PRKDC_CANLF
ID PRKDC_CANLF Reviewed; 4144 AA.
AC Q8WN22;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA-dependent protein kinase catalytic subunit;
DE Short=DNA-PK catalytic subunit;
DE Short=DNA-PKcs;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P78527};
GN Name=PRKDC;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN SCID.
RC STRAIN=Jack Russel terrier;
RX PubMed=11867233; DOI=10.1016/s0378-1119(01)00880-0;
RA Ding Q., Bramble L., Yuzbasiyan-Gurkan V., Bell T., Meek K.;
RT "DNA-PKcs mutations in dogs and horses: allele frequency and association
RT with neoplasia.";
RL Gene 283:263-269(2002).
CC -!- FUNCTION: Serine/threonine-protein kinase that acts as a molecular
CC sensor for DNA damage. Involved in DNA non-homologous end joining
CC (NHEJ) required for double-strand break (DSB) repair and V(D)J
CC recombination. Must be bound to DNA to express its catalytic
CC properties. Promotes processing of hairpin DNA structures in V(D)J
CC recombination by activation of the hairpin endonuclease artemis
CC (DCLRE1C). Recruited by XRCC5 and XRCC6 to DNA ends and is required to
CC (1) protect and align broken ends of DNA, thereby preventing their
CC degradation, (2) and sequester the DSB for repair by NHEJ. Act as a
CC scaffold protein to aid the localization of DNA repair proteins to the
CC site of damage. The assembly of the DNA-PK complex at DNA ends is also
CC required for the NHEJ ligation step. Found at the ends of chromosomes,
CC suggesting a further role in the maintenance of telomeric stability and
CC the prevention of chromosomal end fusion. Also involved in modulation
CC of transcription. As part of the DNA-PK complex, involved in the early
CC steps of ribosome assembly by promoting the processing of precursor
CC rRNA into mature 18S rRNA in the small-subunit processome. Binding to
CC U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-
CC subunit processome. Recognizes the substrate consensus sequence [ST]-Q.
CC Phosphorylates 'Ser-139' of histone variant H2AX, thereby regulating
CC DNA damage response mechanism. Phosphorylates ASF1A, DCLRE1C, c-
CC Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9,
CC FH, SRF, NHEJ1/XLF, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2. Can
CC phosphorylate C1D not only in the presence of linear DNA but also in
CC the presence of supercoiled DNA. Ability to phosphorylate p53/TP53 in
CC the presence of supercoiled DNA is dependent on C1D (By similarity).
CC Contributes to the determination of the circadian period length by
CC antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1
CC protein stability, most likely through an indirect mechanism (By
CC similarity). Plays a role in the regulation of DNA virus-mediated
CC innate immune response by assembling into the HDP-RNP complex, a
CC complex that serves as a platform for IRF3 phosphorylation and
CC subsequent innate immune response activation through the cGAS-STING
CC pathway (By similarity). Also regulates the cGAS-STING pathway by
CC catalyzing phosphorylation of CGAS, thereby impairing CGAS
CC oligomerization and activation (By similarity).
CC {ECO:0000250|UniProtKB:P78527, ECO:0000250|UniProtKB:P97313}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P78527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P78527};
CC -!- ACTIVITY REGULATION: Activity seems to be attenuated by
CC autophosphorylation. Binding to the SL1 region of U3 small nucleolar
CC RNA promotes auto-phosphorylation activity. Inhibited by wortmannin.
CC {ECO:0000250|UniProtKB:P78527}.
CC -!- SUBUNIT: DNA-PK is a heterotrimer of PRKDC and the Ku dimer (composed
CC of XRCC6/Ku70 and XRCC5/Ku86). Formation of this complex may be
CC promoted by interaction with ILF3. Component of the core long-range
CC non-homologous end joining (NHEJ) complex (also named DNA-PK complex)
CC composed of PRKDC, LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF.
CC Additional component of the NHEJ complex includes PAXX. Following
CC autophosphorylation, PRKDC dissociates from DNA. Interacts with DNA-
CC PKcs-interacting protein (KIP) with the region upstream the kinase
CC domain. PRKDC alone also interacts with and phosphorylates DCLRE1C,
CC thereby activating the latent endonuclease activity of this protein.
CC Interacts with C1D. Interacts with TTI1 and TELO2. Interacts with CIB1.
CC Interacts with SETX. Interacts with NR4A3; the DNA-dependent protein
CC kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents
CC NR4A3 ubiquitination and degradation. Interacts with BRAT1. Part of the
CC HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6,
CC paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1
CC RNA. Interacts with KAT5. {ECO:0000250|UniProtKB:P78527}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P78527}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P78527}.
