ID HIRA_DROME Reviewed; 1047 AA.
AC O17468; O46105; O77144; Q5U0S5; Q8T0C3; Q9W3Q3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 27-MAR-2024, entry version 190.
DE RecName: Full=Protein HIRA homolog;
DE AltName: Full=Protein sesame;
DE AltName: Full=dHIRA;
GN Name=Hira; Synonyms=Dhh, ssm; ORFNames=CG12153;
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 [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=9611274; DOI=10.1016/s0378-1119(98)00143-7;
RA Kirov N., Shtilbans A., Rushlow C.;
RT "Isolation and characterization of a new gene encoding a member of the HIRA
RT family of proteins from Drosophila melanogaster.";
RL Gene 212:323-332(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=9712723; DOI=10.1006/bbrc.1998.9165;
RA Llevadot R., Marques G., Pritchard M., Estivill X., Ferrus A., Scambler P.;
RT "Cloning, chromosome mapping and expression analysis of the HIRA gene from
RT Drosophila melanogaster.";
RL Biochem. Biophys. Res. Commun. 249:486-491(1998).
RN [3]
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 [4]
RP GENOME REANNOTATION.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Testis;
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=10837127; DOI=10.1006/dbio.2000.9718;
RA Loppin B., Docquier M., Bonneton F., Couble P.;
RT "The maternal effect mutation sesame affects the formation of the male
RT pronucleus in Drosophila melanogaster.";
RL Dev. Biol. 222:392-404(2000).
RN [8]
RP FUNCTION.
RX PubMed=11735001; DOI=10.1007/s004120100161;
RA Loppin B., Berger F., Couble P.;
RT "The Drosophila maternal gene sesame is required for sperm chromatin
RT remodeling at fertilization.";
RL Chromosoma 110:430-440(2001).
RN [9]
RP FUNCTION.
RX PubMed=15988027; DOI=10.1128/mcb.25.14.6165-6177.2005;
RA Jayaramaiah Raja S., Renkawitz-Pohl R.;
RT "Replacement by Drosophila melanogaster protamines and Mst77F of histones
RT during chromatin condensation in late spermatids and role of sesame in the
RT removal of these proteins from the male pronucleus.";
RL Mol. Cell. Biol. 25:6165-6177(2005).
RN [10]
RP ERRATUM OF PUBMED:15988027.
RA Jayaramaiah Raja S., Renkawitz-Pohl R.;
RL Mol. Cell. Biol. 26:3682-3682(2006).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-225.
RX PubMed=16251970; DOI=10.1038/nature04059;
RA Loppin B., Bonnefoy E., Anselme C., Laurencon A., Karr T.L., Couble P.;
RT "The histone H3.3 chaperone HIRA is essential for chromatin assembly in the
RT male pronucleus.";
RL Nature 437:1386-1390(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
CC -!- FUNCTION: Required for the periodic repression of histone gene
CC transcription during the cell cycle (By similarity). Required for
CC replication-independent chromatin assembly. Promotes remodeling of
CC sperm chromatin following fertilization via the incorporation of
CC histone H3.3 and histone H4. {ECO:0000250, ECO:0000269|PubMed:10837127,
CC ECO:0000269|PubMed:11735001, ECO:0000269|PubMed:15988027,
CC ECO:0000269|PubMed:16251970}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16251970}.
CC Note=Maternally contributed protein localizes specifically to the male
CC nucleus in fertilized eggs. This localization persists from the
CC initiation of sperm nucleus decondensation to the end of pronucleus
CC formation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=O17468-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=O17468-2; Sequence=VSP_006775, VSP_006776, VSP_006777;
CC Name=3;
CC IsoId=O17468-3; Sequence=VSP_006776, VSP_006777;
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically throughout
CC development to adults (male and female). {ECO:0000269|PubMed:9611274,
CC ECO:0000269|PubMed:9712723}.
