KDM7_CAEEL
ID KDM7_CAEEL Reviewed; 910 AA.
AC Q9GYI0; Q9BI67;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Lysine-specific demethylase 7 homolog;
DE Short=ceKDM7A;
DE EC=1.14.11.-;
DE AltName: Full=JmjC domain-containing protein 1.2;
DE AltName: Full=PHD finger protein 8 homolog;
DE AltName: Full=PHF8 homolog;
GN Name=jmjd-1.2; ORFNames=F29B9.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, AND DOMAIN PHD-FINGER.
RX PubMed=20567262; DOI=10.1038/cr.2010.84;
RA Lin H., Wang Y., Wang Y., Tian F., Pu P., Yu Y., Mao H., Yang Y., Wang P.,
RA Hu L., Lin Y., Liu Y., Xu Y., Chen C.D.;
RT "Coordinated regulation of active and repressive histone methylations by a
RT dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans.";
RL Cell Res. 20:899-907(2010).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20346720; DOI=10.1016/j.molcel.2010.03.002;
RA Kleine-Kohlbrecher D., Christensen J., Vandamme J., Abarrategui I., Bak M.,
RA Tommerup N., Shi X., Gozani O., Rappsilber J., Salcini A.E., Helin K.;
RT "A functional link between the histone demethylase PHF8 and the
RT transcription factor ZNF711 in X-linked mental retardation.";
RL Mol. Cell 38:165-178(2010).
RN [4]
RP FUNCTION.
RX PubMed=26476455; DOI=10.1093/nar/gkv1063;
RA Vandamme J., Sidoli S., Mariani L., Friis C., Christensen J., Helin K.,
RA Jensen O.N., Salcini A.E.;
RT "H3K23me2 is a new heterochromatic mark in Caenorhabditis elegans.";
RL Nucleic Acids Res. 43:9694-9710(2015).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-508.
RX PubMed=27133168; DOI=10.1016/j.cell.2016.04.012;
RA Merkwirth C., Jovaisaite V., Durieux J., Matilainen O., Jordan S.D.,
RA Quiros P.M., Steffen K.K., Williams E.G., Mouchiroud L., Tronnes S.U.,
RA Murillo V., Wolff S.C., Shaw R.J., Auwerx J., Dillin A.;
RT "Two Conserved Histone Demethylases Regulate Mitochondrial Stress-Induced
RT Longevity.";
RL Cell 165:1209-1223(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 205-719 IN COMPLEX WITH ZINC; IRON
RP AND METHYLATED H3 PEPTIDES, ZINC-BINDING, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, DOMAIN PHD-FINGER, AND MUTAGENESIS OF ASP-209; TRP-254; ASP-258;
RP GLN-261; TRP-263; ASP-402; GLN-409; THR-411; SER-437; PHE-495; ASP-510;
RP TYR-518; GLU-544; ASN-594 AND 622-GLU--PHE-624.
RX PubMed=20567261; DOI=10.1038/cr.2010.86;
RA Yang Y., Hu L., Wang P., Hou H., Lin Y., Liu Y., Li Z., Gong R., Feng X.,
RA Zhou L., Zhang W., Dong Y., Yang H., Lin H., Wang Y., Chen C.D., Xu Y.;
RT "Structural insights into a dual-specificity histone demethylase ceKDM7A
RT from Caenorhabditis elegans.";
RL Cell Res. 20:886-898(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 201-724 IN COMPLEX WITH
RP SUBSTRATE; INHIBITOR; IRON AND ZINC, AND ACTIVITY REGULATION.
RX PubMed=21251613; DOI=10.1016/j.ccr.2010.12.014;
RA Xu W., Yang H., Liu Y., Yang Y., Wang P., Kim S.H., Ito S., Yang C.,
RA Wang P., Xiao M.T., Liu L.X., Jiang W.Q., Liu J., Zhang J.Y., Wang B.,
RA Frye S., Zhang Y., Xu Y.H., Lei Q.Y., Guan K.L., Zhao S.M., Xiong Y.;
RT "Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of alpha-
RT ketoglutarate-dependent dioxygenases.";
RL Cancer Cell 19:17-30(2011).
CC -!- FUNCTION: Histone demethylase required for nervous system development
CC (PubMed:20346720). Specifically demethylates dimethylated 'Lys-9',
CC 'Lys-23' and 'Lys-27' (H3K9me2, H3K23me2 and H3K27me2, respectively) of
CC histone H3, thereby playing a central role in histone code
CC (PubMed:20346720, PubMed:21251613, PubMed:20567262, PubMed:26476455).
CC Promotes mitochondrial stress-induced longevity (PubMed:27133168).