CC -!- PTM: Autophosphorylated at two clusters, the T2609 cluster and the
CC S2056 cluster. Autophosphorylated on Ser-2069, Thr-2621, Thr-2650 and
CC Thr-2659. Ser-2069 and Thr-2621 are DNA damage-inducible
CC phosphorylation sites (inducible with ionizing radiation, IR)
CC dephosphorylated by PPP5C (By similarity). Autophosphorylation induces
CC a conformational change that leads to remodeling of the DNA-PK complex,
CC requisite for efficient end processing and DNA repair (By similarity).
CC Autophosphorylation in trans within DNA-PK complexes loaded on DNA ends
CC leads to the dissociation of PRKDC from DNA and the transition into the
CC short-range NHEJ complex (By similarity). Autophosphorylation of the
CC T2609 cluster is required for hematopoietic development and protein
CC synthesis in erythrocytes precursors (By similarity).
CC {ECO:0000250|UniProtKB:P78527, ECO:0000250|UniProtKB:P97313}.
CC -!- PTM: S-nitrosylated by GAPDH. {ECO:0000250|UniProtKB:P97313}.
CC -!- PTM: Polyubiquitinated by RNF144A, leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P78527}.
CC -!- DISEASE: Note=Defects in PRKDC are the cause of severe combined immune
CC deficiency (SCID) which is characterized by a lack of mature functional
CC lymphocytes and a high susceptibility to lethal opportunistic
CC infections if not chronically treated with antibiotics. The lack of
CC B- and T-cell immunity resembles severe combined immunodeficiency
CC syndrome in human infants. {ECO:0000269|PubMed:11867233}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; AF448227; AAL40979.1; -; mRNA.
DR SMR; Q8WN22; -.
DR STRING; 9615.ENSCAFP00000009842; -.
DR PaxDb; Q8WN22; -.
DR PRIDE; Q8WN22; -.
DR eggNOG; KOG0891; Eukaryota.
DR InParanoid; Q8WN22; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004677; F:DNA-dependent protein kinase activity; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0034511; F:U3 snoRNA binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:InterPro.
DR GO; GO:0033152; P:immunoglobulin V(D)J recombination; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; ISS:UniProtKB.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045621; P:positive regulation of lymphocyte differentiation; ISS:UniProtKB.
DR GO; GO:1905221; P:positive regulation of platelet formation; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0034462; P:small-subunit processome assembly; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR CDD; cd05172; PIKKc_DNA-PK; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR037706; DNA-PK_dom.
DR InterPro; IPR012582; DNAPKcs_CC3.
DR InterPro; IPR045581; DNAPKcs_CC5.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR Pfam; PF19704; DNAPKcs_CC5; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08163; NUC194; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM01344; NUC194; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Biological rhythms; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Immunity; Innate immunity;
KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribosome biogenesis; SCID; Serine/threonine-protein kinase;
KW TPR repeat; Transferase; Ubl conjugation.
FT CHAIN 1..4144
FT /note="DNA-dependent protein kinase catalytic subunit"
FT /id="PRO_0000225632"
FT REPEAT 298..333
FT /note="HEAT 1"
FT REPEAT 1014..1050
FT /note="HEAT 2"
FT REPEAT 1736..1769
