GenomeNet

Database: UniProt
Entry: Q91VR5
LinkDB: Q91VR5
Original site: Q91VR5 
ID   DDX1_MOUSE              Reviewed;         740 AA.
AC   Q91VR5; Q3TU41;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   13-NOV-2019, entry version 161.
DE   RecName: Full=ATP-dependent RNA helicase DDX1;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 1;
GN   Name=Ddx1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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   [3]
RP   INTERACTION WITH PHF5A.
RX   PubMed=18758164; DOI=10.1159/000138890;
RA   Rzymski T., Grzmil P., Meinhardt A., Wolf S., Burfeind P.;
RT   "PHF5A represents a bridge protein between splicing proteins and ATP-
RT   dependent helicases and is differentially expressed during mouse
RT   spermatogenesis.";
RL   Cytogenet. Genome Res. 121:232-244(2008).
RN   [4]
RP   FUNCTION, DNA-BINDING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=19398953; DOI=10.1038/onc.2009.89;
RA   Tanaka K., Okamoto S., Ishikawa Y., Tamura H., Hara T.;
RT   "DDX1 is required for testicular tumorigenesis, partially through the
RT   transcriptional activation of 12p stem cell genes.";
RL   Oncogene 28:2142-2151(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   FUNCTION, INTERACTION WITH DDX21 AND DHX36, IDENTIFICATION IN A
RP   COMPLEX WITH DDX21; DHX36 AND TICAM1, DOUBLE-STRANDED RNA-BINDING,
RP   IDENTIFICATION BY MASS SPECTROMETRY, REGION DOUBLE-STRANDED
RP   RNA-BINDING DOMAIN, AND SUBCELLULAR LOCATION.
RX   PubMed=21703541; DOI=10.1016/j.immuni.2011.03.027;
RA   Zhang Z., Kim T., Bao M., Facchinetti V., Jung S.Y., Ghaffari A.A.,
RA   Qin J., Cheng G., Liu Y.J.;
RT   "DDX1, DDX21, and DHX36 helicases form a complex with the adaptor
RT   molecule TRIF to sense dsRNA in dendritic cells.";
RL   Immunity 34:866-878(2011).
CC   -!- FUNCTION: Acts as an ATP-dependent RNA helicase, able to unwind
CC       both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded
CC       RNA overhang nuclease activity. Possesses ATPase activity on
CC       various RNA, but not DNA polynucleotides. May play a role in RNA
CC       clearance at DNA double-strand breaks (DSBs), thereby facilitating
CC       the template-guided repair of transcriptionally active regions of
CC       the genome. Together with RELA, acts as a coactivator to enhance
CC       NF-kappa-B-mediated transcriptional activation (By similarity).
CC       Acts as a positive transcriptional regulator of cyclin CCND2
CC       expression (PubMed:19398953). Binds to the cyclin CCND2 promoter
CC       region (PubMed:19398953). Associates with chromatin at the NF-
CC       kappa-B promoter region via association with RELA. Binds to
CC       poly(A) RNA. May be involved in 3'-end cleavage and
CC       polyadenylation of pre-mRNAs. Component of the tRNA-splicing
CC       ligase complex required to facilitate the enzymatic turnover of
CC       catalytic subunit RTCB: together with archease (ZBTB8OS), acts by
CC       facilitating the guanylylation of RTCB, a key intermediate step in
CC       tRNA ligation (By similarity). Component of a multi-helicase-
CC       TICAM1 complex that acts as a cytoplasmic sensor of viral double-
CC       stranded RNA (dsRNA) and plays a role in the activation of a
CC       cascade of antiviral responses including the induction of
CC       proinflammatory cytokines via the adapter molecule TICAM1
CC       (PubMed:21703541). Specifically binds (via helicase ATP-binding
CC       domain) on both short and long poly(I:C) dsRNA (PubMed:21703541).
CC       {ECO:0000250|UniProtKB:Q92499, ECO:0000269|PubMed:19398953,
CC       ECO:0000269|PubMed:21703541}.
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: Found in a multi-helicase-TICAM1 complex at least
CC       composed of DHX36, DDX1, DDX21 and TICAM1; this complex exists in
CC       resting cells with or without poly(I:C) RNA ligand stimulation
CC       (PubMed:21703541). Interacts with DHX36 (PubMed:21703541).
CC       Interacts (via B30.2/SPRY domain) with DDX21 (via N-terminus);
CC       this interaction serves as bridges to TICAM1 (PubMed:21703541).
CC       Interacts with FAM98A (via N- and C-terminus) (By similarity).
