SMCA4_BOVIN
ID SMCA4_BOVIN Reviewed; 1606 AA.
AC A7Z019;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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 that
CC carry out key enzymatic activities, changing chromatin structure by
CC altering DNA-histone contacts within a nucleosome in an ATP-dependent
CC manner. Component of the CREST-BRG1 complex, a multiprotein complex
CC that regulates promoter activation by orchestrating the calcium-
CC dependent release of a repressor complex and the recruitment of an
CC activator complex. In resting neurons, transcription of the c-fOS
CC promoter is inhibited by SMARCA4-dependent recruitment of a phospho-
CC RB1-HDAC repressor complex. Upon calcium influx, RB1 is
CC dephosphorylated by calcineurin, which leads to release of the
CC repressor complex. At the same time, there is increased recruitment of
CC CREBBP to the promoter by a CREST-dependent mechanism, which leads to
CC transcriptional activation. The CREST-BRG1 complex also binds to the
CC NR2B promoter, and activity-dependent induction of NR2B expression
CC involves the release of HDAC1 and recruitment of CREBBP. Belongs to the
CC neural progenitors-specific chromatin remodeling complex (npBAF
CC complex) and the neuron-specific chromatin remodeling complex (nBAF
CC complex). During neural development, a switch from a stem/progenitor to
CC a postmitotic chromatin remodeling mechanism occurs as neurons exit the
CC cell cycle and become committed to their adult state. The transition
CC from proliferating neural stem/progenitor cells to postmitotic neurons
CC requires a switch in subunit composition of the npBAF and nBAF
CC complexes. As neural progenitors exit mitosis and differentiate into
CC neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A,
CC are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
CC or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF
CC complex is essential for the self-renewal/proliferative capacity of the
CC multipotent neural stem cells. The nBAF complex along with CREST plays
CC a role regulating the activity of genes essential for dendrite growth.
CC SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation
CC by enhancing Notch-dependent proliferative signals, while concurrently
CC making the neural stem cell insensitive to SHH-dependent
CC differentiating cues. Acts as a corepressor of ZEB1 to regulate E-
CC cadherin transcription and is required for induction of epithelial-
CC mesenchymal transition (EMT) by ZEB1. Binds via DLX1 to enhancers
CC located in the intergenic region between DLX5 and DLX6 and this binding
CC is stabilized by the long non-coding RNA (lncRNA) Evf2. Binds to RNA in
CC a promiscuous manner. Binding to RNAs including lncRNA Evf2 leads to
CC inhibition of SMARCA4 ATPase and chromatin remodeling activities.
CC {ECO:0000250|UniProtKB:P51532, ECO:0000250|UniProtKB:Q3TKT4}.
CC -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes
CC SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The
CC canonical complex contains a catalytic subunit (either
CC SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1,
CC ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47.
CC Other subunits specific to each of the complexes may also be present
CC permitting several possible developmental- and tissue-specific
CC combinations. Component of the BAF complex, which includes at least
CC actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the
CC BAF complex also contains DPF3. Component of neural progenitors-
CC specific chromatin remodeling complex (npBAF complex) composed of at
CC least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific
CC chromatin 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 (PBAF)
CC chromatin remodeling complex, at least composed of SMARCA4/BRG1,
CC SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57,
CC SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155,
CC SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin. Component of
CC SWI/SNF (GBAF) subcomplex, which includes at least BICRA or BICRAL
CC (mutually exclusive), BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A,
CC ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A. Component of the
CC BAF53 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 of
CC the CREST-BRG1 complex, at least composed of SMARCA4/BRG1/BAF190A,
CC SS18L1/CREST, HDAC1, RB1 and SP1 (By similarity). Interacts with
CC PHF10/BAF45A (By similarity). Interacts with MYOG (By similarity).
CC Interacts directly with IKFZ1; the interaction associates IKFZ1 with
CC the BAF complex. Interacts with ZEB1 (via N-terminus). Interacts with
CC NR3C1, PGR, 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-dependent
CC manner (By similarity). Interacts with KDM6A and KDM6B (By similarity).
CC Interacts with HNRNPU; this interaction occurs in embryonic stem cells
CC and stimulates global Pol II-mediated transcription (By similarity).
CC Interacts with ACTL6A (By similarity). Interacts with DLX1 (By
CC similarity). Interacts with DPF2 (By similarity).
CC {ECO:0000250|UniProtKB:P51532, ECO:0000250|UniProtKB:Q3TKT4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3TKT4}.
CC Note=Colocalizes with long non-coding RNA Evf2 in nuclear RNA clouds.
CC {ECO:0000250|UniProtKB:Q3TKT4}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; BC153216; AAI53217.1; -; mRNA.
DR RefSeq; NP_001099084.1; NM_001105614.1.
DR AlphaFoldDB; A7Z019; -.
DR SMR; A7Z019; -.
DR STRING; 9913.ENSBTAP00000025598; -.
DR PaxDb; A7Z019; -.
DR PRIDE; A7Z019; -.
DR Ensembl; ENSBTAT00000025598; ENSBTAP00000025598; ENSBTAG00000019220.
DR GeneID; 414274; -.
DR KEGG; bta:414274; -.
DR CTD; 6597; -.
DR VEuPathDB; HostDB:ENSBTAG00000019220; -.
DR VGNC; VGNC:34987; SMARCA4.
DR eggNOG; KOG0386; Eukaryota.
