GenomeNet

Database: UniProt
Entry: Q7YQM3
LinkDB: Q7YQM3
Original site: Q7YQM3 
ID   ATRX_PONPY              Reviewed;        2492 AA.
AC   Q7YQM3;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   11-DEC-2019, entry version 112.
DE   RecName: Full=Transcriptional regulator ATRX;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase ATRX;
DE   AltName: Full=X-linked helicase II;
DE   AltName: Full=X-linked nuclear protein;
DE            Short=XNP;
GN   Name=ATRX;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12777533; DOI=10.1093/molbev/msg134;
RA   Kitano T., Schwarz C., Nickel B., Paeaebo S.;
RT   "Gene diversity patterns at 10 X-chromosomal loci in humans and
RT   chimpanzees.";
RL   Mol. Biol. Evol. 20:1281-1289(2003).
CC   -!- FUNCTION: Involved in transcriptional regulation and chromatin
CC       remodeling. Facilitates DNA replication in multiple cellular
CC       environments and is required for efficient replication of a subset of
CC       genomic loci. Binds to DNA tandem repeat sequences in both telomeres
CC       and euchromatin and in vitro binds DNA quadruplex structures. May help
CC       stabilizing G-rich regions into regular chromatin structures by
CC       remodeling G4 DNA and incorporating H3.3-containing nucleosomes.
CC       Catalytic component of the chromatin remodeling complex ATRX:DAXX which
CC       has ATP-dependent DNA translocase activity and catalyzes the
CC       replication-independent deposition of histone H3.3 in pericentric DNA
CC       repeats outside S-phase and telomeres, and the in vitro remodeling of
CC       H3.3-containing nucleosomes. Its heterochromatin targeting is proposed
CC       to involve a combinatorial readout of histone H3 modifications
CC       (specifically methylation states of H3K9 and H3K4) and association with
CC       CBX5. Involved in maintaining telomere structural integrity in
CC       embryonic stem cells which probably implies recruitment of CBX5 to
CC       telomeres. May be involved in transcriptional regulation of telomeric
CC       repeat-containing RNA (TERRA). Acts as negative regulator of chromatin
CC       incorporation of transcriptionally repressive histone H2AFY,
CC       particularily at telomeres. Participates in the allele-specific gene
CC       expression at the imprinted IGF2/H19 gene locus. On the maternal
CC       allele, required for the chromatin occupancy of SMC1 and CTCTF within
CC       the H19 imprinting control region (ICR) and involved in esatblishment
CC       of histone tails modifications in the ICR. May be involved in brain
CC       development and facial morphogenesis. Binds to zinc-finger coding genes
CC       with atypical chromatin signatures and regulates its H3K9me3 levels.
CC       Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the
CC       deposition and maintenance of H3K9me3 at the 3' exons of zinc-finger
CC       genes (By similarity). {ECO:0000250|UniProtKB:P46100}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBUNIT: Interacts with DAXX to form the chromatin remodeling complex
CC       ATRX:DAXX. Probably binds EZH2. Binds annexin V in a calcium and
CC       phosphatidylcholine/phosphatidylserine-dependent manner. Interacts
CC       directly with CBX5 via the PxVxL motif. Interacts with RAD50, MRE11 and
CC       NBN; indicative for an association with the MRN complex. Interacts with
CC       histone H2AFY. Interacts with histone H3 peptides methylated at 'Lys-
CC       10' with preferences H3K9me3 > H3K9me2 > H3K9me1. Interacts with
CC       histone H3 peptides unmethylated at 'Lys-5' (H3K4me0). Interacts with
CC       MECP2, SMC1 and SMC3. Interacts with SETDB1, TRIM28 and ZNF274 (By
CC       similarity). {ECO:0000250|UniProtKB:P46100}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC       {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Associated with
CC       pericentromeric heterochromatin during interphase and mitosis, probably
CC       by interacting with CBX5/HP1 alpha. Colocalizes with histone H3.3,
CC       DAXX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with cohesin
CC       (SMC1 and SMC3) and MECP2 at the maternal H19 ICR (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The ADD domain predominantly interacts with histone H3
CC       trimethylated at 'Lys-10'(H3K9me3) (and to a lesser extent H3 mono- or
CC       dimethylated at 'Lys-10') and simultanously to histone H3 unmethylated
CC       at 'Lys-5' (H3K4me0). The interaction with H3K9me3 is disrupted by the
CC       presence of H3K4me3 suggesting a readout of the combined histone H3
CC       methylation state (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
CC       required for interaction with chromoshadow domains. This motif requires
CC       additional residues -7, -6, +4 and +5 of the central Val which contact
CC       the chromoshadow domain.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
DR   EMBL; AB102643; BAC81112.1; -; mRNA.
