FSH_DROME
ID FSH_DROME Reviewed; 2038 AA.
AC P13709; A4V442; P13710; Q8IRN6; Q9W3L3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Homeotic protein female sterile;
DE AltName: Full=Fragile-chorion membrane protein;
GN Name=fs(1)h; Synonyms=fsh; ORFNames=CG2252;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B), FUNCTION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=2567251; DOI=10.1016/0012-1606(89)90094-8;
RA Haynes S.R., Mozer B.A., Bhatia-Dey N., Dawid I.B.;
RT "The Drosophila fsh locus, a maternal effect homeotic gene, encodes
RT apparent membrane proteins.";
RL Dev. Biol. 134:246-257(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 308-357 AND 848-897, AND NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 1812-1861.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=3031652; DOI=10.1073/pnas.84.7.1819;
RA Haynes S.R., Rebbert M.L., Mozer B.A., Forquignon F., Dawid I.B.;
RT "Pen repeat sequences are GGN clusters and encode a glycine-rich domain in
RT a Drosophila cDNA homologous to the rat helix destabilizing protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1819-1823(1987).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452; SER-943; SER-1653;
RP SER-1980 AND SER-1988, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required maternally for proper expression of other homeotic
CC genes involved in pattern formation, such as Ubx.
CC {ECO:0000269|PubMed:2567251}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=P13709-1; Sequence=Displayed;
CC Name=A; Synonyms=C, D, E;
CC IsoId=P13709-2; Sequence=VSP_014148, VSP_014149;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:2567251}.
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DR EMBL; M23221; AAA28540.1; -; mRNA.
DR EMBL; M23222; AAA28541.1; -; mRNA.
DR EMBL; AE014298; AAF46312.3; -; Genomic_DNA.
DR EMBL; AE014298; AAN09226.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65277.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65278.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65279.1; -; Genomic_DNA.
DR EMBL; BT015270; AAT94499.1; -; mRNA.
DR EMBL; M15762; AAA70424.1; -; Genomic_DNA.
DR EMBL; M15763; AAA70423.1; -; mRNA.
DR EMBL; M15764; AAA70422.1; -; mRNA.
DR PIR; A43742; A43742.
DR RefSeq; NP_001162699.1; NM_001169228.2. [P13709-2]
DR RefSeq; NP_511078.2; NM_078523.3. [P13709-1]
DR RefSeq; NP_727228.1; NM_167144.4. [P13709-2]
DR RefSeq; NP_996368.1; NM_206645.4. [P13709-2]
DR RefSeq; NP_996369.1; NM_206646.4. [P13709-2]
DR RefSeq; NP_996370.1; NM_206647.3. [P13709-2]
DR AlphaFoldDB; P13709; -.
DR SMR; P13709; -.
DR BioGRID; 58193; 26.
DR DIP; DIP-19376N; -.
DR IntAct; P13709; 29.
DR STRING; 7227.FBpp0305499; -.
DR iPTMnet; P13709; -.
DR PaxDb; P13709; -.
DR PRIDE; P13709; -.
DR DNASU; 31722; -.
DR EnsemblMetazoa; FBtr0071118; FBpp0071073; FBgn0004656. [P13709-2]
DR EnsemblMetazoa; FBtr0071119; FBpp0071074; FBgn0004656. [P13709-1]
DR EnsemblMetazoa; FBtr0071120; FBpp0089297; FBgn0004656. [P13709-2]
DR EnsemblMetazoa; FBtr0071121; FBpp0089298; FBgn0004656. [P13709-2]
DR EnsemblMetazoa; FBtr0071122; FBpp0089299; FBgn0004656. [P13709-2]
DR EnsemblMetazoa; FBtr0301309; FBpp0290524; FBgn0004656. [P13709-2]
DR GeneID; 31722; -.
DR KEGG; dme:Dmel_CG2252; -.
DR UCSC; CG2252-RC; d. melanogaster.
DR CTD; 31722; -.
DR FlyBase; FBgn0004656; fs(1)h.
DR VEuPathDB; VectorBase:FBgn0004656; -.
DR eggNOG; KOG1474; Eukaryota.
DR HOGENOM; CLU_001499_3_0_1; -.
DR InParanoid; P13709; -.
DR OMA; GHTHNTN; -.
DR PhylomeDB; P13709; -.
DR Reactome; R-DME-8951936; RUNX3 regulates p14-ARF.
DR SignaLink; P13709; -.
DR BioGRID-ORCS; 31722; 1 hit in 3 CRISPR screens.
DR ChiTaRS; fs(1)h; fly.
DR GenomeRNAi; 31722; -.
DR PRO; PR:P13709; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004656; Expressed in egg cell and 30 other tissues.
DR ExpressionAtlas; P13709; baseline and differential.
DR Genevisible; P13709; DM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:FlyBase.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:FlyBase.
DR GO; GO:0106140; F:P-TEFb complex binding; IDA:FlyBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007362; P:terminal region determination; IMP:FlyBase.
DR CDD; cd05497; Bromo_Brdt_I_like; 1.
DR CDD; cd05498; Bromo_Brdt_II_like; 1.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR031354; BRD4_CDT.
DR InterPro; IPR043508; Bromo_Brdt_I.
