GenomeNet

Database: UniProt
Entry: Q8K1P7
LinkDB: Q8K1P7
Original site: Q8K1P7 
ID   SMCA4_RAT               Reviewed;        1613 AA.
AC   Q8K1P7;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   31-JUL-2019, entry version 122.
DE   RecName: Full=Transcription activator BRG1;
DE            EC=3.6.4.-;
DE   AltName: Full=ATP-dependent helicase SMARCA4;
DE   AltName: Full=BRG1-associated factor 190A;
DE            Short=BAF190A;
DE   AltName: Full=Protein brahma homolog 1;
DE   AltName: Full=SNF2-beta;
DE   AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4;
GN   Name=Smarca4; Synonyms=Baf190a, Brg1, Snf2b, Snf2l4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Hippocampus;
RA   Hirsch O., Almeida O.F.X.;
RT   "Isolation and characterization of the rat brahma related gene-1 (BRG-
RT   1).";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND INTERACTION WITH SS18L1; HDAC1; RB1 AND SP1.
RX   PubMed=19081374; DOI=10.1016/j.neuron.2008.09.040;
RA   Qiu Z., Ghosh A.;
RT   "A calcium-dependent switch in a CREST-BRG1 complex regulates
RT   activity-dependent gene expression.";
RL   Neuron 60:775-787(2008).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-695; SER-699;
RP   SER-1419; SER-1536; SER-1541; SER-1552; SER-1593 AND SER-1597, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Involved in transcriptional activation and repression of
CC       select genes by chromatin remodeling (alteration of DNA-nucleosome
CC       topology). Component of SWI/SNF chromatin remodeling complexes
CC       that carry out key enzymatic activities, changing chromatin
CC       structure by altering DNA-histone contacts within a nucleosome in
CC       an ATP-dependent manner. Component of the CREST-BRG1 complex, a
CC       multiprotein complex that regulates promoter activation by
CC       orchestrating the calcium-dependent release of a repressor complex
CC       and the recruitment of an activator complex. In resting neurons,
CC       transcription of the c-FOS promoter is inhibited by SMARCA4-
CC       dependent recruitment of a phospho-RB1-HDAC repressor complex.
CC       Upon calcium influx, RB1 is dephosphorylated by calcineurin, which
CC       leads to release of the repressor complex. At the same time, there
CC       is increased recruitment of CREBBP to the promoter by a CREST-
CC       dependent mechanism, which leads to transcriptional activation.
CC       The CREST-BRG1 complex also binds to the NR2B promoter, and
CC       activity-dependent induction of NR2B expression involves the
CC       release of HDAC1 and recruitment of CREBBP. Belongs to the neural
CC       progenitors-specific chromatin remodeling complex (npBAF complex)
CC       and the neuron-specific chromatin remodeling complex (nBAF
CC       complex). During neural development, a switch from a
CC       stem/progenitor to a postmitotic chromatin remodeling mechanism
CC       occurs as neurons exit the cell cycle and become committed to
CC       their adult state. The transition from proliferating neural
CC       stem/progenitor cells to postmitotic neurons requires a switch in
CC       subunit composition of the npBAF and nBAF complexes. As neural
CC       progenitors exit mitosis and differentiate into neurons, npBAF
CC       complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are
CC       exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
CC       or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The
CC       npBAF complex is essential for the self-renewal/proliferative
CC       capacity of the multipotent neural stem cells. The nBAF complex
CC       along with CREST plays a role regulating the activity of genes
CC       essential for dendrite growth. SMARCA4/BAF190A may promote neural
CC       stem cell self-renewal/proliferation by enhancing Notch-dependent
CC       proliferative signals, while concurrently making the neural stem
CC       cell insensitive to SHH-dependent differentiating cues. Acts as a
CC       corepressor of ZEB1 to regulate E-cadherin transcription and is
CC       required for induction of epithelial-mesenchymal transition (EMT)
CC       by ZEB1 (By similarity). Binds via DLX1 to enhancers located in
CC       the intergenic region between DLX5 and DLX6 and this binding is
CC       stabilized by the long non-coding RNA (lncRNA) Evf2 (By
CC       similarity). Binds to RNA in a promiscuous manner (By similarity).
CC       Binding to RNAs including lncRNA Evf2 leads to inhibition of
CC       SMARCA4 ATPase and chromatin remodeling activities (By
CC       similarity). {ECO:0000250|UniProtKB:P51532,
CC       ECO:0000250|UniProtKB:Q3TKT4, ECO:0000269|PubMed:19081374}.
