MORC3_MOUSE
ID MORC3_MOUSE Reviewed; 942 AA.
AC F7BJB9; A6H605; Q4QQR6; Q6A0C2; Q8R0R0;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=MORC family CW-type zinc finger protein 3 {ECO:0000250|UniProtKB:Q14149};
DE AltName: Full=Nuclear matrix protein 2 {ECO:0000250|UniProtKB:Q14149};
DE AltName: Full=Zinc finger CW-type coiled-coil domain protein 3 {ECO:0000250|UniProtKB:Q14149};
GN Name=Morc3 {ECO:0000312|MGI:MGI:2136841};
GN Synonyms=Nxp2 {ECO:0000312|MGI:MGI:2136841},
GN Zcwcc3 {ECO:0000312|MGI:MGI:2136841};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:BAD32174.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Natural killer cell {ECO:0000312|EMBL:BAD32174.1};
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000040152,
RC ECO:0000312|Proteomes:UP000000589};
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 [3] {ECO:0000312|EMBL:AAH98072.1, ECO:0000312|EMBL:AAI45706.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH98072.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAI45706.1},
RC Embryonic germ cell {ECO:0000312|EMBL:AAH98072.1}, and
RC Retina {ECO:0000312|EMBL:AAH26506.1};
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17332504; DOI=10.1091/mbc.e06-08-0747;
RA Takahashi K., Yoshida N., Murakami N., Kawata K., Ishizaki H.,
RA Tanaka-Okamoto M., Miyoshi J., Zinn A.R., Shime H., Inoue N.;
RT "Dynamic regulation of p53 subnuclear localization and senescence by
RT MORC3.";
RL Mol. Biol. Cell 18:1701-1709(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=27188231; DOI=10.1038/srep25964;
RA Jadhav G., Teguh D., Kenny J., Tickner J., Xu J.;
RT "Morc3 mutant mice exhibit reduced cortical area and thickness, accompanied
RT by altered haematopoietic stem cells niche and bone cell differentiation.";
RL Sci. Rep. 6:25964-25964(2016).
RN [7] {ECO:0007744|PDB:5IX1, ECO:0007744|PDB:5IX2}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 7-456 IN COMPLEX WITH ZINC,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=27528681; DOI=10.1073/pnas.1609709113;
RA Li S., Yen L., Pastor W.A., Johnston J.B., Du J., Shew C.J., Liu W., Ho J.,
RA Stender B., Clark A.T., Burlingame A.L., Daxinger L., Patel D.J.,
RA Jacobsen S.E.;
RT "Mouse MORC3 is a GHKL ATPase that localizes to H3K4me3 marked chromatin.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E5108-E5116(2016).
CC -!- FUNCTION: Nuclear matrix protein which forms MORC3-NBs (nuclear bodies)
CC via an ATP-dependent mechanism and plays a role in innate immunity by
CC restricting different viruses through modulation of the IFN response.
CC Mechanistically, possesses a primary antiviral function through a
CC MORC3-regulated element that activates IFNB1, and this function is
CC guarded by a secondary IFN-repressing function. Sumoylated MORC3-NBs
CC associates with PML-NBs and recruits TP53 and SP100, thus regulating
CC TP53 activity (PubMed:17332504). Binds RNA in vitro. Histone
CC methylation reader which binds to non-methylated (H3K4me0),
CC monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated
CC (H3K4me3) 'Lys-4' on histone H3. The order of binding preference is
CC H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0. {ECO:0000250|UniProtKB:Q14149,
CC ECO:0000269|PubMed:17332504}.
CC -!- ACTIVITY REGULATION: Dimerization of the ATPase domain is strictly
CC required for the catalytic activity and binding to double-stranded DNA.
CC Disrupting the interface between ATPase and the CW domains releases
CC autoinhibition since the CW domain sterically impedes binding of the
CC ATPase domain to DNA. {ECO:0000250|UniProtKB:Q14149}.
