DD19A_HUMAN
ID DD19A_HUMAN Reviewed; 478 AA.
AC Q9NUU7; B2RPL0; B4DRZ7; Q53FM0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=ATP-dependent RNA helicase DDX19A;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9UMR2};
DE AltName: Full=DDX19-like protein;
DE AltName: Full=DEAD box protein 19A;
GN Name=DDX19A; Synonyms=DDX19L;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Muscle;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [12]
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).
CC -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA export from the
CC nucleus. Rather than unwinding RNA duplexes, DDX19 functions as a
CC remodeler of ribonucleoprotein particles, whereby proteins bound to
CC nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding
CC proteins. {ECO:0000250|UniProtKB:Q9UMR2}.
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 Evidence={ECO:0000250|UniProtKB:Q9UMR2};
CC -!- INTERACTION:
CC Q9NUU7; O43310-2: CTIF; NbExp=4; IntAct=EBI-740301, EBI-12180013;
CC Q9NUU7; A9UHW6: MIF4GD; NbExp=7; IntAct=EBI-740301, EBI-373498;
CC Q9NUU7; A9UHW6-2: MIF4GD; NbExp=3; IntAct=EBI-740301, EBI-9118295;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UMR2}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UMR2}. Note=Associates
CC with the nuclear pore complex cytoplasmic fibrils.
CC {ECO:0000250|UniProtKB:Q9UMR2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NUU7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NUU7-2; Sequence=VSP_056954;
CC -!- DOMAIN: The N-terminal extension helix acts as an autoinhibitory
CC domain, preventing ATP hydrolysis, unless the N-terminus of the protein
CC is displaced by RNA binding, allowing cleft closure to bring key side
CC chains into position for catalysis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5
CC subfamily. {ECO:0000305}.
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DR EMBL; AK001988; BAA92022.1; -; mRNA.
DR EMBL; AK299504; BAG61459.1; -; mRNA.
DR EMBL; AK223262; BAD96982.1; -; mRNA.
DR EMBL; AL832970; CAH10622.1; -; mRNA.
DR EMBL; AC012184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471241; EAW51826.1; -; Genomic_DNA.
DR EMBL; BC005162; AAH05162.1; -; mRNA.
DR EMBL; BC006544; AAH06544.1; -; mRNA.
DR EMBL; BC137496; AAI37497.1; -; mRNA.
DR EMBL; BC137497; AAI37498.1; -; mRNA.
DR CCDS; CCDS10889.1; -. [Q9NUU7-1]
DR RefSeq; NP_001307451.1; NM_001320522.1.
DR RefSeq; NP_001307454.1; NM_001320525.1. [Q9NUU7-2]
DR RefSeq; NP_001307455.1; NM_001320526.1.
DR RefSeq; NP_001307456.1; NM_001320527.1.
DR RefSeq; NP_060802.1; NM_018332.4. [Q9NUU7-1]
DR AlphaFoldDB; Q9NUU7; -.
DR SMR; Q9NUU7; -.
DR BioGRID; 120592; 59.
DR IntAct; Q9NUU7; 29.
DR MINT; Q9NUU7; -.
DR STRING; 9606.ENSP00000306117; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q9NUU7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NUU7; -.
DR MetOSite; Q9NUU7; -.
DR PhosphoSitePlus; Q9NUU7; -.
DR SwissPalm; Q9NUU7; -.
DR BioMuta; DDX19A; -.
DR DMDM; 73919226; -.
DR EPD; Q9NUU7; -.
DR jPOST; Q9NUU7; -.
DR MassIVE; Q9NUU7; -.
DR MaxQB; Q9NUU7; -.
DR PaxDb; Q9NUU7; -.
DR PeptideAtlas; Q9NUU7; -.
DR PRIDE; Q9NUU7; -.
DR ProteomicsDB; 4981; -.
DR ProteomicsDB; 82721; -. [Q9NUU7-1]
DR Antibodypedia; 16355; 100 antibodies from 19 providers.
DR DNASU; 55308; -.
