ID   DDX42_HUMAN             Reviewed;         938 AA.
AC   Q86XP3; A6NML1; A8KA43; O75619; Q68G51; Q96BK1; Q96HR7; Q9Y3V8;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   22-FEB-2012, entry version 82.
DE   RecName: Full=ATP-dependent RNA helicase DDX42;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 42;
DE   AltName: Full=RNA helicase-like protein;
DE            Short=RHELP;
DE   AltName: Full=RNA helicase-related protein;
DE            Short=RNAHP;
DE   AltName: Full=SF3b DEAD box protein;
DE   AltName: Full=Splicing factor 3B-associated 125 kDa protein;
DE            Short=SF3b125;
GN   Name=DDX42;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX   MEDLINE=20193476; PubMed=10727850; DOI=10.1016/S0925-4439(00)00010-7;
RA   Suk K., Kim S., Kim Y.-H., Oh S.-H., Lee M.-K., Kim K.-W., Kim H.-D.,
RA   Seo Y.-S., Lee M.-S.;
RT   "Identification of a novel human member of the DEAD box protein
RT   family.";
RL   Biochim. Biophys. Acta 1501:63-69(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Ikeda A., Tsuritani K.;
RT   "Expression of RNA helicase-related protein in human hair follicle.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Trachea;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Eye, Pancreas, and Uterus;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-938 (ISOFORMS 1/2).
RC   TISSUE=Uterus;
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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2), SUBCELLULAR LOCATION,
RP   AND IDENTIFICATION IN THE SF3B COMPLEX.
RX   MEDLINE=22220069; PubMed=12234937; DOI=10.1093/emboj/cdf480;
RA   Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R.;
RT   "Characterization of novel SF3b and 17S U2 snRNP proteins, including a
RT   human Prp5p homologue and an SF3b DEAD-box protein.";
RL   EMBO J. 21:4978-4988(2002).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; SER-96; SER-109 AND
RP   SER-111, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   FUNCTION, RNA-BINDING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16397294; DOI=10.1093/nar/gkj403;
RA   Uhlmann-Schiffler H., Jalal C., Stahl H.;
RT   "Ddx42p -- a human DEAD box protein with RNA chaperone activities.";
RL   Nucleic Acids Res. 34:10-22(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-109; SER-111;
RP   SER-185 AND SER-754, AND MASS SPECTROMETRY.
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-751 AND
RP   SER-754, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   FUNCTION, INTERACTION WITH TP53BP2, AND SUBCELLULAR LOCATION.
RX   PubMed=19377511; DOI=10.1038/onc.2009.75;
RA   Uhlmann-Schiffler H., Kiermayer S., Stahl H.;
RT   "The DEAD box protein Ddx42p modulates the function of ASPP2, a
RT   stimulator of apoptosis.";
RL   Oncogene 28:2065-2073(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, AND
RP   MASS SPECTROMETRY.
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   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND LYS-5, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [16]
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.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: ATP-dependent RNA helicase. Binds to partially double-
CC       stranded RNAs (dsRNAs) in order to unwind RNA secondary
CC       structures. Unwinding is promoted in the presence of single-strand
CC       binding proteins. Mediates also RNA duplex formation thereby
CC       displacing the single-strand RNA binding protein. ATP and ADP
CC       modulate its activity: ATP binding and hydrolysis by DDX42
CC       triggers RNA strand separation, whereas the ADP-bound form of the
CC       protein triggers annealing of complementary RNA strands. Involved
CC       in the survival of cells by interacting with TP53BP2 and thereby
CC       counteracting the apoptosis-stimulating activity of TP53BP2.