CC   -!- SUBUNIT: Component of the multiprotein chromatin-remodeling
CC       complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related
CC       complexes. The canonical complex contains a catalytic subunit
CC       (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least
CC       SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
CC       SMARCB1/SNF5/BAF47. Other subunits specific to each of the
CC       complexes may also be present permitting several possible
CC       developmental- and tissue-specific combinations. Component of the
CC       BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A,
CC       ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53,
CC       ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170,
CC       SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B,
CC       or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains
CC       DPF3. Component of neural progenitors-specific chromatin
CC       remodeling complex (npBAF complex) composed of at least,
CC       ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC       SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC       SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A,
CC       ACTL6A/BAF53A and actin. Component of neuron-specific chromatin
CC       remodeling complex (nBAF complex) composed of at least,
CC       ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC       SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC       SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC       DPF3/BAF45C, ACTL6B/BAF53B and actin. Component of the SWI/SNF-B
CC       (PBAF) chromatin remodeling complex, at least composed of
CC       SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B,
CC       SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps
CC       SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180,
CC       ARID2/BAF200 and actin. Component of SWI/SNF (GBAF) subcomplex,
CC       which includes at least BICRA or BICRAL (mutually exclusive),
CC       BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53,
CC       SMARCC1/BAF155, and SMARCD1/BAF60A. Component of the BAF53
CC       complex, at least composed of BAF53A, RUVBL1,
CC       SMARCA4/BRG1/BAF190A, and TRRAP, which preferentially acetylates
CC       histone H4 (and H2A) within nucleosomes (By similarity). Component
CC       of the CREST-BRG1 complex, at least composed of
CC       SMARCA4/BRG1/BAF190A, SS18L1/CREST, HDAC1, RB1 and SP1 (By
CC       similarity). Interacts with PHF10/BAF45A (By similarity).
CC       Interacts with MYOG (By similarity). Interacts directly with
CC       IKFZ1; the interaction associates IKFZ1 with the BAF complex.
CC       Interacts with ZEB1 (via N-terminus). Interacts with NR3C1, PGR,
CC       SMARD1, TOPBP1 and ZMIM2/ZIMP7. Interacts with (via the
CC       bromodomain) with TERT; the interaction regulates Wnt-mediated
CC       signaling (By similarity). Interacts with TBX21 in a KDM6B-
CC       dependent manner (By similarity). Interacts with KDM6A and KDM6B
CC       (By similarity). Interacts with HNRNPU; this interaction occurs in
CC       embryonic stem cells and stimulates global Pol II-mediated
CC       transcription (By similarity). Interacts with ACTL6A (By
CC       similarity). Interacts with DLX1 (By similarity). Interacts with
CC       DPF2 (By similarity). {ECO:0000250|UniProtKB:P51532,
CC       ECO:0000250|UniProtKB:Q3TKT4}.
CC   -!- INTERACTION:
CC       G3V612:Olig2; NbExp=2; IntAct=EBI-689301, EBI-6676662;
CC       Q12824:SMARCB1 (xeno); NbExp=2; IntAct=EBI-689301, EBI-358419;
CC       Q4KLI0:Smarcb1; NbExp=2; IntAct=EBI-689301, EBI-689316;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3TKT4}.
CC       Note=Colocalizes with long non-coding RNA Evf2 in nuclear RNA
CC       clouds. {ECO:0000250|UniProtKB:Q3TKT4}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
DR   EMBL; AJ504723; CAD43278.1; -; mRNA.
DR   SMR; Q8K1P7; -.
DR   IntAct; Q8K1P7; 4.
DR   STRING; 10116.ENSRNOP00000013166; -.
DR   iPTMnet; Q8K1P7; -.
DR   PhosphoSitePlus; Q8K1P7; -.
DR   jPOST; Q8K1P7; -.
DR   PaxDb; Q8K1P7; -.
DR   PRIDE; Q8K1P7; -.
DR   UCSC; RGD:621728; rat.
DR   RGD; 621728; Smarca4.
DR   eggNOG; KOG0386; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   eggNOG; COG5076; LUCA.
DR   HOGENOM; HOG000172363; -.
DR   InParanoid; Q8K1P7; -.
DR   PhylomeDB; Q8K1P7; -.
DR   Reactome; R-RNO-1266695; Interleukin-7 signaling.
DR   Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-RNO-3214858; RMTs methylate histone arginines.
DR   Reactome; R-RNO-3247509; Chromatin modifying enzymes.
DR   Reactome; R-RNO-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR   PRO; PR:Q8K1P7; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR   GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:RGD.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006337; P:nucleosome disassembly; IDA:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; IEP:RGD.
