MDC1_MACMU
ID MDC1_MACMU Reviewed; 2173 AA.
AC Q5TM68;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Mediator of DNA damage checkpoint protein 1;
GN Name=MDC1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15269276; DOI=10.1093/molbev/msh216;
RA Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT "Rhesus macaque class I duplicon structures, organization, and evolution
RT within the alpha block of the major histocompatibility complex.";
RL Mol. Biol. Evol. 21:2079-2091(2004).
CC -!- FUNCTION: Required for checkpoint mediated cell cycle arrest in
CC response to DNA damage within both the S phase and G2/M phases of the
CC cell cycle. May serve as a scaffold for the recruitment of DNA repair
CC and signal transduction proteins to discrete foci of DNA damage marked
CC by 'Ser-139' phosphorylation of histone H2AX. Also required for
CC downstream events subsequent to the recruitment of these proteins.
CC These include phosphorylation and activation of the ATM, CHEK1 and
CC CHEK2 kinases, and stabilization of TP53 and apoptosis. ATM and CHEK2
CC may also be activated independently by a parallel pathway mediated by
CC TP53BP1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with several proteins involved in the DNA
CC damage response, although not all these interactions may be direct.
CC Interacts with H2AX, which requires phosphorylation of H2AX. Interacts
CC with the MRN complex, composed of MRE11, RAD50, and NBN. Interacts with
CC CHEK2, which requires ATM-mediated phosphorylation within the FHA
CC domain of CHEK2. Interacts constitutively with the BRCA1-BARD1 complex,
CC SMC1A and TP53BP1. Interacts with ATM and FANCD2, and these
CC interactions are reduced upon DNA damage. Also interacts with the PRKDC
CC complex, composed of XRCC6/KU70, XRCC5/KU80 and PRKDC/XRCC7. This
CC interaction may be required for PRKDC autophosphorylation, which is
CC essential for DNA double strand break (DSB) repair. When phosphorylated
CC by ATM, interacts with RNF8 (via FHA domain). Interacts with CEP164.
CC When phosphorylated, interacts with APTX (via FHA-like domain) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Note=Associated with chromatin. Relocalizes to discrete nuclear foci
CC following DNA damage, this requires phosphorylation of H2AX.
CC Colocalizes with APTX at sites of DNA double-strand breaks (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: Tandemly repeated BRCT domains are characteristic of proteins
CC involved in DNA damage signaling. In MDC1, these repeats are required
CC for localization to chromatin which flanks sites of DNA damage marked
CC by 'Ser-139' phosphorylation of H2AX (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated upon exposure to ionizing radiation (IR),
CC ultraviolet radiation (UV), and hydroxyurea (HU). Phosphorylation in
CC response to IR requires ATM, NBN, and possibly CHEK2. Also
CC phosphorylated during the G2/M phase of the cell cycle and during
CC activation of the mitotic spindle checkpoint. Phosphorylation at Thr-4
CC by ATM stabilizes and enhances homodimerization via the FHA domain (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Sumoylation at Lys-1924 by PIAS4 following DNA damage promotes
CC ubiquitin-mediated degradation. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by RNF4, leading to proteasomal degradation;
CC undergoes 'Lys-48'-linked polyubiquitination. {ECO:0000250}.
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DR EMBL; AB128049; BAD69758.1; -; Genomic_DNA.
DR RefSeq; NP_001108419.1; NM_001114947.1.
DR AlphaFoldDB; Q5TM68; -.
DR SMR; Q5TM68; -.
DR STRING; 9544.ENSMMUP00000031201; -.
DR PRIDE; Q5TM68; -.
DR GeneID; 712318; -.
DR KEGG; mcc:712318; -.
DR CTD; 9656; -.
DR eggNOG; KOG2043; Eukaryota.
DR HOGENOM; CLU_294520_0_0_1; -.
DR InParanoid; Q5TM68; -.
DR OrthoDB; 670424at2759; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF16770; RTT107_BRCT_5; 1.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52113; SSF52113; 2.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 3: Inferred from homology;
KW Acetylation; Cell cycle; Chromosome; DNA damage; DNA repair;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation.