CC {ECO:0000269|PubMed:20346720, ECO:0000269|PubMed:20567261,
CC ECO:0000269|PubMed:20567262}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:20567261};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:20567261};
CC -!- ACTIVITY REGULATION: Competitively inhibited by 2-hydroxyglutarate.
CC {ECO:0000269|PubMed:21251613}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20346720}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q9GYI0-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9GYI0-2; Sequence=VSP_039912;
CC -!- TISSUE SPECIFICITY: Mainly expressed in neurons. Also weakly expressed
CC in some muscle, intestinal and hypodermal cells.
CC {ECO:0000269|PubMed:20346720}.
CC -!- DOMAIN: The PHD-type zinc finger mediates binding to H3K4me3.
CC {ECO:0000269|PubMed:20567261, ECO:0000269|PubMed:20567262}.
CC -!- DISRUPTION PHENOTYPE: Impaired locomotion (PubMed:20346720). While
CC wild-type animals move by alternating dorsal and ventral flexions along
CC the body length, producing a regular sinusoidal track on bacteria, the
CC track pattern left by mutants is irregular, with increased wavelength
CC (distance between successive peaks of a wave) but unchanged amplitude
CC of the wave (PubMed:20346720). An increase of H3K9me2 and H3K27me2
CC levels is observed (PubMed:20346720). RNAi-mediated knockdown
CC suppresses mitochondrial stress-mediated longevity (PubMed:27133168).
CC {ECO:0000269|PubMed:20346720, ECO:0000269|PubMed:27133168}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000305}.
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DR EMBL; FO081255; CCD70224.1; -; Genomic_DNA.
DR EMBL; FO081255; CCD70225.1; -; Genomic_DNA.
DR PIR; T29935; T29935.
DR RefSeq; NP_500610.1; NM_068209.4. [Q9GYI0-1]
DR RefSeq; NP_500611.1; NM_068210.3. [Q9GYI0-2]
DR PDB; 3N9L; X-ray; 2.80 A; A=201-724.
DR PDB; 3N9M; X-ray; 2.49 A; A/C=201-724.
DR PDB; 3N9N; X-ray; 2.30 A; A=201-724.
DR PDB; 3N9O; X-ray; 2.31 A; A=201-724.
DR PDB; 3N9P; X-ray; 2.39 A; A=201-724.
DR PDB; 3N9Q; X-ray; 2.30 A; A=201-724.
DR PDB; 3PUQ; X-ray; 2.25 A; A/C=201-724.
DR PDB; 3PUR; X-ray; 2.10 A; A/C=201-724.
DR PDBsum; 3N9L; -.
DR PDBsum; 3N9M; -.
DR PDBsum; 3N9N; -.
DR PDBsum; 3N9O; -.
DR PDBsum; 3N9P; -.
DR PDBsum; 3N9Q; -.
DR PDBsum; 3PUQ; -.
DR PDBsum; 3PUR; -.
DR AlphaFoldDB; Q9GYI0; -.
DR SMR; Q9GYI0; -.
DR IntAct; Q9GYI0; 2.
DR STRING; 6239.F29B9.2c; -.
DR EPD; Q9GYI0; -.
DR PaxDb; Q9GYI0; -.
DR PeptideAtlas; Q9GYI0; -.
DR EnsemblMetazoa; F29B9.2a.1; F29B9.2a.1; WBGene00017920. [Q9GYI0-1]
DR EnsemblMetazoa; F29B9.2b.1; F29B9.2b.1; WBGene00017920. [Q9GYI0-2]
DR GeneID; 177232; -.
DR UCSC; F29B9.2a; c. elegans.
DR CTD; 177232; -.
DR WormBase; F29B9.2a; CE09781; WBGene00017920; jmjd-1.2. [Q9GYI0-1]
DR WormBase; F29B9.2b; CE27145; WBGene00017920; jmjd-1.2. [Q9GYI0-2]
DR eggNOG; KOG1633; Eukaryota.
DR InParanoid; Q9GYI0; -.
DR PhylomeDB; Q9GYI0; -.
DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-CEL-3214842; HDMs demethylate histones.
DR EvolutionaryTrace; Q9GYI0; -.
DR PRO; PR:Q9GYI0; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00017920; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q9GYI0; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0042393; F:histone binding; IDA:WormBase.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IDA:WormBase.
