PARP1_CHICK
ID PARP1_CHICK Reviewed; 1011 AA.
AC P26446;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Poly [ADP-ribose] polymerase 1;
DE Short=PARP-1;
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 1;
DE Short=ARTD1;
DE AltName: Full=DNA ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 1;
DE Short=ADPRT 1;
DE AltName: Full=Poly[ADP-ribose] synthase 1;
DE AltName: Full=Protein poly-ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
GN Name=PARP1; Synonyms=ADPRT;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oviduct;
RX PubMed=1840535; DOI=10.1016/0378-1119(91)90073-k;
RA Ittel M.-E., Garnier J.-M., Jeltsch J.-M., Niedergang C.;
RT "Chicken poly(ADP-ribose) synthetase: complete deduced amino acid sequence
RT and comparison with mammalian enzyme sequences.";
RL Gene 102:157-164(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 659-1011.
RX PubMed=8755499; DOI=10.1073/pnas.93.15.7481;
RA Ruf A., Mennissier-de Murcia J., de Murcia G.M., Schulz G.E.;
RT "Structure of the catalytic fragment of poly(AD-ribose) polymerase from
RT chicken.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7481-7485(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 659-1011, AND SEQUENCE REVISION TO
RP 895.
RX PubMed=9521710; DOI=10.1021/bi972383s;
RA Ruf A., de Murcia G.M., Schulz G.E.;
RT "Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from
RT crystal structures and homology modeling.";
RL Biochemistry 37:3893-3900(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 659-1011.
RX PubMed=9571033; DOI=10.1006/jmbi.1998.1673;
RA Ruf A., Rolli V., de Murcia G.M., Schulz G.E.;
RT "The mechanism of the elongation and branching reaction of poly(ADP-ribose)
RT polymerase as derived from crystal structures and mutagenesis.";
RL J. Mol. Biol. 278:57-65(1998).
CC -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-
CC ribosylation of proteins and plays a key role in DNA repair. Mediates
CC glutamate, aspartate, serine or tyrosine ADP-ribosylation of proteins:
CC the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor
CC carboxyl group of target residues and further ADP-ribosyl groups are
CC transferred to the 2'-position of the terminal adenosine moiety,
CC building up a polymer with an average chain length of 20-30 units.
CC Serine ADP-ribosylation of proteins constitutes the primary form of
CC ADP-ribosylation of proteins in response to DNA damage. Mainly mediates
CC glutamate and aspartate ADP-ribosylation of target proteins in absence
CC of HPF1. Following interaction with HPF1, catalyzes serine ADP-
CC ribosylation of target proteins; HPF1 conferring serine specificity by
CC completing the PARP1 active site. Also catalyzes tyrosine ADP-
CC ribosylation of target proteins following interaction with HPF1. PARP1
CC initiates the repair of DNA breaks: recognizes and binds DNA breaks
CC within chromatin and recruits HPF1, licensing serine ADP-ribosylation
CC of target proteins, such as histones, thereby promoting decompaction of
CC chromatin and the recruitment of repair factors leading to the
CC reparation of DNA strand breaks. In addition to proteins, also able to
CC ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break
CC termini containing terminal phosphates and a 2'-OH group in single- and
CC double-stranded DNA, respectively. {ECO:0000250|UniProtKB:P09874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29999, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142556; Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58233;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:58236, Rhea:RHEA-
CC COMP:10136, Rhea:RHEA-COMP:15092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:46858, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142557; Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58237;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09874}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P09874}. Chromosome
CC {ECO:0000250|UniProtKB:P09874}. Note=Localizes to sites of DNA damage.
CC {ECO:0000250|UniProtKB:P09874}.
CC -!- DOMAIN: The N-terminal disordered region does not act as a key DNA-
CC binding domain. The WGR and PARP catalytic domains function together to
CC recruit PARP1 to sites of DNA breaks. The N-terminal disordered region
CC is only required for activation on specific types of DNA damage.
CC {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- DOMAIN: The WGR domain bridges two nucleosomes, with the broken DNA
CC aligned in a position suitable for ligation. The bridging induces
CC structural changes in PARP1 that signal the recognition of a DNA break
CC to the catalytic domain of PARP1, promoting HPF1 recruitment and
CC subsequent activation of PARP1, licensing serine ADP-ribosylation of
CC target proteins. {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- PTM: Poly-ADP-ribosylated on glutamate and aspartate residues by
CC autocatalysis. {ECO:0000250|UniProtKB:P09874}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; X52690; CAA36917.1; -; mRNA.
DR PIR; JH0581; JH0581.
DR PDB; 1A26; X-ray; 2.25 A; A=652-1011.
DR PDB; 1EFY; X-ray; 2.20 A; A=659-1008.
DR PDB; 1PAX; X-ray; 2.40 A; A=652-1011.
DR PDB; 2PAW; X-ray; 2.30 A; A=652-1011.
DR PDB; 2PAX; X-ray; 2.40 A; A=652-1011.
DR PDB; 3PAX; X-ray; 2.40 A; A=652-1011.
DR PDB; 4PAX; X-ray; 2.80 A; A=652-1011.
DR PDB; 6I8M; X-ray; 2.10 A; A=651-1011.
DR PDB; 6I8T; X-ray; 2.10 A; A=651-1011.
DR PDBsum; 1A26; -.
DR PDBsum; 1EFY; -.
DR PDBsum; 1PAX; -.
DR PDBsum; 2PAW; -.
DR PDBsum; 2PAX; -.
DR PDBsum; 3PAX; -.
DR PDBsum; 4PAX; -.
DR PDBsum; 6I8M; -.
DR PDBsum; 6I8T; -.
DR AlphaFoldDB; P26446; -.
DR SMR; P26446; -.