CC -!- SIMILARITY: Belongs to the WD repeat HIR1 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be involved in protamine removal but
CC this was shown to be incorrect in the subsequent published erratum.
CC {ECO:0000269|Ref.10}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC48360.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF031081; AAC48360.1; ALT_FRAME; mRNA.
DR EMBL; AJ222709; CAA10954.1; -; mRNA.
DR EMBL; AF071881; AAC64041.1; -; mRNA.
DR EMBL; AE014298; AAF46267.1; -; Genomic_DNA.
DR EMBL; AY069414; AAL39559.1; -; mRNA.
DR EMBL; BT016167; AAV37052.1; -; mRNA.
DR PIR; A59246; A59246.
DR RefSeq; NP_572401.2; NM_132173.3. [O17468-1]
DR AlphaFoldDB; O17468; -.
DR SMR; O17468; -.
DR BioGRID; 58155; 24.
DR IntAct; O17468; 2.
DR STRING; 7227.FBpp0071028; -.
DR iPTMnet; O17468; -.
DR PaxDb; 7227-FBpp0071028; -.
DR EnsemblMetazoa; FBtr0071070; FBpp0071028; FBgn0022786. [O17468-1]
DR GeneID; 31680; -.
DR KEGG; dme:Dmel_CG12153; -.
DR AGR; FB:FBgn0022786; -.
DR CTD; 7290; -.
DR FlyBase; FBgn0022786; Hira.
DR VEuPathDB; VectorBase:FBgn0022786; -.
DR eggNOG; KOG0973; Eukaryota.
DR GeneTree; ENSGT00550000074919; -.
DR HOGENOM; CLU_004372_3_0_1; -.
DR InParanoid; O17468; -.
DR OMA; AWVHHDD; -.
DR OrthoDB; 5478541at2759; -.
DR PhylomeDB; O17468; -.
DR SignaLink; O17468; -.
DR BioGRID-ORCS; 31680; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Hira; fly.
DR GenomeRNAi; 31680; -.
DR PRO; PR:O17468; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0022786; Expressed in embryonic/larval hemocyte (Drosophila) and 20 other cell types or tissues.
DR Genevisible; O17468; DM.
DR GO; GO:0042585; C:germinal vesicle; IDA:FlyBase.
DR GO; GO:0000417; C:HIR complex; IBA:GO_Central.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; IMP:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0035041; P:sperm DNA decondensation; IMP:FlyBase.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR031120; HIR1-like.
DR InterPro; IPR011494; HIRA-like_C.
DR InterPro; IPR019015; HIRA_B_motif.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR13831; MEMBER OF THE HIR1 FAMILY OF WD-REPEAT PROTEINS; 1.
DR PANTHER; PTHR13831:SF0; PROTEIN HIRA; 1.
DR Pfam; PF07569; Hira; 1.
DR Pfam; PF09453; HIRA_B; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..1047
FT /note="Protein HIRA homolog"
FT /id="PRO_0000051022"
FT REPEAT 11..53
FT /note="WD 1"
FT REPEAT 68..107
FT /note="WD 2"
FT REPEAT 127..166
FT /note="WD 3"
FT REPEAT 170..209
FT /note="WD 4"
FT REPEAT 218..263
FT /note="WD 5"
FT REPEAT 264..319
FT /note="WD 6"
FT REPEAT 323..364
FT /note="WD 7"
FT REGION 401..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 63
FT /note="L -> LPVLSDKAEFDADVPKML (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9712723"
FT /id="VSP_006775"
FT VAR_SEQ 430..437
FT /note="KDGKRRIT -> LSLICKIF (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:9712723"
FT /id="VSP_006776"
FT VAR_SEQ 438..1047
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:9712723"
FT /id="VSP_006777"
FT MUTAGEN 225
FT /note="R->K: In allele ssm; maternal effect embryonic
FT lethal mutation which impairs maternal histone deposition
FT in the male pronucleus."
