SUS_DROME
ID SUS_DROME Reviewed; 1325 AA.
AC P22293; O77427; Q8SYG7;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein suppressor of sable {ECO:0000303|PubMed:1703632};
GN Name=su(sable) {ECO:0000312|FlyBase:FBgn0003575};
GN Synonyms=su(s) {ECO:0000303|PubMed:1703632};
GN ORFNames=CG6222 {ECO:0000312|FlyBase:FBgn0003575};
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], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=1703632; DOI=10.1128/mcb.11.2.894-905.1991;
RA Voelker R.A., Gibson W., Graves J.P., Sterling J.F., Eisenberg M.T.;
RT "The Drosophila suppressor of sable gene encodes a polypeptide with regions
RT similar to those of RNA-binding proteins.";
RL Mol. Cell. Biol. 11:894-905(1991).
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.
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 GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [GENOMIC DNA] OF 1-9.
RX PubMed=1963868; DOI=10.1093/genetics/126.4.1071;
RA Voelker R.A., Graves J.P., Gibson W., Eisenberg M.T.;
RT "Mobile element insertions causing mutations in the Drosophila suppressor
RT of sable locus occur in DNase I hypersensitive subregions of 5'-transcribed
RT nontranslated sequences.";
RL Genetics 126:1071-1082(1990).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9121479; DOI=10.1128/mcb.17.4.2291;
RA Murray M.V., Turnage M.A., Williamson K.J., Steinhauer W.R., Searles L.L.;
RT "The Drosophila suppressor of sable protein binds to RNA and associates
RT with a subset of polytene chromosome bands.";
RL Mol. Cell. Biol. 17:2291-2300(1997).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11027289; DOI=10.1128/mcb.20.21.8198-8208.2000;
RA Turnage M.A., Brewer-Jensen P., Bai W.L., Searles L.L.;
RT "Arginine-rich regions mediate the RNA binding and regulatory activities of
RT the protein encoded by the Drosophila melanogaster suppressor of sable
RT gene.";
RL Mol. Cell. Biol. 20:8198-8208(2000).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15082769; DOI=10.1128/mcb.24.9.3734-3746.2004;
RA Kuan Y.S., Brewer-Jensen P., Searles L.L.;
RT "Suppressor of sable, a putative RNA-processing protein, functions at the
RT level of transcription.";
RL Mol. Cell. Biol. 24:3734-3746(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524; THR-604; SER-663 AND
RP THR-664, 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).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19687295; DOI=10.1128/mcb.00039-09;
RA Kuan Y.S., Brewer-Jensen P., Bai W.L., Hunter C., Wilson C.B., Bass S.,
RA Abernethy J., Wing J.S., Searles L.L.;
RT "Drosophila suppressor of sable protein [Su(s)] promotes degradation of
RT aberrant and transposon-derived RNAs.";
RL Mol. Cell. Biol. 29:5590-5603(2009).
RN [12]
RP FUNCTION, AND INTERACTION WITH WDR82.
RX PubMed=26577379; DOI=10.1261/rna.048819.114;
RA Brewer-Jensen P., Wilson C.B., Abernethy J., Mollison L., Card S.,
RA Searles L.L.;
RT "Suppressor of sable [Su(s)] and Wdr82 down-regulate RNA from heat-shock-
RT inducible repetitive elements by a mechanism that involves transcription
RT termination.";
RL RNA 22:139-154(2016).
CC -!- FUNCTION: RNA-binding protein that suppresses transcription of some
CC RNAs (PubMed:1703632, PubMed:9121479, PubMed:11027289, PubMed:15082769,
CC PubMed:19687295, PubMed:26577379). Together with Wdr82, part of a
CC transcription termination checkpoint that promotes transcription
CC termination of RNAs and their subsequent degradation by the nuclear
CC exosome (PubMed:26577379). Promotes transcription termination of
CC aberrant RNAs, transcripts from genes containing a transposon inserted
CC at their very 5' end or RNAs from heat-shock-inducible repetitive
CC element (PubMed:1703632, PubMed:19687295, PubMed:26577379). Binds RNA
CC preferentially at a sequence that resembles a cryptic 5'-splice site
CC (PubMed:9121479). {ECO:0000269|PubMed:11027289,
CC ECO:0000269|PubMed:15082769, ECO:0000269|PubMed:1703632,
CC ECO:0000269|PubMed:19687295, ECO:0000269|PubMed:26577379,
CC ECO:0000269|PubMed:9121479}.
CC -!- SUBUNIT: Interacts with Wdr82. {ECO:0000269|PubMed:26577379}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11027289,
CC ECO:0000269|PubMed:1703632, ECO:0000269|PubMed:9121479}. Chromosome
CC {ECO:0000269|PubMed:15082769, ECO:0000269|PubMed:19687295}.
CC Note=Localizes to polytene chromosomes. {ECO:0000269|PubMed:15082769,
CC ECO:0000269|PubMed:19687295}.
CC -!- DEVELOPMENTAL STAGE: At all stages. {ECO:0000269|PubMed:1703632}.
CC -!- SIMILARITY: Belongs to the suppressor of sable family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL49185.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M57889; AAA28920.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45534.1; -; Genomic_DNA.
DR EMBL; AL031581; CAA20886.1; -; Genomic_DNA.
DR EMBL; AY071563; AAL49185.1; ALT_FRAME; mRNA.
DR EMBL; X59364; CAA42010.1; -; Genomic_DNA.
DR PIR; T13386; T13386.
DR RefSeq; NP_001284753.1; NM_001297824.1.
DR RefSeq; NP_476754.1; NM_057406.4.
DR AlphaFoldDB; P22293; -.