DR   PRIDE; Q7YQM3; -.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0031933; C:telomeric heterochromatin; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006336; P:DNA replication-independent nucleosome assembly; ISS:UniProtKB.
DR   GO; GO:1901581; P:negative regulation of telomeric RNA transcription from RNA pol II promoter; ISS:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR   GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; ISS:UniProtKB.
DR   GO; GO:0032206; P:positive regulation of telomere maintenance; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; ISS:UniProtKB.
DR   GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR025766; ADD.
DR   InterPro; IPR041430; ADD_ATRX.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF17981; ADD_ATRX; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51533; ADD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Chromatin regulator; Chromosome; DNA damage;
KW   DNA repair; DNA-binding; Helicase; Hydrolase; Isopeptide bond;
KW   Metal-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Telomere; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..2492
FT                   /note="Transcriptional regulator ATRX"
FT                   /id="PRO_0000074305"
FT   DOMAIN          159..296
FT                   /note="ADD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   DOMAIN          1581..1768
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          2025..2205
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         170..206
FT                   /note="GATA-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   ZN_FING         217..272
FT                   /note="PHD-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   NP_BIND         1594..1601
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          1189..1326
FT                   /note="Interaction with DAXX"
FT                   /evidence="ECO:0000250"
FT   REGION          2010..2280
FT                   /note="Interaction with MECP2"
FT                   /evidence="ECO:0000250"
FT   MOTIF           581..594
FT                   /note="PxVxL motif"
FT   MOTIF           1719..1722
FT                   /note="DEGH box"
FT   COMPBIAS        745..750
FT                   /note="Poly-Ser"
FT   COMPBIAS        1151..1156
FT                   /note="Poly-Ser"
FT   COMPBIAS        1166..1169
FT                   /note="Poly-Lys"
FT   COMPBIAS        1202..1206
FT                   /note="Poly-Ser"
FT   COMPBIAS        1259..1266
FT                   /note="Poly-Asp"
FT   COMPBIAS        1443..1466
FT                   /note="Poly-Glu"
FT   COMPBIAS        1499..1502
FT                   /note="Poly-Glu"
FT   COMPBIAS        1929..1939
FT                   /note="Poly-Lys"
FT   COMPBIAS        1941..1948
FT                   /note="Poly-Ser"
FT   COMPBIAS        2222..2225
FT                   /note="Poly-Lys"
FT   COMPBIAS        2262..2265
FT                   /note="Poly-Glu"
FT   COMPBIAS        2420..2425
FT                   /note="Poly-Gln"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         89
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         112
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61687"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         591
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         594
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         598
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         634
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         674
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         677
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         729
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         731
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         784
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61687"
FT   MOD_RES         819
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         849
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         850
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         875
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         876
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         889
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         962
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         967
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         974
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         977
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1011
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70486"
FT   MOD_RES         1012
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70486"
FT   MOD_RES         1013
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70486"
FT   MOD_RES         1061
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1063
