SMCA1_MOUSE
ID SMCA1_MOUSE Reviewed; 1046 AA.
AC Q6PGB8; B1AUP6; B1AUP7; Q8BSS1; Q91Y58;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Probable global transcription activator SNF2L1;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P28370};
DE AltName: Full=ATP-dependent helicase SMARCA1;
DE AltName: Full=DNA-dependent ATPase SNF2L;
DE AltName: Full=Nucleosome-remodeling factor subunit SNF2L;
DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1;
GN Name=Smarca1; Synonyms=Snf2l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11359880; DOI=10.1046/j.1471-4159.2001.00324.x;
RA Lazzaro M.A., Picketts D.J.;
RT "Cloning and characterization of the murine Imitation Switch (ISWI) genes:
RT differential expression patterns suggest distinct developmental roles for
RT Snf2h and Snf2l.";
RL J. Neurochem. 77:1145-1156(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=14609955; DOI=10.1093/emboj/cdg582;
RA Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J.,
RA Shiekhattar R.;
RT "Isolation of human NURF: a regulator of Engrailed gene expression.";
RL EMBO J. 22:6089-6100(2003).
RN [6]
RP INDUCTION.
RX PubMed=16740656; DOI=10.1210/me.2005-0213;
RA Lazzaro M.A., Pepin D., Pescador N., Murphy B.D., Vanderhyden B.C.,
RA Picketts D.J.;
RT "The imitation switch protein SNF2L regulates steroidogenic acute
RT regulatory protein expression during terminal differentiation of ovarian
RT granulosa cells.";
RL Mol. Endocrinol. 20:2406-2417(2006).
CC -!- FUNCTION: Helicase that possesses intrinsic ATP-dependent chromatin-
CC remodeling activity (By similarity). ATPase activity is substrate-
CC dependent, and is increased when nucleosomes are the substrate, but is
CC also catalytically active when DNA alone is the substrate (By
CC similarity). Catalytic subunit of ISWI chromatin-remodeling complexes,
CC which form ordered nucleosome arrays on chromatin and facilitate access
CC to DNA during DNA-templated processes such as DNA replication,
CC transcription, and repair (By similarity). Within the ISWI chromatin-
CC remodeling complexes, slides edge- and center-positioned histone
CC octamers away from their original location on the DNA template (By
CC similarity). Catalytic activity and histone octamer sliding propensity
CC is regulated and determined by components of the ISWI chromatin-
CC remodeling complexes (By similarity). The BAZ1A-, BAZ1B-, BAZ2A- and
CC BAZ2B-containing ISWI chromatin-remodeling complexes regulate the
CC spacing of nucleosomes along the chromatin and have the ability to
CC slide mononucleosomes to the center of a DNA template (By similarity).
CC The CECR2- and RSF1-containing ISWI chromatin-remodeling complexes do
CC not have the ability to slide mononucleosomes to the center of a DNA
CC template (By similarity). Within the NURF-1 and CERF-1 ISWI chromatin
CC remodeling complexes, nucleosomes are the preferred substrate for its
CC ATPase activity (By similarity). Within the NURF-1 ISWI chromatin-
CC remodeling complex, binds to the promoters of En1 and En2 to positively
CC regulate their expression and promote brain development (By
CC similarity). May promote neurite outgrowth (By similarity). May be
CC involved in the development of luteal cells (By similarity).
CC {ECO:0000250|UniProtKB:P28370}.
CC -!- SUBUNIT: May form homodimers (By similarity). Component of the ACF-1
CC ISWI chromatin remodeling complex at least composed of SMARCA1 and
CC BAZ1A, which regulates the spacing of histone octamers on the DNA
CC template to facilitate access to DNA (By similarity). Within the
CC complex interacts with BAZ1A; the interaction is direct (By
CC similarity). Component of the WICH-1 ISWI chromatin remodeling complex
CC at least composed of SMARCA1 and BAZ1B/WSTF (By similarity). Within the
CC complex interacts with BAZ1B/WSTF (By similarity). Component of the
CC NoRC-1 ISWI chromatin remodeling complex at least composed of SMARCA1
CC and BAZ2A/TIP5 (By similarity). Within the complex interacts with
CC BAZ2A/TIP5 (By similarity). Component of the BRF-1 ISWI chromatin
CC remodeling complex at least composed of SMARCA1 and BAZ2B (By
CC similarity). Within the complex interacts with BAZ2B (By similarity).