CC       Interacts with MBNL1 (By similarity). Interacts with CSTF2 (By
CC       similarity). Interacts with HNRNPK (By similarity). Interacts with
CC       ATM (By similarity). Interacts with RELA (via C-terminus) (By
CC       similarity). Component of the tRNA-splicing ligase complex (By
CC       similarity). Interacts with PHF5A (via C-terminus)
CC       (PubMed:18758164). Interacts with PQBP1 (By similarity). Interacts
CC       with ERCC6 (By similarity). {ECO:0000250|UniProtKB:Q92499,
CC       ECO:0000269|PubMed:18758164, ECO:0000269|PubMed:21703541}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92499}.
CC       Cytoplasm, cytosol {ECO:0000269|PubMed:21703541}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q92499}. Cytoplasmic granule
CC       {ECO:0000250|UniProtKB:Q92499}. Mitochondrion
CC       {ECO:0000269|PubMed:21703541}. Note=Localized with MBNL1, TIAL1
CC       and YBX1 in stress granules upon stress. Localized with CSTF2 in
CC       cleavage bodies. Forms large aggregates called DDX1 bodies.
CC       Relocalized into multiple foci (IR-induced foci or IRIF) after IR
CC       treatment, a process that depends on the presence of chromosomal
CC       DNA and/or RNA-DNA duplexes. Relocalized at sites of DNA double-
CC       strand breaks (DSBs) in an ATM-dependent manner after IR
CC       treatment. Colocalized with RELA in the nucleus upon TNF-alpha
CC       induction. Enters into the nucleus in case of active transcription
CC       while it accumulates in cytosol when transcription level is low
CC       (By similarity). Colocalizes in the cytosol with DDX21, DHX36 and
CC       TICAM1 (PubMed:21703541). Colocalizes in the mitochondria with
CC       TICAM1 and poly(I:C) RNA ligand (PubMed:21703541). The multi-
CC       helicase-TICAM1 complex may translocate to the mitochondria upon
CC       poly(I:C) stimulation (PubMed:21703541).
CC       {ECO:0000250|UniProtKB:Q92499, ECO:0000269|PubMed:21703541}.
CC   -!- TISSUE SPECIFICITY: Testis-specific. Expressed in the germ line
CC       stem cells, spermatogonia and spermatocytes of the testis. Also
CC       expressed in the seminoma and nonseminoma types of testicular germ
CC       cell tumors (TGCTs) (at protein level).
CC       {ECO:0000269|PubMed:19398953}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the testis from 11.5 to 19.5
CC       dpc. {ECO:0000269|PubMed:19398953}.
CC   -!- DOMAIN: The helicase domain is involved in the stimulation of RELA
CC       transcriptional activity. {ECO:0000250|UniProtKB:Q92499}.
CC   -!- PTM: Phosphorylated by ATM kinase; phosphorylation is increased in
CC       response to ionizing radiation (IR).
CC       {ECO:0000250|UniProtKB:Q92499}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX1
CC       subfamily. {ECO:0000305}.
DR   EMBL; AK028341; BAC25893.1; -; mRNA.
DR   EMBL; AK153335; BAE31914.1; -; mRNA.
DR   EMBL; AK160982; BAE36130.1; -; mRNA.
DR   EMBL; BC010624; AAH10624.1; -; mRNA.
DR   CCDS; CCDS25819.1; -.
DR   RefSeq; NP_598801.1; NM_134040.1.
DR   BioGrid; 222684; 10.
DR   IntAct; Q91VR5; 5.
DR   MINT; Q91VR5; -.
DR   STRING; 10090.ENSMUSP00000065987; -.
DR   iPTMnet; Q91VR5; -.
DR   PhosphoSitePlus; Q91VR5; -.
DR   SwissPalm; Q91VR5; -.
DR   REPRODUCTION-2DPAGE; Q91VR5; -.
DR   EPD; Q91VR5; -.
DR   jPOST; Q91VR5; -.
DR   MaxQB; Q91VR5; -.
DR   PaxDb; Q91VR5; -.
DR   PeptideAtlas; Q91VR5; -.
DR   PRIDE; Q91VR5; -.
DR   Ensembl; ENSMUST00000071103; ENSMUSP00000065987; ENSMUSG00000037149.
DR   GeneID; 104721; -.
DR   KEGG; mmu:104721; -.
DR   UCSC; uc007nbh.1; mouse.
DR   CTD; 1653; -.
DR   MGI; MGI:2144727; Ddx1.
DR   eggNOG; KOG0349; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   GeneTree; ENSGT00940000155678; -.