CC       Relocalizes TP53BP2 to the cytoplasm.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Component of splicing factor SF3B which is composed of at
CC       least eight subunits; SF3B1/SAP155/SF3B155, SF3B2/SAP145/SF3B155,
CC       SF3B3/SAP130/SF3B130, SF3B4/SAP49/SF3B49, SF3B14A, PHF5A/SF3B14B,
CC       SF3B10 and SF3B125. Interacts (via the C-terminus) with TP53BP2;
CC       the interaction is not inhibitied by TP53BP2 ubiquitination and is
CC       independent of p53/TP53.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus speckle. Nucleus, Cajal
CC       body. Note=Isoform 2 is present in Cajal bodies (CBs) and nuclear
CC       speckles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q86XP3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86XP3-2; Sequence=VSP_023518;
CC   -!- TISSUE SPECIFICITY: Expressed in several cell lines (at protein
CC       level). Expressed in liver, lung, tonsil, thymus, muscle and
CC       pancreatic islets.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX42
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC32396.1; Type=Frameshift; Positions=818;
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DR   EMBL; AF083255; AAC32396.1; ALT_FRAME; mRNA.
DR   EMBL; AB036090; BAC66466.1; -; mRNA.
DR   EMBL; AK292908; BAF85597.1; -; mRNA.
DR   EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471109; EAW94277.1; -; Genomic_DNA.
DR   EMBL; BC008208; AAH08208.1; -; mRNA.
DR   EMBL; BC015505; AAH15505.1; -; mRNA.
DR   EMBL; BC078667; AAH78667.1; -; mRNA.
DR   EMBL; BC093081; AAH93081.1; -; mRNA.
DR   EMBL; AL050096; CAB43268.1; -; mRNA.
DR   EMBL; BK000566; DAA00077.1; -; mRNA.
DR   IPI; IPI00409671; -.
DR   IPI; IPI00829889; -.
DR   PIR; T08745; T08745.
DR   RefSeq; NP_031398.2; NM_007372.2.
DR   RefSeq; NP_987095.1; NM_203499.1.
DR   UniGene; Hs.702010; -.
DR   HSSP; P09052; 2DB3.
DR   ProteinModelPortal; Q86XP3; -.
DR   SMR; Q86XP3; 230-628.
DR   IntAct; Q86XP3; 4.
DR   MINT; MINT-1427725; -.
DR   STRING; Q86XP3; -.
DR   PhosphoSite; Q86XP3; -.
DR   DMDM; 74750541; -.
DR   PRIDE; Q86XP3; -.
DR   Ensembl; ENST00000359353; ENSP00000352308; ENSG00000198231.
DR   Ensembl; ENST00000389924; ENSP00000374574; ENSG00000198231.
DR   Ensembl; ENST00000457800; ENSP00000390121; ENSG00000198231.
DR   GeneID; 11325; -.
DR   KEGG; hsa:11325; -.
DR   UCSC; uc002jbu.1; human.
DR   CTD; 11325; -.
DR   GeneCards; GC17P061851; -.
DR   H-InvDB; HIX0014072; -.
DR   HGNC; HGNC:18676; DDX42.
DR   HPA; HPA023447; -.
DR   HPA; HPA023571; -.
DR   HPA; HPA025941; -.
DR   MIM; 613369; gene.
DR   neXtProt; NX_Q86XP3; -.
DR   PharmGKB; PA134875761; -.
DR   eggNOG; COG0513; -.
DR   GeneTree; ENSGT00610000086076; -.
DR   HOVERGEN; HBG081425; -.
DR   InParanoid; Q86XP3; -.
DR   KO; K12835; -.
DR   OMA; GANDGRN; -.
DR   OrthoDB; EOG47WNN9; -.
DR   PhylomeDB; Q86XP3; -.
DR   NextBio; 43019; -.
DR   ArrayExpress; Q86XP3; -.
DR   Bgee; Q86XP3; -.
DR   CleanEx; HS_DDX42; -.
DR   Genevestigator; Q86XP3; -.
DR   GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR   GO; GO:0045767; P:regulation of anti-apoptosis; IMP:UniProtKB.
DR   InterPro; IPR014001; DEAD-like_helicase.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
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   PROSITE; PS00039; DEAD_ATP_HELICASE; 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; Coiled coil;
KW   Complete proteome; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN         1    938       ATP-dependent RNA helicase DDX42.