DR GeneTree; ENSGT00940000156887; -.
DR HOGENOM; CLU_000315_15_0_1; -.
DR InParanoid; A7Z019; -.
DR OrthoDB; 685477at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000019220; Expressed in thymus and 106 other tissues.
DR ExpressionAtlas; A7Z019; baseline and differential.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016514; C:SWI/SNF complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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-rel_dom; 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 2: Evidence at transcript level;
KW Acetylation; Activator; ATP-binding; Bromodomain; Chromatin regulator;
KW Helicase; Hydrolase; Isopeptide bond; Neurogenesis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1606
FT /note="Transcription activator BRG1"
FT /id="PRO_0000391342"
FT DOMAIN 171..206
FT /note="QLQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001"
FT DOMAIN 452..524
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 758..923
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1076..1238
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1436..1506
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..274
FT /note="Necessary for interaction with SS18L1/CREST"
FT /evidence="ECO:0000250"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..720
FT /note="RNA-binding region which is sufficient for binding
FT to lncRNA Evf2"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT REGION 569..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..908
FT /note="Sufficient for interaction with DLX1"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT REGION 1239..1405
FT /note="Sufficient for interaction with DLX1"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT REGION 1356..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1523..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 873..876
FT /note="DEGH box"
FT /evidence="ECO:0000250"
FT COMPBIAS 9..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..280
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..332
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..666
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1545
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1546..1572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 771..778
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 1498..1499
FT /note="Required for binding to 'Lys-15'-acetylated histone
FT 3"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 188
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 345
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 601
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 618
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6DIC0"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1382
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT CROSSLNK 1324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51532"
SQ SEQUENCE 1606 AA; 180679 MW; 6B313F0CD28C9D7E CRC64;
MSTPDPALGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SIMGPSPGPP SAGHPIPTQG
PGGYPQDNMH QMHKPMESMH EKGMSDDPRY TQMKGMGMRS GGHAGMGPPP SPMDQHSQGY
PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGADPQ ALGQQNRGPT PFNQNQLHQL
RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQPQMPAL PPPSVSATGP GPSPGPAPPN
YSRPHGMGGP NMPPPGPSGV PPGMPGQPPG GPPKPWPEGP MANAAAPTST PQKLIPPQPT
GRPSPAPPAV PPAASPVMPP QTQSPGQPAQ PAPMVPLHQK QSRITPIQKP RGLDPVEILQ
EREYRLQARI AHRIQELENL PGSLAGDLRT KATIELKALR LLNFQRQLRQ EVVVCMRRDT
ALETALNAKA YKRSKRQSLR EARITEKLEK QQKIEQERKR RQKHQEYLNS ILQHAKDFKE
YHRSVTGKIQ KLTKAVATYH ANTEREQKKE NERIEKERMR RLMAEDEEGY RKLIDQKKDK
RLAYLLQQTD EYVANLTELV RQHKAAQVAK EKKKKKKKKK AENAEGQTPA IGPDGEPLDE
TSQMSDLPVK VIHVESGKIL TGTDAPKAGQ LEAWLEMNPG YEVAPRSDSE ESGSEEEEEE
EEEEQPQPAQ PPTLPVEEKK KIPDPDSDDV SEVDARHIIE NAKQDVDDEY GVSQALARGL
QSYYAVAHAV TERVDKQSAL MVNGVLKQYQ IKGLEWLVSL YNNNLNGILA DEMGLGKTIQ
TIALITYLME HKRINGPFLI IVPLSTLSNW AYEFDKWAPS VVKVSYKGSP AARRAFVPQL
RSGKFNVLLT TYEYIIKDKH ILAKIRWKYM IVDEGHRMKN HHCKLTQVLN THYVAPRRLL
LTGTPLQNKL PELWALLNFL LPTIFKSCST FEQWFNAPFA MTGEKVDLNE EETILIIRRL
HKVLRPFLLR RLKKEVEAQL PEKVEYVIKC DMSALQRVLY RHMQAKGVLL TDGSEKDKKG
KGGTKTLMNT IMQLRKICNH PYMFQHIEES FSEHLGFTGG IVQGLDLYRA SGKFELLDRI
LPKLRATNHK VLLFCQMTSL MTIMEDYFAY RGFKYLRLDG TTKAEDRGML LKTFNEPGSE
YFIFLLSTRA GGLGLNLQSA DTVIIFDSDW NPHQDLQAQD RAHRIGQQNE VRVLRLCTVN
SVEEKILAAA KYKLNVDQKV IQAGMFDQKS SSHERRAFLQ AILEHEEQDE EEDEVPDDET
VNQMIARHEE EFDLFMRMDL DRRREEARNP KRKPRLMEED ELPSWIIKDD AEVERLTCEE
EEEKMFGRGS RHRKEVDYSD SLTEKQWLKA IEEGTLEEIE EEVRQKKSSR KRKRDSDAGP
STPTTSTRSR DKDDESKKQK KRGRPPAEKL SPNPPNLTKK MKKIVDAVIK YKDSSSGRQL
SEVFIQLPSR KELPEYYELI RKPVDFKKIK ERIRNHKYRS LNDLEKDVML LCQNAQTFNL
EGSLIYEDSI VLQSVFTSVR QKIEKEDDSE GEESEEEEEG EEEGSESESR SVKVKIKLGR
KEKAQDRLKG GRRRPSRGSR AKPVVSDDDS EEEQEEDRSG SGSEED