DR SMR; P22293; -.
DR BioGRID; 57580; 8.
DR DIP; DIP-19699N; -.
DR IntAct; P22293; 25.
DR STRING; 7227.FBpp0070115; -.
DR iPTMnet; P22293; -.
DR PaxDb; P22293; -.
DR PRIDE; P22293; -.
DR DNASU; 31012; -.
DR EnsemblMetazoa; FBtr0070120; FBpp0070115; FBgn0003575.
DR EnsemblMetazoa; FBtr0340082; FBpp0309081; FBgn0003575.
DR GeneID; 31012; -.
DR KEGG; dme:Dmel_CG6222; -.
DR CTD; 31012; -.
DR FlyBase; FBgn0003575; su(sable).
DR VEuPathDB; VectorBase:FBgn0003575; -.
DR eggNOG; KOG1040; Eukaryota.
DR HOGENOM; CLU_247398_0_0_1; -.
DR InParanoid; P22293; -.
DR OMA; HTPLRWQ; -.
DR OrthoDB; 272743at2759; -.
DR PhylomeDB; P22293; -.
DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 31012; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31012; -.
DR PRO; PR:P22293; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003575; Expressed in embryonic/larval hemocyte (Drosophila) and 25 other tissues.
DR ExpressionAtlas; P22293; baseline and differential.
DR Genevisible; P22293; DM.
DR GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:0032785; P:negative regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0071027; P:nuclear RNA surveillance; IDA:UniProtKB.
DR InterPro; IPR045124; Su(sable)-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR13119; PTHR13119; 1.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Transcription termination; Zinc; Zinc-finger.
FT CHAIN 1..1325
FT /note="Protein suppressor of sable"
FT /id="PRO_0000072321"
FT ZN_FING 330..357
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 358..381
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..327
FT /note="Highly charged"
FT REGION 499..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 149..179
FT /evidence="ECO:0000255"
FT COILED 276..296
FT /evidence="ECO:0000255"
FT COILED 444..478
FT /evidence="ECO:0000255"
FT COMPBIAS 9..30
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..664
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1014
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 604
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 664
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 687
FT /note="E -> G (in Ref. 5; AAL49185)"
FT /evidence="ECO:0000305"
FT CONFLICT 720..722
FT /note="Missing (in Ref. 1; AAA28920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1325 AA; 143840 MW; D5710DCF441DD48F CRC64;
MSVALADEPL IDLEEDLEDG EIDDDEEDEQ QSSKIQVQKK TFVGDDDVQF VGVEAKNQND
DEDVVYVGPS TDAVCLQNSN STKSKKPRPL EDDHASSIEL AIANALKKKG IEPPMPRMRS
SNQDTSDQSL EGSGEGLATA NPLLQSTRSS RRRKRKKERE REQKKDKEQQ NRSRRDENDV
SVVPGGVEDM DEYEMMNVRG GSPPPGGAAP PLSSCGQRFS GADWDMDDGS AATGAAGLGA
GGGGGYNSHS SYDSYSDEET NGPGLMNQRR RTRRDNEKEH QRGVNNRKRR DRDRLEGGLA
GSGSKRNRRD SGEGGGGGQE KMGGSNRVEP RKLELCKFYL MDCCAKRDKC SYMHKEFPCK
YYYLGMDCYA GDDCLFYHGE PLSEQLRNVL LKHMETAPKE ILGDFKRISR DIAIVQMTRR
HEQLCDQLNR ENTWNSIGCG LMGKRQDHQM QQQQQQLQHQ QLQQQQEQQQ TQQQAAADGG
GCIPSLLDMV INPPLSENKR KSRWTEKMGA KAAAGAAGSS ERDSTSPDAK PLPPHLDLAN
LSHVLSAENM AKLNKLGITN LEQMLQVPFG QLTEAGLTLV EIGEIQRKAE DAKPQTQAEL
ESSTPPSKRE TEANNSNSKS NGLIMVDYTQ YLKDAHVSFS GNDPLDDDRD DDEQLIIDDG
NDSTAEEDQQ PKKAKAPPAA THESSTEEAP LPSVFDLPSF MNNMLGQGSS ARQLLPASAT
SPNQENAHLP GGDQSTHKSA PIGGGTSTNV LGRILFGDKQ SDPEARAAFY RDIIRNPFKA
HSGDGDVDSS NENSNSNSHS LTPTPTPEPG SQSPKPEDHD QDMPELPVIA PALPPTTPSL
YVRRSMYDFD PVKEQEHGRQ ELLTEEKEQY QRDTDMRLPF EPMKHYMPAT EIDAAIFSHT
PIRWQLHEVT IEESSYAQIR ASALHKEQRE LRDPRMRRIL GLPETPDNSG PLGSVPIMGP
SSFSVDNIAR CATTIASPDL ETAVRDSTPS SPPPSVVNLP SMSVPPPSMR VPPPNIQVEK
PTVRTDPRRD PRRAVLQAPT KGASTANTTA PNASGGSKQI SEIRSLLQVS NWYNNLGTNN
KIMVNQQLAL VFTELKKFHQ LPNDAPKIFD VSFIVNNTTL QQIFAKLFIF VDDNGEVVQI
PEEPNGNGAA LGGGGDSGGG VGGGGGGGGV VLPNLSQPPP NLSQMLRLPP PNIRMLRMSG
MMMQMGNVGP PFNQPPPRGG LMGMPPNGNG LNQGVGNLGG LGQLGINQGG GPVPNGNPFN
PFGGNNGGGA GVMNNMNSMG NMGMGFNNFN NNGGRGGHFP GGGSGGNGNG NNRNQRGGNH
RNRNI
