ID   DDX59_HUMAN             Reviewed;         619 AA.
AC   Q5T1V6; Q6PJL2; Q8IVW3; Q9H0W3;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   29-SEP-2021, entry version 155.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX59;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 59;
DE   AltName: Full=Zinc finger HIT domain-containing protein 5 {ECO:0000303|PubMed:28561026};
GN   Name=DDX59; Synonyms=ZNHIT5 {ECO:0000303|PubMed:28561026};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-472.
RC   TISSUE=Brain, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-156 AND SER-160, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   INTERACTION WITH RUVBL1/RUVBL2 COMPLEX.
RX   PubMed=28561026; DOI=10.1038/ncomms15615;
RA   Cloutier P., Poitras C., Durand M., Hekmat O., Fiola-Masson E.,
RA   Bouchard A., Faubert D., Chabot B., Coulombe B.;
RT   "R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2
RT   to regulate assembly of U5 small nuclear ribonucleoprotein.";
RL   Nat. Commun. 8:15615-15615(2017).
RN   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [11]
RP   STRUCTURE BY NMR OF 94-146.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the ZF-hit domain in DEAD (Asp-Glu-Ala-Asp) box
RT   polypeptide 59.";
RL   Submitted (FEB-2009) to the PDB data bank.
RN   [12]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-77.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [13]
RP   VARIANTS OFD5 GLY-367 AND ARG-534, CHARACTERIZATION OF VARIANT OFD5
RP   GLY-367, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=23972372; DOI=10.1016/j.ajhg.2013.07.012;
RA   Shamseldin H.E., Rajab A., Alhashem A., Shaheen R., Al-Shidi T., Alamro R.,
RA   Al Harassi S., Alkuraya F.S.;
RT   "Mutations in DDX59 implicate RNA helicase in the pathogenesis of
RT   orofaciodigital syndrome.";
RL   Am. J. Hum. Genet. 93:555-560(2013).
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=3.6.4.13;
CC   -!- SUBUNIT: Interacts (via HIT-type zinc finger) with the RUVBL1/RUVBL2
CC       complex in the presence of ADP. {ECO:0000269|PubMed:28561026}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23972372}. Nucleus
CC       {ECO:0000269|PubMed:23972372}. Note=Exhibits granular localization in
CC       the nucleus, as well as in the cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5T1V6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5T1V6-2; Sequence=VSP_024227;
CC   -!- TISSUE SPECIFICITY: Expressed in fibroblasts (at protein level).
CC       {ECO:0000269|PubMed:23972372}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- DISEASE: Orofaciodigital syndrome 5 (OFD5) [MIM:174300]: A form of
CC       orofaciodigital syndrome, a group of heterogeneous disorders
CC       characterized by malformations of the oral cavity, face and digits, and
CC       associated phenotypic abnormalities that lead to the delineation of
CC       various subtypes. OFD5 patients show the core features of cleft palate,
CC       lobulated tongue, and polydactyly. Additional features include frontal
CC       bossing and intellectual disability. {ECO:0000269|PubMed:23972372}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX59 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH14183.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 433.; Evidence={ECO:0000305};
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DR   EMBL; AL136611; CAB66546.1; -; mRNA.
DR   EMBL; AL445483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014183; AAH14183.1; ALT_SEQ; mRNA.
DR   EMBL; BC041801; AAH41801.1; -; mRNA.
DR   CCDS; CCDS30964.1; -. [Q5T1V6-1]
DR   RefSeq; NP_001026895.2; NM_001031725.5. [Q5T1V6-1]
DR   RefSeq; NP_001307110.1; NM_001320181.1.
DR   RefSeq; NP_001307111.1; NM_001320182.1.
DR   RefSeq; XP_011508337.1; XM_011510035.2.
DR   RefSeq; XP_016857920.1; XM_017002431.1.
DR   RefSeq; XP_016857921.1; XM_017002432.1. [Q5T1V6-1]
DR   PDB; 2YQP; NMR; -; A=94-146.
DR   PDBsum; 2YQP; -.
DR   SMR; Q5T1V6; -.
DR   BioGRID; 123664; 14.
DR   IntAct; Q5T1V6; 1.
DR   STRING; 9606.ENSP00000330460; -.
DR   GlyGen; Q5T1V6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5T1V6; -.
DR   PhosphoSitePlus; Q5T1V6; -.
DR   BioMuta; DDX59; -.
DR   DMDM; 74762230; -.
DR   EPD; Q5T1V6; -.
DR   jPOST; Q5T1V6; -.
DR   MassIVE; Q5T1V6; -.
DR   MaxQB; Q5T1V6; -.
DR   PaxDb; Q5T1V6; -.
DR   PeptideAtlas; Q5T1V6; -.
DR   PRIDE; Q5T1V6; -.
DR   ProteomicsDB; 64290; -. [Q5T1V6-1]
DR   ProteomicsDB; 64291; -. [Q5T1V6-2]
DR   Antibodypedia; 34489; 246 antibodies.
DR   DNASU; 83479; -.
DR   Ensembl; ENST00000331314; ENSP00000330460; ENSG00000118197. [Q5T1V6-1]
DR   Ensembl; ENST00000447706; ENSP00000394367; ENSG00000118197. [Q5T1V6-2]
DR   GeneID; 83479; -.
DR   KEGG; hsa:83479; -.
DR   UCSC; uc009wzk.4; human. [Q5T1V6-1]
DR   CTD; 83479; -.
DR   DisGeNET; 83479; -.