CC -!- SUBUNIT: Homodimer. The sumoylated form interacts with PML (via SUMO-
CC interacting motif). Interacts with TP53. {ECO:0000269|PubMed:17332504}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17332504}. Nucleus matrix
CC {ECO:0000250|UniProtKB:Q14149}. Nucleus, PML body
CC {ECO:0000269|PubMed:17332504}. Chromosome
CC {ECO:0000269|PubMed:27528681}. Note=Also found in PML-independent
CC nuclear bodies. Localization to nuclear bodies is ATP-dependent.
CC {ECO:0000250|UniProtKB:Q14149}.
CC -!- DOMAIN: The CW-TYPE zinc finger mediates its binding to trimethylated
CC histone H3K4me3. {ECO:0000250|UniProtKB:Q14149}.
CC -!- PTM: Sumoylation is involved in interaction with PML and localization
CC to PML nuclear bodies. {ECO:0000250|UniProtKB:Q14149}.
CC -!- DISRUPTION PHENOTYPE: Lethality occurs at birth or within a day
CC thereafter, for unknown reasons. Embryos at 14.5 dpc are
CC morphologically indistinguishable from wild type (PubMed:17332504).
CC MORC3 deletion leads to increased osteoblast differentiation and
CC altered osteoblastic gene expression through up-regulation of IFN-
CC beta/STAT1 signaling pathway (PubMed:27188231).
CC {ECO:0000269|PubMed:17332504, ECO:0000269|PubMed:27188231}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32174.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK172896; BAD32174.1; ALT_INIT; mRNA.
DR EMBL; AC168220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC098072; AAH98072.1; -; mRNA.
DR EMBL; BC145705; AAI45706.1; -; mRNA.
DR EMBL; BC026506; AAH26506.1; -; mRNA.
DR CCDS; CCDS79490.1; -.
DR RefSeq; NP_001038994.2; NM_001045529.3.
DR PDB; 5IX1; X-ray; 2.60 A; A/B=7-456.
DR PDB; 5IX2; X-ray; 2.90 A; A/B=7-456.
DR PDBsum; 5IX1; -.
DR PDBsum; 5IX2; -.
DR AlphaFoldDB; F7BJB9; -.
DR SMR; F7BJB9; -.
DR IntAct; F7BJB9; 3.
DR STRING; 10090.ENSMUSP00000040152; -.
DR iPTMnet; F7BJB9; -.
DR PhosphoSitePlus; F7BJB9; -.
DR EPD; F7BJB9; -.
DR jPOST; F7BJB9; -.
DR MaxQB; F7BJB9; -.
DR PaxDb; F7BJB9; -.
DR PRIDE; F7BJB9; -.
DR ProteomicsDB; 252593; -.
DR Antibodypedia; 5016; 94 antibodies from 23 providers.
DR DNASU; 338467; -.
DR Ensembl; ENSMUST00000044068; ENSMUSP00000040152; ENSMUSG00000039456.
DR Ensembl; ENSMUST00000202261; ENSMUSP00000144369; ENSMUSG00000039456.
DR GeneID; 338467; -.
DR KEGG; mmu:338467; -.
DR UCSC; uc008aaa.2; mouse.
DR CTD; 23515; -.
DR MGI; MGI:2136841; Morc3.
DR VEuPathDB; HostDB:ENSMUSG00000039456; -.
DR eggNOG; KOG1845; Eukaryota.
DR GeneTree; ENSGT00940000160495; -.
DR InParanoid; F7BJB9; -.
DR OMA; LTMIVPD; -.
DR OrthoDB; 193855at2759; -.
DR PhylomeDB; F7BJB9; -.
DR TreeFam; TF329118; -.
DR BioGRID-ORCS; 338467; 7 hits in 65 CRISPR screens.
DR ChiTaRS; Morc3; mouse.
DR PRO; PR:F7BJB9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; F7BJB9; protein.
DR Bgee; ENSMUSG00000039456; Expressed in cleaving embryo and 262 other tissues.
DR ExpressionAtlas; F7BJB9; baseline and differential.
DR Genevisible; Q6A0C2; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; IDA:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; ISO:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:2000774; P:positive regulation of cellular senescence; ISO:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR045261; MORC_ATPase.