FT /evidence="ECO:0000269|PubMed:16251970"
FT CONFLICT 53
FT /note="A -> G (in Ref. 1; AAC48360)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="D -> E (in Ref. 1; AAC48360)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="C -> G (in Ref. 1; AAC48360)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="C -> S (in Ref. 1; AAC48360)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..163
FT /note="QAFPH -> RHFHN (in Ref. 2; AAC64041)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="K -> E (in Ref. 2; AAC64041)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="S -> W (in Ref. 1; AAC48360)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="G -> A (in Ref. 2; AAC64041)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="N -> D (in Ref. 2; CAA10954)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="D -> Y (in Ref. 1; AAC48360)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="A -> V (in Ref. 1; AAC48360)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="N -> I (in Ref. 6; AAV37052)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="L -> M (in Ref. 6; AAV37052)"
FT /evidence="ECO:0000305"
FT CONFLICT 453..455
FT /note="MNI -> LNF (in Ref. 1; AAC48360)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="S -> R (in Ref. 2; CAA10954)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="L -> V (in Ref. 1; AAC48360)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="S -> T (in Ref. 6; AAV37052)"
FT /evidence="ECO:0000305"
FT CONFLICT 890..892
FT /note="QKT -> PKA (in Ref. 6; AAV37052)"
FT /evidence="ECO:0000305"
FT CONFLICT 1043
FT /note="K -> Q (in Ref. 1; AAC48360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1047 AA; 113415 MW; 3614D5F411DC440C CRC64;
MRLLKPAWVH HDDKQIFSVD IHKDCTKFAT GGQGSDCGRV VIWNLLPVLS DKAEFDADVP
KMLCQMDQHL ACVNCVRWSQ NGQNLASGSD DKLIMIWRKS AGSSGVFGTG GMQKNHESWK
CFYTLRGHDG DVLDLAWSPN DVYLASCSID NTVIIWDAQA FPHSVATLKG HTGLVKGVSW
DPLGRFLASQ SDDRSIKIWN TMNWSLSHTI TEPFEECGGT THILRLSWSP DGQYLVSAHA
MNGGGPTAQI IEREGWKCDK DFVGHRKAVT CVRFHNSILS RQENDGSPSK PLQYCCLAVG
SRDRSLSVWM TALQRPMVVI HELFNASILD LTWGPQECLL MACSVDGSIA CLKFTEEELG
KAISEEEQNA IIRKMYGKNY VNGLGKSAPV LEHPQRLLLP QGDKPTKFPL SNNNEANQRP
ISKQTETRTK DGKRRITPMF IPLHEDGPTS LSMNIVSSSG SSTTALTSCS AAIGTLPAAA
PTESAATPLM PLEPLVSKID LGRLDSRLKT QPASQRRQSL PFDPGQSNEL LRTPRLEEHQ
SSTCSPSNLN VTATGKSEFV KAALDYRLHV SNGHLKTQHG MLAKVTASDS KEMLWEFYVG
SPLVNLNLCE KYAMLCSLDG SMRLISMETG CPVFPAISLT SSAVHCAFSP DNSLVGVLTE
CGLLRIWDIA KKVVSLAAGC LELLNKHGTA AQFSVTNQGM PLIGFPSGNS YSYSTSLQSW
LVLATKDAIM YHGIRGTLPR DMDQMQQKFP LLSMQASSQN YFSFTGSMEL RHSESWQQCA
KIRFIENQIK LCEALQSLDE LQHWHKMLTF QLATHGSEKR MRVFLDDLLS MPEPGISQFV
PKLELMQCVL DTLKPHSEWN RLHSEYTELL KECKSERQKD IFATPAPPQQ KTASSAGSSP
RSGEATGEEV TEKDGATAVA AAVVAGSRMA VTTGTSTTTT TTASSSLSSS GSSSSTSGSG
SSSSSSSTSS LSVPQPAPSL SPEIQTLDSP TVCIDDEILS ASSSLPPLDT SPVEVSPAST
SGGAASTSPA ASVAGSAPVS SSKTDQT
//