CC Component of the NURF-1 ISWI chromatin remodeling complex (also called
CC the nucleosome-remodeling factor (NURF) complex) at least composed of
CC SMARCA1, BPTF, RBBP4 and RBBP7 (By similarity). Within the complex
CC interacts with BPTF (By similarity). Within the complex interacts with
CC RBBP4 and RBBP7 (By similarity). Component of the CERF-1 ISWI chromatin
CC remodeling complex (also called the CECR2-containing-remodeling factor
CC (CERF) complex) at least composed of CECR2 and SMARCA1 (By similarity).
CC Within the complex interacts with CECR2 (By similarity). Component of
CC the RSF-1 ISWI chromatin remodeling complex at least composed of
CC SMARCA1 and RSF1 (By similarity). Within the complex interacts with
CC RSF1 (By similarity). Interacts with PRLR (By similarity). Interacts
CC with ERCC6 (By similarity). {ECO:0000250|UniProtKB:P28370}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PGB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PGB8-2; Sequence=VSP_020378;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in cortex, cerebellum,
CC ovaries, testes, uterus and placenta. {ECO:0000269|PubMed:11359880,
CC ECO:0000269|PubMed:14609955}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the embryo at 9.5 dpc-15.5
CC dpc. Brain expression increases during the first two weeks of postnatal
CC development. {ECO:0000269|PubMed:11359880}.
CC -!- INDUCTION: By ovulation in ovaries (at protein level).
CC {ECO:0000269|PubMed:16740656}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK52453.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF325920; AAK52453.1; ALT_FRAME; mRNA.
DR EMBL; AK030741; BAC27109.1; -; mRNA.
DR EMBL; AL671903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057115; AAH57115.1; -; mRNA.
DR CCDS; CCDS30104.1; -. [Q6PGB8-1]
DR CCDS; CCDS72374.1; -. [Q6PGB8-2]
DR RefSeq; NP_001277637.1; NM_001290708.1. [Q6PGB8-2]
DR RefSeq; NP_444353.3; NM_053123.4. [Q6PGB8-1]
DR AlphaFoldDB; Q6PGB8; -.
DR SMR; Q6PGB8; -.
DR BioGRID; 220299; 7.
DR ComplexPortal; CPX-454; CERF chromatin remodelling complex.
DR ComplexPortal; CPX-694; NuRF chromatin remodeling complex.
DR IntAct; Q6PGB8; 1.
DR STRING; 10090.ENSMUSP00000086366; -.
DR iPTMnet; Q6PGB8; -.
DR PhosphoSitePlus; Q6PGB8; -.
DR EPD; Q6PGB8; -.
DR MaxQB; Q6PGB8; -.
DR PaxDb; Q6PGB8; -.
DR PRIDE; Q6PGB8; -.
DR ProteomicsDB; 261430; -. [Q6PGB8-1]
DR ProteomicsDB; 261431; -. [Q6PGB8-2]
DR Antibodypedia; 518; 205 antibodies from 27 providers.
DR DNASU; 93761; -.
DR Ensembl; ENSMUST00000077569; ENSMUSP00000076769; ENSMUSG00000031099. [Q6PGB8-1]
DR Ensembl; ENSMUST00000088973; ENSMUSP00000086366; ENSMUSG00000031099. [Q6PGB8-1]
DR Ensembl; ENSMUST00000101616; ENSMUSP00000099138; ENSMUSG00000031099. [Q6PGB8-2]
DR GeneID; 93761; -.
DR KEGG; mmu:93761; -.
DR UCSC; uc009tbl.2; mouse. [Q6PGB8-1]
DR UCSC; uc009tbm.2; mouse. [Q6PGB8-2]
DR CTD; 6594; -.
DR MGI; MGI:1935127; Smarca1.
DR VEuPathDB; HostDB:ENSMUSG00000031099; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000157297; -.
DR InParanoid; Q6PGB8; -.
DR OMA; IHDWQFF; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; Q6PGB8; -.
DR TreeFam; TF300674; -.
DR BRENDA; 2.7.11.17; 3474.
DR BioGRID-ORCS; 93761; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Smarca1; mouse.
DR PRO; PR:Q6PGB8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6PGB8; protein.