FT /note="TPR 1"
FT REPEAT 2903..2935
FT /note="TPR 2"
FT DOMAIN 2922..3555
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT REPEAT 2936..2964
FT /note="TPR 3"
FT REPEAT 2965..2998
FT /note="TPR 4"
FT REPEAT 3711..3748
FT /note="TPR 5"
FT DOMAIN 3738..4069
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 4112..4144
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1516..1551
FT /note="Interaction with C1D"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT REGION 1516..1551
FT /note="Leucine-zipper"
FT REGION 2448..3228
FT /note="KIP-binding"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT REGION 2697..2729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3744..3750
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3935..3943
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3955..3980
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT SITE 2033..2034
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 1075
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 1219
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 1983
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 2069
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 2271
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 2547
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 2621
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 2624
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 2650
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 2659
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 2805
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 3221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 3257
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 3276
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 3654
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 3658
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 3747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 3837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
FT MOD_RES 4042
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78527"
SQ SEQUENCE 4144 AA; 473061 MW; 27CE0079556E094E CRC64;
MFSSSQIPRV FLIPSRRELR LVLQLQESLS AGDRCSAAMA SYQLTRGLGQ ECVLSSDPAV
LALQTSLVFS KDFGLLVFVR KSLSIDEFRD CREEVLKFLY IFLEKIGQKI TPYSLDIKTT
CTSVYTKDKA AKCKIPALDL LIKLLQTLRS SRLMDEFSIG ELFNKFYGEL ALKTKIQDTV
LEKIYELLGV LAEVHPSEMI NNSEKLFRAF LGELKIQMTS AIREPKLPVL AGCLKGLSSL
MCNFTKSMEE DPQTSREIFD FALKAIRPQI DLKRYAVPLA GLCLFTLHAS QFSTCLLDNY
VSLFEVLSKW CSHTNVEMKK AAHSALESFL KQVSFMVAKD AEMHKSKLQY FMEQFYGIIR
NMDSNSKDLS IAIRGYGLFA GPCKVINAKD VDFMYIELIQ RCKQLFLTQI DTVDDHVYHM
PSFLQSIASV LLYLDRVPEV YTPVLEHLMV AQIDSFPQYS PKMQSVCCKA LVKVFLALGG
KGPVLWNCIS TVVHQGLIRI CSKPVILQKG VESEPEEYRA SGEVRTGKWK VPTYKDYLDL
FRSLLSCDQM MDSLLADEAF LFVNSSLQNL NRLLYDEFVK SVLKIIEKLD LTLEKRNVGE
HEDENEATGV WVIPTSDPAA NLHPAKPKDF SAFINLVEFC RDILPEKHIE FFEPWVYSFA
YELILQSTRL PLISGFYKLL SVAVRNAKKI KYFEGVGMKS QTQAPKDPEK YSCFALFAKF
GKEVTVKMKQ YKDELLASCL TFILSLPHDI IELDIRAYIP ALQMAFKLGL SYTPLAEVGL
NALEEWSVCI CKHIIQPHYK DILPSLDGYL KTSALSDETK NSWEVSAPSQ AAQKGFNQVV
LKHLKKTKNI SSNEALSLEE IRIRVVQMLG FLGGQINKNL LTATSSDEMM KKCVAWDREK
RLSFAVPFIE MKPVIYLDVF LPRVTELALS ASDRQTKVAA CELLHSMVMF TLGKATQMPE
CGQGFPPMYQ LYKRTFPALL RLACDVDQVT RQLYEPLVMQ LIHWFTNNKK FESQDTVALL
ETILDGIVDP VDSTLRDFCG RCIREFLKWS IKQTTPQQQE KSPVNTKSLF KRLYSFALHP
