GenomeNet

Database: UniProt
Entry: Q7L014
LinkDB: Q7L014
Original site: Q7L014 
ID   DDX46_HUMAN             Reviewed;        1031 AA.
AC   Q7L014; O94894; Q96EI0; Q9Y658;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   16-OCT-2019, entry version 158.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX46;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 46;
DE   AltName: Full=PRP5 homolog;
GN   Name=DDX46; Synonyms=KIAA0801;
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].
RC   TISSUE=Pituitary tumor;
RA   Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA   Luo M., Chen J., Hu R.;
RT   "Human RNA helicase gene.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XI.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 5:277-286(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-804, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-294; SER-295; SER-296
RP   AND SER-804, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-294; SER-295; SER-296
RP   AND SER-804, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-263 AND LYS-776, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-804, AND IDENTIFICATION
RP   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
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).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-804, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; SER-804 AND
RP   SER-928, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=25255805; DOI=10.1038/ncomms5919;
RA   Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
RA   Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT   "Global profiling of co- and post-translationally N-myristoylated
RT   proteomes in human cells.";
RL   Nat. Commun. 5:4919-4919(2014).
RN   [16]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-186, AND IDENTIFICATION BY
RP   MASS 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   [17]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-186, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [18]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-186; LYS-325; LYS-779;
RP   LYS-907 AND LYS-915, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: Plays an essential role in splicing, either prior to, or
CC       during splicing A complex formation.
CC       {ECO:0000269|PubMed:12234937}.
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: Integral component of the 17S U2 snRNP.
CC       {ECO:0000269|PubMed:12234937}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle
CC       {ECO:0000269|PubMed:12234937}. Nucleus, Cajal body
CC       {ECO:0000269|PubMed:12234937}. Membrane {ECO:0000305}; Lipid-
CC       anchor {ECO:0000305}. Note=Present in Cajal bodies (CBs) and
CC       nuclear speckles.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA34521.2; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AF106680; AAD43033.1; -; mRNA.
DR   EMBL; AB018344; BAA34521.2; ALT_INIT; mRNA.
DR   EMBL; BC012304; AAH12304.1; -; mRNA.
DR   EMBL; BK000565; DAA00076.1; -; mRNA.
DR   CCDS; CCDS34240.1; -.
DR   RefSeq; NP_001287789.1; NM_001300860.1.
DR   RefSeq; NP_055644.2; NM_014829.3.
DR   SMR; Q7L014; -.
DR   BioGrid; 115210; 67.
DR   CORUM; Q7L014; -.
DR   IntAct; Q7L014; 26.
DR   MINT; Q7L014; -.
DR   STRING; 9606.ENSP00000416534; -.
DR   iPTMnet; Q7L014; -.
DR   PhosphoSitePlus; Q7L014; -.
DR   SwissPalm; Q7L014; -.
DR   BioMuta; DDX46; -.
DR   DMDM; 116241326; -.
DR   EPD; Q7L014; -.
DR   jPOST; Q7L014; -.
DR   MassIVE; Q7L014; -.
DR   MaxQB; Q7L014; -.
DR   PaxDb; Q7L014; -.
DR   PeptideAtlas; Q7L014; -.
DR   PRIDE; Q7L014; -.
DR   ProteomicsDB; 68726; -.
DR   Ensembl; ENST00000354283; ENSP00000346236; ENSG00000145833.
DR   GeneID; 9879; -.
DR   KEGG; hsa:9879; -.
DR   UCSC; uc003kzw.5; human.
DR   CTD; 9879; -.
DR   DisGeNET; 9879; -.
DR   GeneCards; DDX46; -.
DR   HGNC; HGNC:18681; DDX46.
DR   HPA; HPA036554; -.
DR   HPA; HPA057501; -.
DR   MIM; 617848; gene.
DR   neXtProt; NX_Q7L014; -.
DR   OpenTargets; ENSG00000145833; -.
DR   PharmGKB; PA134894452; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   eggNOG; ENOG410XSQV; LUCA.
DR   GeneTree; ENSGT00940000157753; -.
DR   HOGENOM; HOG000007229; -.
DR   InParanoid; Q7L014; -.
DR   KO; K12811; -.
DR   OrthoDB; 245118at2759; -.
DR   PhylomeDB; Q7L014; -.
DR   TreeFam; TF354236; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   ChiTaRS; DDX46; human.
DR   GeneWiki; DDX46; -.
DR   GenomeRNAi; 9879; -.
DR   Pharos; Q7L014; -.
DR   PMAP-CutDB; Q7L014; -.
DR   PRO; PR:Q7L014; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000145833; Expressed in 233 organ(s), highest expression level in lung.
DR   ExpressionAtlas; Q7L014; baseline and differential.
DR   Genevisible; Q7L014; HS.
DR   GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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; 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   SUPFAM; SSF52540; SSF52540; 2.
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; ATP-binding; Coiled coil; Complete proteome; Helicase;
KW   Hydrolase; Isopeptide bond; Lipoprotein; Membrane; mRNA processing;
KW   mRNA splicing; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; RNA-binding; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:25255805}.