DR Bgee; ENSMUSG00000031099; Expressed in gonadal ridge and 227 other tissues.
DR ExpressionAtlas; Q6PGB8; baseline and differential.
DR Genevisible; Q6PGB8; MM.
DR GO; GO:1904949; C:ATPase complex; ISO:MGI.
DR GO; GO:0090537; C:CERF complex; ISO:MGI.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016589; C:NURF complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; ISO:MGI.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISS:HGNC.
DR GO; GO:0030182; P:neuron differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:HGNC.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:HGNC.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR CDD; cd18065; DEXHc_SMARCA1; 1.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.1040.30; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR044755; SMARCA1_N.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF13892; DBINO; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; SSF101224; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ATP-binding; Chromatin regulator;
KW Coiled coil; DNA-binding; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1046
FT /note="Probable global transcription activator SNF2L1"
FT /id="PRO_0000249246"
FT DOMAIN 199..364
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 494..645
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 847..899
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 950..1014
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 27..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1003..1037
FT /evidence="ECO:0000255"
FT MOTIF 315..318
FT /note="DEAH box"
FT BINDING 212..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28370"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28370"
FT MOD_RES 946
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P28370"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P28370"
FT CROSSLNK 720
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P28370"
FT CROSSLNK 742
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P28370"
FT VAR_SEQ 1040..1046
FT /note="VKFSAFS -> SQKRKAESATESSGRKDVKKVKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11359880"
FT /id="VSP_020378"
FT CONFLICT 53
FT /note="G -> A (in Ref. 1; AAK52453 and 2; BAC27109)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="D -> A (in Ref. 1; AAK52453)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="Q -> H (in Ref. 2; BAC27109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1046 AA; 121715 MW; 11D60F70FE466FC5 CRC64;
MEPDTATEAA TVAVSDARAT VVVVEDEQPG PSTFKEEGAA AAATEGTTAT EKGEKKEKIT
SPFQLKLAAK ASKSEKEMDP EYEEKMVNMP LKADRAKRFE FLLKQTELFA HFIQPSAQKS
PTSPLNMKLA RPRVKKDDKQ SLISVGDYRH RRTEQEEDEE LLSESRKTSN VCVRFEVSPS
YVKGGPLRDY QIRGLNWLIS LYENGVNGIL ADEMGLGKTL QTIALLGYLK HYRNIPGPHM
VLVPKSTLHN WMNEFKRWVP SLRVICFVGD KDVRAAFIRD EMMPGEWDVC VTSYEMVIKE
KSVFKKFHWR YLVIDEAHRI KNEKSKLSEI VREFKSTNRL LLTGTPLQNN LHELWALLNF
LLPDVFNSAD DFDSWFDTKN CLGDQKLVER LHAVLKPFLL RRIKTDVEKS LPPKKEIKIY
LGLSKMQREW YTKILMKDID VLNSSGKMDK MRLLNILMQL RKCCNHPYLF DGAEPGPPYT
TDEHIVGNSG KMVALDKLLA RIKEQGSRVL IFSQMTRLLD ILEDYCMWRG YEYSRLDGQT
PHEEREEAID AFNAPNSSKF IFMLSTRAGG LGINLASADV VILYDSDWNP QVDLQAMDRA
HRIGQKKPVR VFRLITDNTV EERIVERAEI KLRLDSIVIQ QGRLIDQQSN KLAKEEMLQM
IRHGATHVFA CKESELTDED IVTILERGEK KTAEMNERMQ KMGESSLRNF RMDLEQSLYK
FEGEDYREKQ KLGTVEWIEP PKRERKANYA VDAYFREALR VSEPKIPKAP RPPKQPNVQD
FQFFPPRLFE LLEKEILYYR KTIGYKVPRN PEIPNPAIAQ REEQKKIDGA EPLTPQETEE
KDKLLTQGFT NWTKRDFNQF IKANEKYGRD DIDNIAREVE GKSPEEVMEY SAVFWERCNE
LQDIEKIMAQ IERGEARIQR RISIKKALDA KIARYKAPFH QLRIQYGTSK GKNYTEEEDR
FLICMLHKMG FDRENVYEEL RQCVRNAPQF RFDWFIKSRT AMEFQRRCNT LISLIEKENM
EIEERERAEK KKRATKTPMV KFSAFS
