DDX59_HUMAN
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 03-AUG-2022, entry version 158.
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 AlphaFoldDB; Q5T1V6; -.
DR SMR; Q5T1V6; -.
DR BioGRID; 123664; 21.
DR IntAct; Q5T1V6; 1.
DR MINT; Q5T1V6; -.
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; 263 antibodies from 22 providers.
DR DNASU; 83479; -.
DR Ensembl; ENST00000331314.11; ENSP00000330460.6; ENSG00000118197.14. [Q5T1V6-1]
DR Ensembl; ENST00000447706.6; ENSP00000394367.2; ENSG00000118197.14. [Q5T1V6-2]
DR GeneID; 83479; -.
DR KEGG; hsa:83479; -.
DR MANE-Select; ENST00000331314.11; ENSP00000330460.6; NM_001031725.6; NP_001026895.2.
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 SignaLink; Q5T1V6; -.
DR BioGRID-ORCS; 83479; 640 hits in 1081 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 buccal mucosa cell and 194 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:0016887; 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 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 BINDING 247..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