FT   CHAIN         2   1031       Probable ATP-dependent RNA helicase
FT                                DDX46.
FT                                /FTId=PRO_0000055121.
FT   DOMAIN      403    581       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      592    753       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     416    423       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED      152    197       {ECO:0000255}.
FT   MOTIF       372    400       Q motif.
FT   MOTIF       529    532       DEAD box.
FT   COMPBIAS      3    103       Arg-rich.
FT   COMPBIAS    202    209       Poly-Asp.
FT   MOD_RES     199    199       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q62780}.
FT   MOD_RES     263    263       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     294    294       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332}.
FT   MOD_RES     295    295       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332}.
FT   MOD_RES     296    296       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332}.
FT   MOD_RES     346    346       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     776    776       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     804    804       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     903    903       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q569Z5}.
FT   MOD_RES     928    928       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   LIPID         2      2       N-myristoyl glycine.
FT                                {ECO:0000269|PubMed:25255805}.
FT   CROSSLNK    186    186       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    325    325       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    779    779       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    907    907       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    915    915       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VARIANT     207    207       E -> Q (in dbSNP:rs10447293).
FT                                /FTId=VAR_028079.
FT   CONFLICT    109    109       N -> S (in Ref. 1; AAD43033).
FT                                {ECO:0000305}.
FT   CONFLICT    114    114       T -> A (in Ref. 1; AAD43033).
FT                                {ECO:0000305}.
FT   CONFLICT    124    125       TD -> AE (in Ref. 1; AAD43033).
FT                                {ECO:0000305}.
FT   CONFLICT    128    128       E -> D (in Ref. 1; AAD43033).
FT                                {ECO:0000305}.
FT   CONFLICT    222    222       G -> D (in Ref. 1; AAD43033).
FT                                {ECO:0000305}.
FT   CONFLICT    251    251       G -> A (in Ref. 1; AAD43033).
FT                                {ECO:0000305}.
FT   CONFLICT    447    447       I -> L (in Ref. 1; AAD43033).
FT                                {ECO:0000305}.
FT   CONFLICT    462    469       TKECKKFS -> PKGVRSF (in Ref. 1;
FT                                AAD43033). {ECO:0000305}.
FT   CONFLICT    870    870       Q -> QV (in Ref. 1; AAD43033 and 2;
FT                                BAA34521). {ECO:0000305}.
SQ   SEQUENCE   1031 AA;  117362 MW;  52535164FEB48A72 CRC64;
     MGRESRHYRK RSASRGRSGS RSRSRSPSDK RSKRGDDRRS RSRDRDRRRE RSRSRDKRRS
     RSRDRKRLRR SRSRERDRSR ERRRSRSRDR RRSRSRSRGR RSRSSSPGNK SKKTENRSRS
     KEKTDGGESS KEKKKDKDDK EDEKEKDAGN FDQNKLEEEM RKRKERVEKW REEQRKKAME
     NIGELKKEIE EMKQGKKWSL EDDDDDEDDP AEAEKEGNEM EGEELDPLDA YMEEVKEEVK
     KFNMRSVKGG GGNEKKSGPT VTKVVTVVTT KKAVVDSDKK KGELMENDQD AMEYSSEEEE
     VDLQTALTGY QTKQRKLLEP VDHGKIEYEP FRKNFYVEVP ELAKMSQEEV NVFRLEMEGI
     TVKGKGCPKP IKSWVQCGIS MKILNSLKKH GYEKPTPIQT QAIPAIMSGR DLIGIAKTGS
     GKTIAFLLPM FRHIMDQRSL EEGEGPIAVI MTPTRELALQ ITKECKKFSK TLGLRVVCVY
     GGTGISEQIA ELKRGAEIIV CTPGRMIDML AANSGRVTNL RRVTYVVLDE ADRMFDMGFE
     PQVMRIVDNV RPDRQTVMFS ATFPRAMEAL ARRILSKPIE VQVGGRSVVC SDVEQQVIVI
     EEEKKFLKLL ELLGHYQESG SVIIFVDKQE HADGLLKDLM RASYPCMSLH GGIDQYDRDS
     IINDFKNGTC KLLVATSVAA RGLDVKHLIL VVNYSCPNHY EDYVHRAGRT GRAGNKGYAY
     TFITEDQARY AGDIIKALEL SGTAVPPDLE KLWSDFKDQQ KAEGKIIKKS SGFSGKGFKF
     DETEQALANE RKKLQKAALG LQDSDDEDAA VDIDEQIESM FNSKKRVKDM AAPGTSSVPA
     PTAGNAEKLE IAKRLALRIN AQKNLGIESQ DVMQQATNAI LRGGTILAPT VSAKTIAEQL
     AEKINAKLNY VPLEKQEEER QDGGQNESFK RYEEELEIND FPQTARWKVT SKEALQRISE
     YSEAAITIRG TYFPPGKEPK EGERKIYLAI ESANELAVQK AKAEITRLIK EELIRLQNSY
     QPTNKGRYKV L
//
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