DR   HOGENOM; HOG000251633; -.
DR   InParanoid; Q91VR5; -.
DR   KO; K13177; -.
DR   OMA; DGVHDRD; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q91VR5; -.
DR   TreeFam; TF106114; -.
DR   ChiTaRS; Ddx1; mouse.
DR   PRO; PR:Q91VR5; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   Bgee; ENSMUSG00000037149; Expressed in 299 organ(s), highest expression level in metanephric ureteric bud.
DR   ExpressionAtlas; Q91VR5; baseline and differential.
DR   Genevisible; Q91VR5; MM.
DR   GO; GO:0071920; C:cleavage body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR   GO; GO:0072669; C:tRNA-splicing ligase complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0033677; F:DNA/RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; ISS:UniProtKB.
DR   GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organism development; IEA:Ensembl.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; ISO:MGI.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR   GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; IMP:UniProtKB.
DR   GO; GO:1903608; P:protein localization to cytoplasmic stress granule; ISO:MGI.
DR   GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
DR   GO; GO:0009615; P:response to virus; IMP:MGI.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; ISS:UniProtKB.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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; IPR003877; SPRY_dom.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Antiviral defense; ATP-binding;
KW   Complete proteome; Cytoplasm; DNA-binding; Exonuclease; Helicase;
KW   Hydrolase; Immunity; Innate immunity; Isopeptide bond; Mitochondrion;
KW   mRNA processing; Nuclease; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding; Transcription;
KW   Transcription regulation; tRNA processing; Ubl conjugation.
FT   CHAIN         1    740       ATP-dependent RNA helicase DDX1.
FT                                /FTId=PRO_0000054987.
FT   DOMAIN        2    428       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN       70    247       B30.2/SPRY. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   DOMAIN      493    681       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      46     53       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        1    525       Necessary for interaction with RELA.
FT                                {ECO:0000250|UniProtKB:Q92499}.
FT   REGION        1    448       Interaction with dsRNA.
FT                                {ECO:0000269|PubMed:21703541}.
FT   REGION        1    295       Necessary for interaction with HNRNPK.
FT                                {ECO:0000250|UniProtKB:Q92499}.
FT   REGION      525    740       Necessary for interaction with HNRNPK.
FT                                {ECO:0000250|UniProtKB:Q92499}.
FT   MOTIF       370    373       DEAD box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOD_RES     239    239       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q92499}.
FT   MOD_RES     268    268       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q92499}.
FT   MOD_RES     281    281       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q92499}.
FT   MOD_RES     481    481       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CROSSLNK    281    281       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q92499}.
SQ   SEQUENCE   740 AA;  82500 MW;  76457FBB75A3CEC2 CRC64;
     MAAFSEMGVM PEIAQAVEEM DWLLPTDIQA ESIPLILGGG DVLMAAETGS GKTGAFSIPV
     IQIVYETLKD QQEGKKGKTT IKTGASVLNK WQMNPYDRGS AFAIGSDGLC CQSREVKEWH
     GCRGTRGLLK GKHYYEVSCH DQGLCRVGWS TMQASLDLGT DKFGFGFGGT GKKSHNKQFD
     NYGEEFTMHD TIGCYLDIDK GHVKFSKNGK DLGLAFEIPA HIKNQALFPA CVLKNAELKF
     NFGEEEFKFP PKDGFVALSK APDNYIVKSQ HTGNAQVSQT KFLPNAPKAL IVEPSRELAE
     QTLNNVKQFK KYIDNPKLRE LLIIGGVAAR DQLSVLDNGV DIVVGTPGRL DDLVSTGKLN
     LSQVRFLVLD EADGLLSQGY SDFINRMHNQ IPQITCDGKR LQVIVCSATL HSFDVKKLSE
     KIMHFPTWVD LKGEDSVPDT VHHVVVPVNP KTDKLWERLG KNHIRTDDVH AKDNTRPGAN
     SPEMWSEAIK ILKGEYAVRA IKEHKMDQAI IFCRTKIDCD NLEQYFMQQG GGPDKKGHQF
     SCVCLHGDRK PHERKQNLER FKKGDVRFLI CTDVAARGID IHGVPYVINV TLPDEKQNYV
     HRIGRVGRAE RMGLAISLVA TEKEKVWYHV CSNRGKGCYN TRLKEDGGCT IWYNEMQLLS
     EIEEHLNCTI SQVEPDIKVP VDEFDGKVTY GQKRAAGGGN YKGHVDVLAP TVQELAALEK
     EAQTSFLHLG YLPNQLFRTF
//
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