DR GO; GO:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071557; P:histone H3-K27 demethylation; IDA:WormBase.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IDA:WormBase.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Dioxygenase; Iron;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..910
FT /note="Lysine-specific demethylase 7 homolog"
FT /id="PRO_0000399813"
FT DOMAIN 441..612
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 208..290
FT /note="PHD-type"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 505..510
FT /ligand="substrate"
FT BINDING 508
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538,
FT ECO:0000269|PubMed:20567261, ECO:0000269|PubMed:21251613"
FT BINDING 510
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538,
FT ECO:0000269|PubMed:20567261, ECO:0000269|PubMed:21251613"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21251613"
FT BINDING 525
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21251613"
FT BINDING 580
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538,
FT ECO:0000269|PubMed:20567261, ECO:0000269|PubMed:21251613"
FT BINDING 580
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21251613"
FT VAR_SEQ 86..98
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_039912"
FT MUTAGEN 209
FT /note="D->A: Abolishes binding to H3K4me3."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 254
FT /note="W->A: Abolishes binding to H3K4me3."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 258
FT /note="D->A: Abolishes binding to H3K4me3."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 261
FT /note="Q->A: Abolishes binding to H3K4me3."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 263
FT /note="W->A: Abolishes binding to H3K4me3."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 402
FT /note="D->A: Impairs histone methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 409
FT /note="Q->A: Impairs histone methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 411
FT /note="T->A: Impairs histone methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 437
FT /note="S->A: Abolishes histone methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 495
FT /note="F->A: Strongly impairs histone methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 508
FT /note="H->A: Fails to increase longevity."
FT /evidence="ECO:0000269|PubMed:27133168"
FT MUTAGEN 510
FT /note="D->A: Strongly impairs histone methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 518
FT /note="Y->A: Strongly impairs histone methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 544
FT /note="E->A: Impairs histone methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 594
FT /note="N->A: Strongly impairs histone methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:20567261"
FT MUTAGEN 622..624
FT /note="EKF->AAA: Abolishes histone methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:20567261"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3N9N"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:3PUR"
FT TURN 244..249
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:3PUR"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3PUR"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3PUR"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:3PUR"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 349..358
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 388..395
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:3PUR"
FT TURN 406..409
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 454..459
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 461..465
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 474..478
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 493..499
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 515..530
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 534..545
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 553..556
FT /evidence="ECO:0007829|PDB:3PUR"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:3PUR"
FT STRAND 579..595
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 598..600
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 601..617
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:3N9N"
FT HELIX 629..639
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 641..650
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 656..683
FT /evidence="ECO:0007829|PDB:3PUR"
FT HELIX 693..715
FT /evidence="ECO:0007829|PDB:3PUR"
SQ SEQUENCE 910 AA; 104672 MW; 8AE17DC5860EDFA5 CRC64;
MDGNDINIQK NEFSRDQSAL LMMDQHSDHK NHESAIGEPG MSYTASQPAL SSTEHQTPLV
SEASVAAPQN HLNGNSHESV SEMDRNSVDF AIESVLMKAR AYNKMGAPKD PRRKQHNPKS
EPKIEPHVTD SSDNQAAMSN KMEAEAPKME SNQNYVSNGS EPPFRFVSIS NFDEMKTKKK
EVQEELKLEV DSDSEEDDVP EQKTPKESDR CGGCGKFTHE DDLIALEEEK KKEKEKPLMS
KKKSHHHKKN DFQWIGCDSC QTWYHFLCSG LEQFEYYLYE KFFCPKCVPH TGHSIRYKVV
APHRYRWYSP NEKHLGIEVG SKTWIEDFIT RENTVPSPTD DEVCIVEDGY EFRREFEKLG
GADNWGKVFM VKDMDGLNMT MPKPGFDLED VVKIMGSDYE VDTIDVYNQS TYSMKLDTFR
KLFRDTKNRP LLYNFLSLEF SDNNEMKEIA KPPRFVQEIS MVNRLWPDVS GAEYIKLLQR
EEYLPEDQRP KVEQFCLAGM AGSYTDFHVD FGGSSVYYHI LKGEKIFYIA APTEQNFAAY
QAHETSPDTT TWFGDIANGA VKRVVIKEGQ TLLIPAGWIH AVLTPVDSLV FGGNFLHLGN
LEMQMRVYHL ENAIRKEIRS EEKFYFPNFE LLHWMYMRNV LLEKITEANQ EGSDMREQEK
NIWTASQIMK AEMERWMDRE LRLGPEKNAI LPTDDKNKIM ISVRKQIEIQ TKIQNAKNKP
MGLKQKRKSR ESAERDDEDY CPSSSTAYKK KYTKKAKKDN DDAPKVKKAK KEEVPEEKVP
VPEAAGPSEV TAPLTIKIGM GPTEDQKGVV QIFNNQCTSS GRKVKLNQNV ADYCGSHLEA
RVEEIPEKAT KSFRELDNEL ERCEAVHSGE KIKKVKEPKP PKQPKEKKEK PPPKKKEMSS
RDRLMKKLKM
