEVQGIKE DTSDDGPIFW VRPGEQMVPT DGKNRSTEPR HPLATRGNDR
RETAFNDRTN AHADQVREST EDDPTTTTTT TTTTSSSSSS SKSKKSAKSD PTFVKSTAAV
GVLQGIRNPD ANDDDEYYED ERKAVKEVIV FDAHDLHKVA HHLAMDLYEP PVSQCHRWVD
DAILNTMRRE GIRYAKLELH ENDMYFLPRN VIHQFRTVSA CSSVAWHVRL RHYYDVDQPA
SLSDPQFECD SDYSDDGDFD D