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61687"
FT   MOD_RES         1245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61687"
FT   MOD_RES         1253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61687"
FT   MOD_RES         1322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1348
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1527
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1529
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1906
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61687"
FT   MOD_RES         1913
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61687"
FT   MOD_RES         1992
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         1996
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         2220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   MOD_RES         2474
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61687"
FT   MOD_RES         2480
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61687"
FT   CROSSLNK        10
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        138
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        142
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        299
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        438
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        623
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        623
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        1004
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        1488
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        1982
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        1982
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
FT   CROSSLNK        1987
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46100"
SQ   SEQUENCE   2492 AA;  282616 MW;  48EC97106D0CEF20 CRC64;
     MTAEPMSESK LNTLVQKLHD FLAHSSEESE ETSSPPRLAM NQNTDKISGS GSNSDMMENS
     KEEGTSSSEK SKSSGSSRSK RKPSIVTKYV ESDDEKPLDD ETVNEDASNE NSENDITMQS
     LPKGTVIVQP EPVLNEDKDD FKGPEFRSRS KMKTENLKKR GEDGLHGIVS CTACGQQVNH
     FQKDSIYRHP SLQVLICKNC FKYYMSDDIS RDSDGMDEQC RWCAEGGNLI CCDFCHNAFC
     KKCILRNLGR KELSTIMDEN NQWYCYICHP EPLLDLVTAC NSVFDNLEQL LQQNKKKIKV
     DSEKSNKVYE HTSRFSPKKT SSNCNGEEKK LDDSCSGSVT YSYSALIVPK EMIKKAKKLI
     ETTANMNSSY VKFLKQATDN SEINSATKLR QLKAFKSVLA DIKKAHLALE EDLNSEFRAM
     DAVSKEKNTK EHKVIEAKFE TKARKGEKPC ALEKKDISKS EAKLSRKQVD SEHMYQNVPT
     EEQRANKSTG GEHKKSDRKE EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQS
     SVDHQGDGSS GTEQEVESSS VKLSISSKDN RGGIKSKTTA KVTKELYVKL TPVSLSNSPI
     KGADCQEVPQ DKDGYKSCGL NPKLEKCGLG QENSDNEHLV ENEVSLLLEE SDLRRSPRVK
     TTPLRRQTET NPVTSNSDEE CNETVKEKQK LSVPVRKKDK RNSSDSAIDN PKPNKLPKSK
     QSETVDQNSD SDEMLAILKE VSRMSHSSSS DTDINEIHTN HKTLYDLKTQ AGKDDKGKRK
     RKSSTSGSDF DTKKGKSAKS SIISKKKRQT QSESSNYDSE LEKEIKSMSK IGAARTTKKR
     IPNTKDFDSS EDEKHSKKGM DNQGHKNLKT SQEGSSDDAE RKQERENFSS AEGTVDKDTT
     IMELRDRLPK KQQASASTDG VDKLSGKEEG FTSLEVRKVA ETKEKSKHLK TKICKKVQDG
     LSDITEKFLK KDQSDETSED DKKQSKKGTE EKKKTSDFKK KVIKMEQQYE SSSDGTEKLP
     EREEICHFPK GIKQIKNGTT DGEKKNKKIR DKTSKKKDEL SDYAEKSTGK GDSCDSSEDK
     KSKNGAYGRE KKRCTLLGKS SRKRQDCSSS DTEKYSMKED GCNSSDKRLK RIELRERRNL
     SSKRNTKEIQ SGSSSSDAEE SSEDNKKKKQ RTSSKKKAVI VKEKKRNSLR TSTKRKQADI
     TSSSSSDIED DDQNSIGEGS SDEQKIKPVT ENLVLSSHTG FCQSSGDEAL SKSVPVTVDD
     DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK KRTGKQNEEN PGDEEAKNQV
     NSESDSDSEE SKKPRYRHRL LRHKLTVSDG ESGEEKKTKP KEHKEVKGRN RRKVSSEDSE
     DSDFQESGVS EEVSESEDEQ RPRTRSAKKA ELEENQRSYK QKKKRRRIKV QEDSSSENKS
     NSEEEEEEKE EEEEEEEEEE EEEEDENDDS KSPGKGRKKI RKILKDDKLR TETQNALKEE
     EERRKRIAER EREREKLREV IEIEDASPTK CPITTKLVLD EDEETKEPLV QVHRNMVIKL
     KPHQVDGVQF MWDCCCESVK KTKKSPGSGC ILAHCMGLGK TLQVVSFLHT VLLCDKLDFS
     TALVVCPLNT ALNWMNEFEK WQEGLKDDEK LEVSELATVK RPQERSYMLQ RWQEDGGVMI
     IGYEMYRNLA QGRNVKSRKL KEIFNKALVD PGPDFVVCDE GHILKNEASA VSKAMNSIRS
     RRRIILTGTP LQNNLIEYHC MVNFIKENLL GSIKEFRNRF INPIQNGQCA DSTMVDVRVM
     KKRAHILYEM LAGCVQRKDY TALTKFLPPK HEYVLAVRMT SIQCKLYQYY LDHLTGVGNN
     SEGGRGKAGA KLFQDFQMLS RIWTHPWCLQ LDYISKENKG YFDEDSMDEF IASDSDETSM
     SLSSDDYTKK KKKGKKGKKD SSSSGSGSDN DVEVIKVWNS RSRGGGEGNV DETGNNPSVS
     LKLEESKATS SSNPSSPAPD WYKDFVTDAD AEVLEHSGKM VLLFEILRMA EEIGDKVLVF
     SQSLISLDLI EDFLELASRE KTEDKDKPLI YKGEGKWLRN IDYYRLDGST TAQSRKKWAE
     EFNDETNVRG RLFIISTKAG SLGINLVAAN RVIIFDASWN PSYDIQSIFR VYRFGQTKPV
     YVYRFLAQGT MEDKIYDRQV TKQSLSFRVV DQQQVERHFT MNELTELYTF EPDLLDDPNS
     EKKKKRDTPM LPKDTILAEL LQIHKEHIVG YHEHDSLLDH KEEEELTEEE RKAAWAEYEA
     EKKGLTMRFN IPTGTNLPPV SFNSQTPYIP FNLGALSAMS NQQLEDLINQ GREKVVEATN
     SVTAVRIQPL EDIISAVWKE NMNLSEAQVQ ALALSRQASQ ELDVKRREAI YNDVLTKQQM
     LISCVQRILM NRRLQQQYNQ QQQQQMTYQQ ATLGHLMMPK PPNLIMNPSN YQQIDMRGMY
     QPVAGGMQPP PLQRAPPPMR SKNPGPSQGK SM
//
DBGET integrated database retrieval system