DR InterPro; IPR041006; Morc_S5.
DR InterPro; IPR011124; Znf_CW.
DR PANTHER; PTHR23336; PTHR23336; 1.
DR Pfam; PF17942; Morc6_S5; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Coiled coil; Immunity; Innate immunity;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..942
FT /note="MORC family CW-type zinc finger protein 3"
FT /id="PRO_0000435141"
FT ZN_FING 404..454
FT /note="CW-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT REGION 326..353
FT /note="Nuclear matrix binding"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT REGION 503..594
FT /note="RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT REGION 623..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 696..874
FT /evidence="ECO:0000255"
FT COMPBIAS 624..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454,
FT ECO:0000269|PubMed:27528681"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454,
FT ECO:0000269|PubMed:27528681"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454,
FT ECO:0000269|PubMed:27528681"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454,
FT ECO:0000269|PubMed:27528681"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 558
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 604
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 604
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 657
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 657
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 658
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 658
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 743
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 743
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 797
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CROSSLNK 797
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14149"
FT CONFLICT 134
FT /note="Y -> H (in Ref. 3; AAH98072)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="G -> S (in Ref. 3; AAI45706)"
FT /evidence="ECO:0000305"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:5IX1"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:5IX1"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:5IX1"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:5IX1"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5IX1"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 112..131
FT /evidence="ECO:0007829|PDB:5IX1"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5IX1"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:5IX1"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 190..201
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:5IX1"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:5IX1"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:5IX1"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:5IX2"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 299..308
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:5IX1"
FT HELIX 365..385
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:5IX1"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:5IX1"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:5IX2"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:5IX1"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:5IX1"
SQ SEQUENCE 942 AA; 106522 MW; 29EFFF22B7B24C94 CRC64;
MAAQPPTGIR LSALCPKFLH TNSTSHTWPF SAVAELIDNA YDPDVNAKQI WIDKTVISDH
ICLTFTDNGN GMTADKLHKM LSFGFSDKVT MNGHVPVGLY GNGFKSGSMR LGKDAMVFTK
NGETMSVGFL SQTYLEVIKA EHVVVPIVTF NKHRQMINLT ESKASLAAIL EHSLFSTEQK
LLAELNAIMG KKGTRIIIWN LRSYKNATEF DFEKDKYDIR IPEDLDETAG RKGYKKQERM
DQIAPESDYS LRAYCSILYL KPRMQIIIRG QKVKTQLVSK SLAYIERDVY RPKFLTRTVR
ITFGFNCRNK DHYGIMMYHK NRLIKAYEKV GCQLKANNMG VGVVGIIECN FLKPTHNKQD
FDYTNEYRLT ILALGEKLND YWNEMKVKKN AEYPVNLPVE DIQKRPDQTW VQCDACLKWR
KLPDGIDQLP EKWYCSNNPD PQFRNCEVPE EPEDEDLVHP TYEKTYKKTS KERFRIRQPE
ILPRILPQIN PELLYQTSVS SQSFSPVKES VPRPHLSEVT SPFAARIINL NLASPASEPE
NSSMKRKLGV HSSILNAKTR RLSNPPVENS SYKNDDDEDV IILEENSTPK PAVDLEVKSD
IEVKSEQSHT EQSGIHVDLV SSPKPCVQAS STSTSTSRSD PGITVSTQTD APGLTVKKEE
SMEEDMGVRN GTATLSCVGT EAKVQETSAE SVDATSHQLQ ELRSELLVVT QERDDYKRQC
QMFTDQIQVL QQRLLEMNDK CVKKEKCHQS TETDAVFLLD SVNGQAESLD HLGSQYQQAL
QEIERLKRQC SALQQVKSEC SQASCTESKS EVDEMAVQLD DVFRQLDKCT IERDQYKNEV
QLLEIEKSHI HSQCEELQTE VEQLKSTGQQ AAADGSTASN AEEPVSYVDG ESLKLRSLRV
NVGQLLAMIV PDLDLQQVNY DVDVVDEILG QVVEQMSEIS ST