FT CHAIN 1..2173
FT /note="Mediator of DNA damage checkpoint protein 1"
FT /id="PRO_0000096317"
FT DOMAIN 54..105
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 1976..2054
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 2075..2166
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..150
FT /note="Interaction with CHEK2"
FT /evidence="ECO:0000250"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..222
FT /note="Interaction with the MRN complex"
FT /evidence="ECO:0000250"
FT REGION 145..570
FT /note="Required for nuclear localization (NLS1)"
FT /evidence="ECO:0000250"
FT REGION 193..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..1770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1694
FT /note="Interaction with the PRKDC complex"
FT /evidence="ECO:0000250"
FT REGION 1782..2173
FT /note="Required for nuclear localization (NLS2)"
FT /evidence="ECO:0000250"
FT REGION 1809..1971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1754..1770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1919..1963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2M8"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 380
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 451
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV9"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV9"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 525
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2M8"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV9"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 814
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 957
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1088
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV9"
FT MOD_RES 1241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1304
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1486
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1509
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1550
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1617
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV9"
FT MOD_RES 1632
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1651
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1673
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1692
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1714
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1748
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1755
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1765
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1781
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1884
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1904
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1942
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 2027
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 618
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 618
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1824
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1874
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1924
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1924
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
SQ SEQUENCE 2173 AA; 235118 MW; 13C5F1CD2073477E CRC64;
MEDTQAIDWD VEEEEETEQS SESLRCNVEP VGRLHIFSGA HGPEKDFPLH LGKNVVGRMP
DCSVALPFPS ISKQHAEIEI LAWDKAPILR DCGSLNGTQI LRPPKVLSPG VSHRLRDQEL
ILFADLLCQY HRLDVSLPFV SRGPLTVEET PRVQGGTQPQ RLLLAEDSEE EVDFLSERHV
VKKSRTTSSP VAMIVPESDE EGHSPVLGGP GPPFAFNLNS DTDAEEGQQS ATEEASSAAR
RGATIEAEQS EAEVVTEIQL EKDQPSVKER DNDTKVKRGA GNGVVPAGMI LERSQPPGED
SDTDVDDDSR PPGRPAEVHL ERAQPFGFID SDTDAEEEGI PATPVVVPMK KRKIFHGVGT
RGPGAPGLSH LQESQAGSDT DVEEGKAPQA VPLEKSQASM VINSDTDDEE EVSAALTLAR
LKESQPAVWN RDAEEDMAHH AVLLQRSQTT TGRDSDTDVE EEELPVENKQ TVPKAHTKIR
ALVRAHSEKD QPPFGDSDDS VEADKSSPGI HLERSQASIT VDINTQVEEE VPPGSAIVHM
KKHQVSMEGT NQTDVKADGG PAKLLVVSLE EASPPHGDCE IDAEEGTSLA ASAVADVRKS
QLPAEGDAGA EWTAACLKQE RAYEVGAQGG SPVAQVEQDL PTSRENLTDL VVDTDTPGES
TQPQREGAQV PTGREREQHV GRTKDSEDNC DDSEDPDLQA TQCFLENQGL EAVQSMEDEP
TQAFMLTPPQ ELGSSHCSFQ TTGTLDEPWE VLATQPFCLR ESEDSETQPF DTHLEAYGPC
LSPPRAIPGD QHPESPVHTE PMGIQGRGRQ TVDKGMGIPK ETAERVGPER GPLERETEKL
LPERQTDVTG EEELTRGIQD REQKQLLARD TQRQESDKNG ESASPERDRE SLKVEIETSK
EIQGKQVQKQ TLPSKAFERE VERPVADREC EPAELEEKVP KVILERDAQR GEPKGGSQDQ
KGQASSPTSE PGVGAGDLPG PTSAPVPSGS QSGGRGSPVS PRRHQKGLLN CKMPPTEKAS
RIGAAEKASR GDQESPDACL PPTVPEASAP PQKPLNSQSQ KHLAPQPLLS PLSPSIEPTI
RKTGQDRSQE APETPLSSEL EPFHPKPKII TRKSSRMTPF PATSAAPEPH PSTSTAQPVT
PKPTSQATRS RTNRSSVKTP EPVVPTVPEL QPSTSTDQPV ASEPTSQATR GRKNRSSVKT
PEAVVPTALE LHPSNSTDQP VTPKPTSEAI RSRTNRSSVK TPEAVVPTAL ELHPSNSTDQ
PVTPKPTSEA IRSRTNRSSV KTPEPVVPTV PELQPSTSTD QPVTSEPTSQ ATRGRTNRSS
VKTPEPVVPT VPELQPSTST DQPVASEPTS QATRGRKNRS SVKTPEAVVP TALELHPSNS
TDQPVTPKPT SRTTRSRTNM SSVKTPESTV PIAPELPPST STEQPVITEP TYQPTRGRKN
RSSVKTPETV VATAPKLQSS TSTDQPITPE PTSQATRGRT NRSSVKSPET VLRTAPELQP
STSTHQPVTA KHTSQATRGR TNRSSVKTPE PVVSTAPELQ PSTSTHQPIT PEPTSQATRG
RTDRTSVKTP KIVVPTVPEL QASTSTDQPV TSEPTSRTTR GRKNRSSVKT PETVVPTAPE
PHPTTSTDQP ITPKPTSRAT RGRTNRSSVK TPELIVPIAP EFHPSTSRSQ LVTPEPTSRA
TRGRKNRSSV KTPEPAVPTA PELHPTTSTD QPVTPKPTSR ATRGRTNRSS VKTPEPVEPA
ASDLEPFTPT DQPVTPEAIP QGSQSKTLRS STVSAMLIPT TPEFQSPVTT DQPISPEPIP
QASCIKRQRA TGNPGSLTAP IDHKPCSAPL EPKSRPSRNQ RWGAVRADES LTAIPEPASP
QLLDIPTHAS QIQKVEPAGR SRFTPELQPK ASQSRKRSLA IMDSPPHQKQ PQRGEVSQKT
VIIKEEEEDT AEKPGKEEDV MTPKPGKRKR DQAEEEPNRI PNRSLRRTKL NQESTAPKVL
FTGVVDAQGE RAVLALGGSL AGSAAEASHL VTDRIRRTVK FLCALGRGIP ILSLDWLHQS
RKAGCFLPPD EYVVTDPEQE KNFGFSLQDA LSRARERRLL EGYEIYVTPG VQPPPPQMGE
IISCCGGTYL PSMPRSYKPQ RVVITCPQDF PRCSVPLRVG LPLLSPEFLL TGVLKQEAKP
EAFVLSPLEM SST