DR Ensembl; ENST00000302243.12; ENSP00000306117.7; ENSG00000168872.17. [Q9NUU7-1]
DR GeneID; 55308; -.
DR KEGG; hsa:55308; -.
DR MANE-Select; ENST00000302243.12; ENSP00000306117.7; NM_018332.5; NP_060802.1.
DR UCSC; uc002eyv.4; human. [Q9NUU7-1]
DR CTD; 55308; -.
DR DisGeNET; 55308; -.
DR GeneCards; DDX19A; -.
DR HGNC; HGNC:25628; DDX19A.
DR HPA; ENSG00000168872; Low tissue specificity.
DR neXtProt; NX_Q9NUU7; -.
DR OpenTargets; ENSG00000168872; -.
DR PharmGKB; PA134894996; -.
DR VEuPathDB; HostDB:ENSG00000168872; -.
DR eggNOG; KOG0332; Eukaryota.
DR GeneTree; ENSGT00940000154417; -.
DR InParanoid; Q9NUU7; -.
DR OMA; MDIPQVN; -.
DR OrthoDB; 608788at2759; -.
DR PhylomeDB; Q9NUU7; -.
DR TreeFam; TF314957; -.
DR PathwayCommons; Q9NUU7; -.
DR SignaLink; Q9NUU7; -.
DR BioGRID-ORCS; 55308; 377 hits in 1089 CRISPR screens.
DR ChiTaRS; DDX19A; human.
DR GenomeRNAi; 55308; -.
DR Pharos; Q9NUU7; Tdark.
DR PRO; PR:Q9NUU7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NUU7; protein.
DR Bgee; ENSG00000168872; Expressed in gastrocnemius and 106 other tissues.
DR ExpressionAtlas; Q9NUU7; baseline and differential.
DR Genevisible; Q9NUU7; HS.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; 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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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 Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Helicase;
KW Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..478
FT /note="ATP-dependent RNA helicase DDX19A"
FT /id="PRO_0000055021"
FT DOMAIN 124..294
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 305..473
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 2..299
FT /note="N-terminal lobe"
FT /evidence="ECO:0000250"
FT REGION 54..67
FT /note="N-terminal helix"
FT /evidence="ECO:0000250"
FT REGION 300..478
FT /note="C-terminal lobe"
FT /evidence="ECO:0000250"
FT MOTIF 91..119
FT /note="Q motif"
FT MOTIF 241..244
FT /note="DEAD box"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 137..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY15"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..98
FT /note="MATDSWALAVDEQEAAVKSMTNLQIKEEKVKADTNGIIKTSTTAEKTDEEEK
FT EDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPNSPLYSVKSFEELRL -> MSGTFLIR
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056954"
FT CONFLICT 463
FT /note="E -> G (in Ref. 2; BAD96982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 53975 MW; C51F9E1D7B8584D0 CRC64;
MATDSWALAV DEQEAAVKSM TNLQIKEEKV KADTNGIIKT STTAEKTDEE EKEDRAAQSL
LNKLIRSNLV DNTNQVEVLQ RDPNSPLYSV KSFEELRLKP QLLQGVYAMG FNRPSKIQEN
ALPMMLAEPP QNLIAQSQSG TGKTAAFVLA MLSRVEPSDR YPQCLCLSPT YELALQTGKV
IEQMGKFYPE LKLAYAVRGN KLERGQKISE QIVIGTPGTV LDWCSKLKFI DPKKIKVFVL
DEADVMIATQ GHQDQSIRIQ RMLPRNCQML LFSATFEDSV WKFAQKVVPD PNVIKLKREE
ETLDTIKQYY VLCSSRDEKF QALCNLYGAI TIAQAMIFCH TRKTASWLAA ELSKEGHQVA
LLSGEMMVEQ RAAVIERFRE GKEKVLVTTN VCARGIDVEQ VSVVINFDLP VDKDGNPDNE
TYLHRIGRTG RFGKRGLAVN MVDSKHSMNI LNRIQEHFNK KIERLDTDDL DEIEKIAN