DR   GeneCards; DDX59; -.
DR   HGNC; HGNC:25360; DDX59.
DR   HPA; ENSG00000118197; Low tissue specificity.
DR   MalaCards; DDX59; -.
DR   MIM; 174300; phenotype.
DR   MIM; 615464; gene.
DR   neXtProt; NX_Q5T1V6; -.
DR   OpenTargets; ENSG00000118197; -.
DR   Orphanet; 2919; Orofaciodigital syndrome type 5.
DR   PharmGKB; PA142672000; -.
DR   VEuPathDB; HostDB:ENSG00000118197; -.
DR   eggNOG; KOG0331; Eukaryota.
DR   GeneTree; ENSGT00940000158639; -.
DR   HOGENOM; CLU_003041_1_5_1; -.
DR   InParanoid; Q5T1V6; -.
DR   OMA; DESFCIR; -.
DR   OrthoDB; 400908at2759; -.
DR   PhylomeDB; Q5T1V6; -.
DR   TreeFam; TF330866; -.
DR   PathwayCommons; Q5T1V6; -.
DR   BioGRID-ORCS; 83479; 630 hits in 1019 CRISPR screens.
DR   ChiTaRS; DDX59; human.
DR   EvolutionaryTrace; Q5T1V6; -.
DR   GeneWiki; DDX59; -.
DR   GenomeRNAi; 83479; -.
DR   Pharos; Q5T1V6; Tbio.
DR   PRO; PR:Q5T1V6; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5T1V6; protein.
DR   Bgee; ENSG00000118197; Expressed in amniotic fluid and 228 other tissues.
DR   ExpressionAtlas; Q5T1V6; baseline and differential.
DR   Genevisible; Q5T1V6; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140603; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   InterPro; IPR007529; Znf_HIT.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04438; zf-HIT; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Ciliopathy; Cytoplasm;
KW   Disease variant; Helicase; Hydrolase; Isopeptide bond; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..619
FT                   /note="Probable ATP-dependent RNA helicase DDX59"
FT                   /id="PRO_0000282713"
FT   DOMAIN          234..405
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          416..579
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         104..133
FT                   /note="HIT-type"
FT   NP_BIND         247..254
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          57..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           203..231
FT                   /note="Q motif"
FT   MOTIF           353..356
FT                   /note="DEAD box"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         76
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         156
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   CROSSLNK        26
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         533..619
FT                   /note="IGRVGRLGQNGTAITFINNNSKRLFWDIAKRVKPTGSILPPQLLNSPYLHDQ
FT                   KRKEQQKDKQTQNDLVTGANLMDIIRKHDKSNSQK -> ENTYKSTWRNPQHFQQDVRM
FT                   TLGYVGKAQWEEDNQLKVKLGLKKNCSS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11230166"
FT                   /id="VSP_024227"
FT   VARIANT         77
FT                   /note="P -> T (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035842"
FT   VARIANT         107
FT                   /note="I -> V (in dbSNP:rs3795634)"
FT                   /id="VAR_031424"
FT   VARIANT         367
FT                   /note="V -> G (in OFD5; markedly reduced expression in
FT                   fibroblasts compared to wild-type protein; impaired SHH
FT                   signaling in SAG-treated fibroblasts; dbSNP:rs587777067)"
FT                   /evidence="ECO:0000269|PubMed:23972372"
FT                   /id="VAR_070198"
FT   VARIANT         472
FT                   /note="S -> R (in dbSNP:rs17854157)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_033001"
FT   VARIANT         534
FT                   /note="G -> R (in OFD5; dbSNP:rs886037652)"
FT                   /evidence="ECO:0000269|PubMed:23972372"
FT                   /id="VAR_070199"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:2YQP"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:2YQP"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:2YQP"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:2YQP"
FT   HELIX           129..143
FT                   /evidence="ECO:0007829|PDB:2YQP"
SQ   SEQUENCE   619 AA;  68810 MW;  2B4EE96C11CB48ED CRC64;
     MFVPRSLKIK RNANDDGKSC VAKIIKPDPE DLQLDKSRDV PVDAVATEAA TIDRHISESC
     PFPSPGGQLA EVHSVSPEQG AKDSHPSEEP VKSFSKTQRW AEPGEPICVV CGRYGEYICD
     KTDEDVCSLE CKAKHLLQVK EKEEKSKLSN PQKADSEPES PLNASYVYKE HPFILNLQED
     QIENLKQQLG ILVQGQEVTR PIIDFEHCSL PEVLNHNLKK SGYEVPTPIQ MQMIPVGLLG
     RDILASADTG SGKTAAFLLP VIMRALFESK TPSALILTPT RELAIQIERQ AKELMSGLPR
     MKTVLLVGGL PLPPQLYRLQ QHVKVIIATP GRLLDIIKQS SVELCGVKIV VVDEADTMLK
     MGFQQQVLDI LENIPNDCQT ILVSATIPTS IEQLASQLLH NPVRIITGEK NLPCANVRQI
     ILWVEDPAKK KKLFEILNDK KLFKPPVLVF VDCKLGADLL SEAVQKITGL KSISIHSEKS
     QIERKNILKG LLEGDYEVVV STGVLGRGLD LISVRLVVNF DMPSSMDEYV HQIGRVGRLG
     QNGTAITFIN NNSKRLFWDI AKRVKPTGSI LPPQLLNSPY LHDQKRKEQQ KDKQTQNDLV
     TGANLMDIIR KHDKSNSQK
//