DR STRING; 9031.ENSGALP00000015000; -.
DR PaxDb; P26446; -.
DR VEuPathDB; HostDB:geneid_396199; -.
DR eggNOG; KOG1037; Eukaryota.
DR InParanoid; P26446; -.
DR OrthoDB; 909382at2759; -.
DR PhylomeDB; P26446; -.
DR EvolutionaryTrace; P26446; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
DR GO; GO:0030592; P:DNA ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0018424; P:peptidyl-glutamic acid poly-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:UniProtKB.
DR Gene3D; 1.20.142.10; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.30.1740.10; -; 2.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR012982; PADR1.
DR InterPro; IPR038650; PADR1_dom_sf.
DR InterPro; IPR008288; PARP.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR InterPro; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08063; PADR1; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR Pfam; PF00645; zf-PARP; 2.
DR PIRSF; PIRSF000489; NAD_ADPRT; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SMART; SM01336; zf-PARP; 2.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS00347; PARP_ZN_FINGER_1; 2.
DR PROSITE; PS50064; PARP_ZN_FINGER_2; 2.
DR PROSITE; PS51977; WGR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Chromosome; DNA damage; DNA repair;
KW DNA-binding; Glycosyltransferase; Metal-binding; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..1011
FT /note="Poly [ADP-ribose] polymerase 1"
FT /id="PRO_0000211322"
FT DOMAIN 382..473
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 539..635
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 659..776
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 785..1011
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT ZN_FING 9..91
FT /note="PARP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT ZN_FING 113..203
FT /note="PARP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT REGION 198..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..522
FT /note="Automodification domain"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT REGION 496..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 207..209
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOTIF 220..225
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT ACT_SITE 985
FT /note="For poly [ADP-ribose] polymerase activity"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT BINDING 859..861
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 868
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 875
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 901
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT MOD_RES 403
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 404
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 410
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 411
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 432
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 434
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 441
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 442
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 453
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 454
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 468
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 481
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 485
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 488
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 509
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 510
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 517
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT CONFLICT 895
FT /note="A -> R (in Ref. 1; CAA36917)"
FT /evidence="ECO:0000305"
FT HELIX 664..673
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 676..685
FT /evidence="ECO:0007829|PDB:6I8M"
FT TURN 690..692
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 695..697
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 700..719
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 723..736
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 742..744
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 752..776
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 786..793
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 796..800
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 806..817
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 821..823
FT /evidence="ECO:0007829|PDB:1EFY"
FT STRAND 827..838
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 841..845
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 846..850
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 854..861
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 863..865
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 866..872
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 883..885
FT /evidence="ECO:0007829|PDB:1EFY"
FT STRAND 890..897
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 898..902
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 903..905
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 909..911
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 913..922
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 925..931
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 944..947
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 950..953
FT /evidence="ECO:0007829|PDB:6I8M"
FT TURN 955..957
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 959..961
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 964..966
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 971..973
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 978..980
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 985..990
FT /evidence="ECO:0007829|PDB:6I8M"
FT HELIX 991..993
FT /evidence="ECO:0007829|PDB:6I8M"
FT STRAND 994..1005
FT /evidence="ECO:0007829|PDB:6I8M"
SQ SEQUENCE 1011 AA; 113520 MW; 261AED9383139144 CRC64;
MAETGDKPYR AEYAKSGRAS CKKCGESIAK DSLRLALMVQ SPMFDGKVPH WHHYSCFWKR
ARIVSHTDID GFPELRWEDQ EKIKKAIETG ALQEEKGGTR KEVGKAEKSL TDFAAEYAKS
NRSTCKGCEQ KIEKGQIRIS KKMVHPEKPQ LGMIDNWYHP DCFVSRRAEL GFLPAYGATQ
LLGFSILKAE DKETLKKQLP ATKTEGKRKG EEVDGNVVAK KKSRKEKEKE SKQEKQLKEQ
TELIWGIKDE LRKVCSTNDL KELLIANKQE VPSGENAILD RVADGMAFGA LLPCEECKGQ
FVFKSDAYYC SGDITAWTKC VAKTQTPNRK DWVIPKEFRE IPYLKKFKCK KQDRIFPPEA
ATVNSAPPPP ASAPLTETVT APQDKPLTNM KILTLGKLSK NKEEVKNIVE ELGGKMTTTA
NKATLCISTQ KEVEKMSKKM EEVKDAKVRV VSEEFLKDVK SSNKGFQELL SLHAISPWGA
EVKTEHQEVA VDGKCSKPAN MKSAGKVKEE QGPSKSEKKM KLTVKGGAAV DPDSGLEDSA
HVFEKGGKIF SATLGLVDIV KGTNSYYKLQ LLEDDRESRY WVFRSWGRVG TVIGSNKLEQ
MPSKEDAVEH FLNLYEEKTG NSWHSKNFTK YPKKFYPLEI DYGQDEEAVR KLTVSAGTKS
KLAKPIQDLI KMIFDVESMK KAMVEFEIDL QKMPLGKLSK RQIQSAYSIL NEVQQAVSDG
GSESQILDLS NRFYTLIPHD FGMKKPPLLS NLEYIQAKVQ MLDNLLDIEV AYSLLRGGNE
DGDKDPIDIN YEKLRTDIKV VDKDSEEAKI IKQYVKNTHA ATHNAYDLKV VEIFRIEREG
ESQRYKPFKQ LHNRQLLWHG SRTTNFAGIL SQGLRIAPPE APVTGYMFGK GIYFADMVSK
SANYCHTSQA DPIGLILLGE VALGNMYELK NASHITKLPK GKHSVKGLGK TAPDPTATTT
LDGVEVPLGN GISTGINDTC LLYNEYIVYD VAQVNLKYLL KLKFNYKTSL W