FT                                /FTId=PRO_0000280058.
FT   DOMAIN      284    459       Helicase ATP-binding.
FT   DOMAIN      487    632       Helicase C-terminal.
FT   NP_BIND     297    304       ATP (By similarity).
FT   REGION      738    833       Necessary for interaction with TP53BP2.
FT   COILED      116    157       Potential.
FT   MOTIF       253    281       Q motif.
FT   MOTIF       407    410       DEAD box.
FT   COMPBIAS     43     46       Poly-Ser.
FT   COMPBIAS    175    178       Poly-Glu.
FT   COMPBIAS    654    659       Poly-Gly.
FT   COMPBIAS    762    883       Gly-rich.
FT   COMPBIAS    819    871       His-rich.
FT   MOD_RES       1      1       N-acetylmethionine.
FT   MOD_RES       5      5       N6-acetyllysine.
FT   MOD_RES      10     10       Phosphothreonine.
FT   MOD_RES      96     96       Phosphoserine.
FT   MOD_RES     104    104       Phosphoserine.
FT   MOD_RES     109    109       Phosphoserine.
FT   MOD_RES     111    111       Phosphoserine.
FT   MOD_RES     185    185       Phosphoserine.
FT   MOD_RES     751    751       Phosphoserine.
FT   MOD_RES     754    754       Phosphoserine.
FT   VAR_SEQ       1    119       Missing (in isoform 2).
FT                                /FTId=VSP_023518.
SQ   SEQUENCE   938 AA;  102975 MW;  D89A252E095D8913 CRC64;
     MNWNKGGPGT KRGFGFGGFA ISAGKKEEPK LPQQSHSAFG ATSSSSGFGK SAPPQLPSFY
     KIGSKRANFD EENAYFEDEE EDSSNVDLPY IPAENSPTRQ QFHSKPVDSD SDDDPLEAFM
     AEVEDQAARD MKRLEEKDKE RKNVKGIRDD IEEEDDQEAY FRYMAENPTA GVVQEEEEDN
     LEYDSDGNPI APTKKIIDPL PPIDHSEIDY PPFEKNFYNE HEEITNLTPQ QLIDLRHKLN
     LRVSGAAPPR PGSSFAHFGF DEQLMHQIRK SEYTQPTPIQ CQGVPVALSG RDMIGIAKTG
     SGKTAAFIWP MLIHIMDQKE LEPGDGPIAV IVCPTRELCQ QIHAECKRFG KAYNLRSVAV
     YGGGSMWEQA KALQEGAEIV VCTPGRLIDH VKKKATNLQR VSYLVFDEAD RMFDMGFEYQ
     VRSIASHVRP DRQTLLFSAT FRKKIEKLAR DILIDPIRVV QGDIGEANED VTQIVEILHS
     GPSKWNWLTR RLVEFTSSGS VLLFVTKKAN AEELANNLKQ EGHNLGLLHG DMDQSERNKV
     ISDFKKKDIP VLVATDVAAR GLDIPSIKTV INYDVARDID THTHRIGRTG RAGEKGVAYT
     LLTPKDSNFA GDLVRNLEGA NQHVSKELLD LAMQNAWFRK SRFKGGKGKK LNIGGGGLGY
     RERPGLGSEN MDRGNNNVMS NYEAYKPSTG AMGDRLTAMK AAFQSQYKSH FVAASLSNQK
     AGSSAAGASG WTSAGSLNSV PTNSAQQGHN SPDSPVTSAA KGIPGFGNTG NISGAPVTYP
     SAGAQGVNNT ASGNNSREGT GGSNGKRERY TENRGSSRHS HGETGNRHSD SPRHGDGGRH
     GDGYRHPESS SRHTDGHRHG ENRHGGSAGR HGENRGANDG RNGESRKEAF NRESKMEPKM
     EPKVDSSKMD KVDSKTDKTA DGFAVPEPPK RKKSRWDS
//