DR InterPro; IPR043509; Bromo_Brdt_II.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF17105; BRD4_CDT; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Bromodomain; Developmental protein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2038
FT /note="Homeotic protein female sterile"
FT /id="PRO_0000211194"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 816..830
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 874..894
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1731..1751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1939..1959
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 51..123
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 495..567
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 942..1024
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 145..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1580..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1645..1728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1957..2023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..617
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1793..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1859..1903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1981..1995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1999..2019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1653
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1980
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1988
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1022
FT /note="H -> RKPYY (in isoform A)"
FT /evidence="ECO:0000303|PubMed:2567251, ECO:0000303|Ref.4"
FT /id="VSP_014148"
FT VAR_SEQ 1107..2038
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:2567251, ECO:0000303|Ref.4"
FT /id="VSP_014149"
FT CONFLICT 909
FT /note="A -> G (in Ref. 1; AAA28540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1403
FT /note="Q -> QQ (in Ref. 1; AAA28540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1532
FT /note="Missing (in Ref. 1; AAA28540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2038 AA; 205345 MW; DC4A1A7B1266191E CRC64;
MSSSEPPPRY EPPVEPVNGI VQPPVIPPAE RPGRNTNQLQ YLIKTVMKVI WKHHFSWPFQ
QPVDAKKLNL PDYHKIIKQP MDMGTIKKRL ENNYYWSAKE TIQDFNTMFN NCYVYNKPGE
DVVVMAQTLE KVFLQKIESM PKEELELEPV TAKGGKKKQR APATPKSSSG GAGASTGSGT
SSAAVTSGPG SGSTKVSVAA SSAQQSGLQG ATGAGGGSSS TPGTQPGSGA GGAIAARPVS
AMGGTVSSTA GGAPSIPPIS TMPPHTVPGS TNTTTTAMAG GVGGPGAAGA NPNAAALMAS
LLNAGQTGAY PGAPGQTAVN SSSLLDGSTA AVAAAAAAAA AAAAAAGGAA GAAGGAGTIP
AVAVNAANAV QAYVNAGVSV GVDAVIPPQQ PAKIKKGVKR KADTTTPTAN AFESPYTQMD
SKSAKIATRR ESNRQDLTFQ GSGYNMSPLG VSGVPGLGGL VAGGVAGVAV AKNKEKLSDA
LKSCNEILKE LFSKKHSGYA WPFYKPVDAE MLGLHDYHDI IKKPMDLGTV KRKMDNREYK
SAPEFAADVR LIFTNCYKYN PPDHDVVAMG RKLQDVFEMR YANIPDEPVA NAAHHHGHGH
GHGHGHGHGH GHGHGHGHGH GYGGSSSLKH DASDSSSEDS SDTENESNSD EERSARLKML
ESKLLGLQEE IRKLSEEASA KKKAKKKLKE KKKSIGGGSG SGSASHHCHA TGGGANAGGA
GGPGSGGHGS VSVPGGVGSL GPGGAGGANL NALLGGSLVG HGGAAVAGGV PNVGALHSQV
HDVAMAFSQM AGGGAAAGAG FGAGVTAAGA SSGGKAGTLA GALAAGAAAG AGGTTAGSGS
SKGAKSKGGR GAKGSGAGGV GASNNAAAGN AAGGAAGAAA GAGSVGGVGG AGAAGGGNAS
KRAKGSSSAG AGGGVGGANA SAGGAGARGS SKKKPSQVMN FDSEEEDTAK PMSYDEKRQL
SLDINKLPGD KLGRVVHIIQ NREPSLRDSN PDEIEIDFET LKPSTLRELE SYVASCLRKK
THKKPSGKSK DEQMAEKKQE LEKRLQDVTG QLGASKKTAK KDESASSKVE AVQPANPVSS
SSSSSDSSSS SSSDSSSSDS SDSEAGDGDE RPPRKKKSRD SNGSNVNNPS INVVMGGNLP
SGALSPTTML MGLDHVVNSN TPTSQMSNML GNANPLTAAA MLNNNNKTSL PGSNFGGAPA
PGNMMHAGAG VPVAGAAVSA STGQQHNKNG PNDLSKVQPG GPINAALPPH SFAGGTATVA
TSQSSGGIRI ASNLHKPSGL GGGDLGEHHA ALAAALTSGI NSTGTAGGGI NNNGGSNNNA
NPLGGSHGDA MVNASLASLA SGLKQIPQFD DPVEQSLASL EFSAGSTGKS GLTDNFLMQQ
HLMQPAGPQQ QQQQQQQQPF GHQQQQQQQQ QQQQQQQQHM DYVTELLSKG AENVGGMNGN
HLLNFNLDMA AAYQQKHPQQ QQQQAHNNGF NVADFGMAGF DGLNMTAASF LDLEPSLQQQ
QMQQMQLQQQ HHQQQQQQTH QQQQQHQQQH HQQQQQQQLT QQQLQQQQQQ QQQQQHLQQQ
QHQQQHHQAA NKLLIIPKPI ESMMPSPPDK QQLQQHQKVL PPQQSPSDMK LHPNAAAAAA
VASAQAKLVQ TFKANEQNLK NASSWSSLAS ANSPQSHTSS SSSSSKAKPA MDSFQQFRNK
AKERDRLKLL EAAEKEKKNQ KEAAEKEQQR KHHKSSSSSL TSAAVAQAAA IAAATAAAAV
TLGAAAAAAL ASSASNPSGG SSSGGAGSTS QQAITGDRDR DRDRERERER SGSGGGQSGN
GNNSSNSANS NGPGSAGSGG SGGGGGSGPA SAGGPNSGGG GTANSNSGGG GGGGGPALLN
AGSNSNSGVG SGGAASSNSN SSVGGIVGSG GPGSNSQGSS GGGGGGPASG GGMGSGAIDY
GQQVAVLTQV AANAQAQHVA AAVAAQAILA ASPLGAMESG RKSVHDAQPQ ISRVEDIKAS
PGGQGQSSPA QQSPQDRAAA KRAEQRRAEQ ERRRREALAG QIDMNMQSDL MAAFEETL
