MDC1_PANTR
ID MDC1_PANTR Reviewed; 2171 AA.
AC Q7YR40; Q1XHY6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Mediator of DNA damage checkpoint protein 1;
GN Name=MDC1;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT insertions/deletions as the major path to genomic divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
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-1922 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; BA000041; BAC78176.1; -; Genomic_DNA.
DR EMBL; AB210171; BAE92783.1; -; Genomic_DNA.
DR EMBL; AB210172; BAE92784.1; -; Genomic_DNA.
DR RefSeq; NP_001035841.1; NM_001042382.1.
DR AlphaFoldDB; Q7YR40; -.
DR SMR; Q7YR40; -.
DR STRING; 9598.ENSPTRP00000042596; -.
DR PaxDb; Q7YR40; -.
DR GeneID; 471959; -.
DR KEGG; ptr:471959; -.
DR CTD; 9656; -.
DR eggNOG; KOG2043; Eukaryota.
DR InParanoid; Q7YR40; -.
DR OrthoDB; 670424at2759; -.
DR Proteomes; UP000002277; 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; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
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..2171
FT /note="Mediator of DNA damage checkpoint protein 1"
FT /id="PRO_0000096319"
FT DOMAIN 54..105
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 1974..2052
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 2073..2164
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..220
FT /note="Interaction with the MRN complex"
FT /evidence="ECO:0000250"
FT REGION 145..568
FT /note="Required for nuclear localization (NLS1)"
FT /evidence="ECO:0000250"
FT REGION 185..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..1969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1692
FT /note="Interaction with the PRKDC complex"
FT /evidence="ECO:0000250"
FT REGION 1780..2171
FT /note="Required for nuclear localization (NLS2)"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..19
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1701..1718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1917..1961
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 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 301
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 378
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 404
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 449
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV9"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV9"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2M8"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 812
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1086
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV9"
FT MOD_RES 1239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1280
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1302
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1484
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1485
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1507
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1548
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1615
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV9"
FT MOD_RES 1630
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1649
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1671
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1690
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1712
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1746
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1753
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1779
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1793
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1857