DR   Gene3D; 1.20.920.10; -; 1.
DR   Gene3D; 2.20.28.130; -; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR030100; BRG1.
DR   InterPro; IPR006576; BRK_domain.
DR   InterPro; IPR037259; BRK_sf.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029295; SnAC.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF76; PTHR10799:SF76; 1.
DR   Pfam; PF07533; BRK; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF08880; QLQ; 1.
DR   Pfam; PF14619; SnAC; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00592; BRK; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00573; HSA; 1.
DR   SMART; SM00951; QLQ; 1.
DR   SMART; SM01314; SnAC; 1.
DR   SUPFAM; SSF160481; SSF160481; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
DR   PROSITE; PS51666; QLQ; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; ATP-binding; Bromodomain; Chromatin regulator;
KW   Complete proteome; Helicase; Hydrolase; Isopeptide bond; Neurogenesis;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; RNA-binding; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN         1   1613       Transcription activator BRG1.
FT                                /FTId=PRO_0000391344.
FT   DOMAIN      171    206       QLQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01001}.
FT   DOMAIN      460    532       HSA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00549}.
FT   DOMAIN      766    931       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1084   1246       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     1443   1513       Bromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00035}.
FT   NP_BIND     779    786       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        1    282       Necessary for interaction with
FT                                SS18L1/CREST.
FT                                {ECO:0000269|PubMed:19081374}.
FT   REGION      462    728       RNA-binding region which is sufficient
FT                                for binding to lncRNA Evf2.
FT                                {ECO:0000250|UniProtKB:Q3TKT4}.
FT   REGION      837    916       Sufficient for interaction with DLX1.
FT                                {ECO:0000250|UniProtKB:Q3TKT4}.
FT   REGION     1247   1413       Sufficient for interaction with DLX1.
FT                                {ECO:0000250|UniProtKB:Q3TKT4}.
FT   MOTIF       881    884       DEGH box. {ECO:0000250}.
FT   COMPBIAS    663    672       Poly-Glu.
FT   COMPBIAS   1252   1370       Glu-rich.
FT   COMPBIAS   1531   1555       Glu-rich.
FT   SITE       1505   1506       Required for binding to 'Lys-15'-
FT                                acetylated histone 3. {ECO:0000250}.
FT   MOD_RES      11     11       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES     188    188       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES     353    353       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES     609    609       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES     610    610       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES     613    613       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     626    626       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q6DIC0}.
FT   MOD_RES     695    695       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     699    699       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1349   1349       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES    1390   1390       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q3TKT4}.
FT   MOD_RES    1419   1419       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1536   1536       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1541   1541       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1552   1552       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1593   1593       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1597   1597       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   CROSSLNK   1332   1332       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P51532}.
SQ   SEQUENCE   1613 AA;  181427 MW;  7E5F1B04D4C26C87 CRC64;
     MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPMPTQG
     PGGYPQDNMH QMHKPMESMH EKGMPDDPRY NQMKGMGMRS GAHTGMGPPP SPMDQHSQGY
     PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGSDPQ ALGQQNRGPT PFNQNQLHQL
     RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP
     GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ
     KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PLVPLHQKQS RITPIQKPRG
     LDPVEILQER EYRLQARIVH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV
     VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL
     QHAKDFREYH RSVTGKLQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK
     LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG
     PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES
     GSEEEEEEEE EEQPQPAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA KQDVDDEYGV
     SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE
     MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA
     RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH
     YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT GEKVDLNEEE
     TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH MQAKGVLLTD
     GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV QGLDLYRASG
     KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK
     TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR
     VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI LEHEEQDEEE
     DEVPDDETVN QMIARHEEEF DLFMRMDLDR RREEARNPKR KPRLMEEDEL PSWIIKDDAE
     VERLTCEEEE EKMFGRGSRH RKEVDYSDSL TEKQWLKAIE EGTLEEIEEE VRQKKSSRKR
     KRDSEAGSST PTTSTRSRDK DEESKKQKKR GRPPAEKLSP NPPNLTKKMK KIVDAVIKYK
     DSSGRQLSEV FIQLPSRKEL PEYYELIRKP VDFKKIKERI RNHKYRSLND LEKDVMLLCQ
     NAQTFNLEGS LIYEDSIVLQ SVFTSVRQKI EKEDDSEGEE SEEEEEGEEE GSESESRSVK
     VKIKLGRKEK AQDRLKGGRR RPSRGSRAKP VVSDDDSDEE QEEDRSGSGS EED
//
DBGET integrated database retrieval system