NAFKRLGASL AFNNIYREFR EEESLVEQFV FEALVTYLES LALAHTDEKP LGTIRQCCDA
IDHLRHIIEK KHVSLNKVKK RRRPRGFPPS ASLCLLDMVQ WLLAHCGRPQ TECRHKSIEL
FYKFVPLLPG NKSPSLWLKD ILKNKDTSFL INTFEGGGGS CDRPSGILVQ PTLFHLQGPF
SLRAALQWMD MLLAALECYN TFIEEKTLKA PDVLGTETQS SLWKAVAFFL DNIAMHDITA
AEKCFGTGAA GHRPSPQEGE RYNYSKCTIV VRIMEFTTTL LNTSPDGWKL LEEDLCNNKN
FMTLLVKILC QPSSIGFNIG DVLVMNHLPD VCVNLMKALK KSPYKDTLEM CLKEKITVQS
IEELCAVDLY GPDAYVDRAT LASVVSACKQ LHRAGVLHVV LPSQSADQRH SVGIKLLFLV
YKSIAPGDER EYFPSLDPSC KRLASGLLEL AFAFGGLCEH LVDLLLDTAV LSMPASGESQ
RNMVSFSHGE YFYSLFSEII NTELLRNLDM TVLKLMKSSV DNPKMVSAIL NGMLDQSFRD
RASRKQQGLK LASTILHNWK KWDSWWAKDS APESKTAVLT LLAKILQIDS SVSFNTNHSA
FPEVFTTYTS LLADSNLGLH LMGQAVILLP FFTNLTGGNL EDLEHVLEKL IVSNFPMKSE
EFPVGTLRYS NYVDCMKKFL DALELSQSPV LLQLMAEILC REQQHVMEEL FQSTFKKIAR
KSSCVTQLAL LESVYRMFKR DDLLSNVTRQ AFVDRSLLTL LWHCGLNALR EFFGKIVVET
IDVLKSRFTK LNESTFDTQI TKKMGFYKML DVMYSRLSKD DVHSKESKIN QVFHGSCITE
GNELTKTLIK LCYDAFTENM AGENQLLERR RLYHCAAYNC AISVICCVFT ELKFYQGFLF
SEKPEKNLLI LENLIDLKRC YTFPIEVEVP MERRKKYIEI RKEAREAVNG DSDGPHYLSS
LSYLADSSLS EEMSQFDFST GVQSYSYGSQ DPKSTHGHFR RREHKDPMVQ DAVLELEMDE
LNQHECMATM TALIKHMQRN QILSKDEGSV PRNLPPWMKF LHDKLGNPSV SLNIRLFLAK
LVINTEEVFR PYAKYWLSPL LQLVVSENNG GEGIHYMVVE IVVTVLSWTG LATPVGVPKD
EVLANRLLHF LMEHVFHQKR AVFRHNLEII KTLVECWKDC LSVPYRLIFE KFSSKDPNSK
DNSVGIQLLG IVMANNLPPY DPKCGIERIK YFEALVSNMS FVKYKEVYAA AAEVLGLTLR
YITERENILE NVVYELVIKQ LKQHQNTMED KFIVCLNKVV KNFPPLADRF MNAVFFLLPK
FHGVMKTLCL EVVLCRAEEI TNIYLELKSK DFIQVMRHRD DERQKVCLDI IYKMMAKLKP
VELRDLLNSV VEFISHPSPV CREQMYNILM WIHDNYRDPE SQADDDSREV FKLAKDVLIQ
GLIDENAGLQ LIIRNFWSHE TRLPSNTLDR LLALNSLYSP KIEVHFLSLA TDFLLEMTSL
SPDYANPVFE HPLSECEFQE YTIDSDWRFR STVLTPMFIE TQASQSTLQT RTQERSLPAQ
GVMARQIRAT QQQYDFTPTQ TADGRSSFNW LTGSSIDPLV DYTVSSSDSS SSSLLFAQKR
NEKSQRAPLK SVGPDFGEKK LGLPGDKVDN KAKGIDNRTE ILRLRRRFIK DQEKLSLIYA
RKGIAEQKRE KEIKSELKMK HDAQVILYRS YRQGDLPDIQ IKYSSLVTPL QAVAQRDPVV
AKQLFGSLFS GIIKEMDKYK TMSEKNNITQ KLLQDFSHFL NSTFSFFPPF VSCIQEISCQ
HTDLLSLDPG SIRASCLASL QQPVGVRLLE EALLHLGPQE PPAKQFKGRM RVSPDVVRWM
ELAKLYRSIG EYDILRGIFS SEIGTKQITQ SAIFAEARSD YSEAAKQYNE ALNKEEWVDG
EPTEAEKDFW ELASLDCYNQ LAEWKSLAYC SIVSVDNENP PDLNKMWSEP FYRETYLPYM
IRSKLKLLLQ GEADQSLLTF IDEAVNKDLQ KALIELHYSQ ELSLLYILQD DIDRAKYYIE
NCIQIFMQNY SSIDVLLHRS RLTKLQSVQT MIEIQEFISF ISRQGNLSSQ APLKRLLKSW
TNRYPDARMD PVHIWDDIIT NRCFFLSKIE EKLTLPLGDH SLSMDEERDS SDKMEVQEQG
EEVCSLIKNC MFSMKMKMVE SARKQHNFSL AMKLLKELRR ESKTRDDWQV KWVHTYCRLS
HSRIQGQSCL QQILSALKTV SLLAGESTSS YFSKNVLAFH DQNILLGTTY SIIANALRRE
PACLAEIEES RARRILDLSG SSLENAEKVI AVLYQRAFHH LSEAVRTAEE EAQPSLRGQG
PVASLTDAYM TLADFCDQQL RKEEESASVT ESVELQTYPG LVVDNMLKAL KLHSSEARLK
FPRLLQIIEL YPEETLSLMT KEISSTPCWQ FIGWISHMVA LLDQEEAVAV QCTVEEIADN
YPQAIVYPFI ISSESYSFKD TSTGHKNKEF VARIKTKLDL GGVIQDFISA LEQLSNPEML
FKDWTDDMKA ELAKNPVSKK NIEKMYERMY AALGDLRAPG LGAFRRRFIQ VFGKEFDKHF
GKGGSKLPGM KLRDFGSITD SLFYKMCTDS KPPGNLKECS PWMSDFKVEF LRNELEIPGQ
YDGKGKPLPE YHARIAGFDE RIKVMASIRK PKRIIIRGRD EKEYPLLVKG GEDLRQDQRI
EQLFEVMNVL LSQDTACSQR NMQLKTYHVI PMTSRLGLIE WIENTLTLKD FLLSNMSREE
KAAYTSDPKA PPCEYRDWLA KMSGKYDVGA YMSMFKAASR TETVTSFRRR ESRVPADLLK
RAFLKMSTGP AAFLALRSHF ASSHALMCIS HWILGIGDRH LNNFMVSMET GGLIGIDFGH
AFGSATQFLP VPELMPFRLT RQFINLMLPM KEAGVVYSIM VHALRAFRSH SDLLTNTMDV
FVKEPSFDWK NFEQKMLKKG GSWIQEINVT EKNWYPRQKI HYAKRKLAGA NPAVITCDEL
FLGHEKALAF GDYVAVARGS KDHNIRAQQP ENGLSEEAQV KCLIDQATDP NILGRTWIGW
EPWM