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1882
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1902
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1940
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 2025
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 616
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 616
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1495
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1495
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1822
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1872
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1922
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1922
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CONFLICT 438
FT /note="R -> C (in Ref. 2; BAE92783/BAE92784)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="L -> Q (in Ref. 2; BAE92783/BAE92784)"
FT /evidence="ECO:0000305"
FT CONFLICT 1160..1161
FT /note="QG -> PV (in Ref. 2; BAE92783/BAE92784)"
FT /evidence="ECO:0000305"
FT CONFLICT 1427
FT /note="K -> E (in Ref. 2; BAE92783/BAE92784)"
FT /evidence="ECO:0000305"
FT CONFLICT 1530
FT /note="V -> D (in Ref. 2; BAE92783/BAE92784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2171 AA; 235388 MW; 8D8F30C9CDEF7114 CRC64;
MEDTQAIDWD VEEEEETEQS SESLRCNVEP VGRLHIFSGA HGPEKDFPLH LGKNVVGRMP
DCSVALPFPS ISKQHAEIEI LAWDKAPILR DCGSLNGTQI LRPPKVLSPG VSHRLRDQEL
ILFADLLCQY HRLDVSLPFV SRGPLTVEET PRVQGGTQPQ RLLLAEDSEE EVDFLSERRM
VKKSRTTSSS VIVPESDEEG HSPVLGGLGP PFAFNLNSDT DVEEGQQPAT EEASSAARRG
ATVEAKQSEA EVVTEIQLEK DQPLVKERDD DTKVKRGAEN GVVPAGVILE RSQPPGEDSD
TDVDDDSRPP GRPAEVHLER AQPFGFINSD TDAEEERIPA TPVVIPMKKR KIFHGVGTRG
PGAPGLAHLQ ESQAGSDTDV EEGKAPQAVP LEKSQASMVI NSDTDDEEEV SAALTLAHLK
ESQPAIWNRD AEEDMPQRVV LLQRSQTTTE RDSDTDVEEE ELPVENREAV LKDHTKIRAL
VRAHSEKDQP PFGDSDDSVE ADKSSPGIHL ERSQASTTVD INTQVEKEVP PGSAIIHIKK
HQVSVEGTNQ TDVKAVGGPA KLLVVSLEEA WPLHGDCETD AEEDTSLAAS AVADVRKSQL
PAEGDAGAEW AAAVLKQERA HEVGAQGGPP VAQVEQDLPI SRENLTDLVV DTDTLGESTQ
PQREGAQVPT GREREQHVGG TKDSEDNYGD SEDLDLQATQ CFLENQGLEA VQSMEDEPTQ
AFMLTPPQEL GPSHCSFQTT GTLDEPWEVL ATQPFCLRES EDSETQPFDT HLEAYGPCLS
PPRAIPGDQH PESPVHTEPM GIQGRGRQTV DKVMGIPKET AERVGPERGP LERETEKLLP
ERQTDVTGEE ELTKGKQDRE QKQLLARDTQ RQESDKNGES ASPERDRESL KVEIETSEEI
QEKQVQKQTL PSKAFEREVE RPVANRECDP AELEEKVPKV ILERDTQRGE PEGGSQDQKG
QASSPIPEPG VEAGDLPGPT SAPVTSGSQS GGRGSPVSPR RHQKGLLNCK MPPAEKASRI
RAAEKVSRGD QESPDACLPP TVPEAPAPPQ KPLNSQSQKH LAPPPLLSPL LPSIKPTVRK
TRQDGSQEAP EAPLSSELEP FHPKPKIRTR KSSRMTTFPA TSAAPEPHPS TSTAQPVTPK
PTSQATRSRT NRSSVKTPEQ GVPTAPELQP CTSTDQPVTS EPTSQVTRGR KSRSSVKTPE
TVVPTALELQ PSTSTDRPVT SEPTSHATRG RKNRSSVKTP EPVVPTAPEL QPSTSTDQPV
TSEPTYQATR GRKNRSSVKT PEPVVPTAPE LQPSTSTDQP VTPKPTSRTT RSRTNMSSVK
NPESTVPIAP ELPPSTSTEQ PVTPEPTSRA TRGRKNRSSG KTPETLVPTA PKLEPSTSTD
QPVTPEPTSQ ATRGRTNRSS VKTPETVVPT APELQLSTST DQAVTPKPTS RTTRSRTNMS
SVKNPESTVP IAPELPPSTS TEQPVTPEPT SRATRGRKNR SSGKTPETLV PTAPKLEPST
STDQPVTPEP TSQATRGRTN RSSVKTPETV VPTAPELQPS TSTDQPVTPE PTSQVTRGRT
DRSSVKTPET VVPTAPELQA SASTDQPVTS EPTSRTTRGR KNRSSVKTPE TVVPTAPELQ
PSTSTDQPVT PEPTSQATRG RTNRSSVKTP ESIVPIAPEL QPSTSRNQLV TPEPTSRATR
CRTNRSSVKT PEPVVPTAPE PHPTTSTDQP VTPKLTSRAT RRKTNRSSVK TPKPVEPAAS
DLEPFTPTDQ SVTPEAIAQG GQSKTLRSST VRAMPVPTTP EFQSPVTTDQ PISPEPITQP
SCIKRQRAAG NPGSLAAPID HKPCSAPLEP KSQASRNQRW GAVRAAESLT AIPEPASPQL
LETPIHASQI QKVEPAGRSR FTPELQPKAS QSRKRSLATM DSPPHQKQPQ RGEVSQKTVI
IKEEEEDTAE KPGKEEDVVT PKPGKRKRDQ AEEEPNRIPS RSLRRTKLNQ ESTAPKVLFT
GVVDARGERA VLALGGSLAG SAAEASHLVT DRIRRTVKFL CALGRGIPIL SLDWLHQSHK
AGFFLPPDEY VVTDPEQEKN FGFSLQDALS RARERRLLEG YEIYVTPGVQ PPPPQMGEII
SCCGGTYLPS MPRSYKPQRV VITCPQDFPH CSIPLRVGLP LLSPEFLLTG VLKQEAKPEA
FVLSPLEMSS T
