PSC_DROME
ID PSC_DROME Reviewed; 1601 AA.
AC P35820; Q9V6I9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Polycomb group protein Psc;
DE AltName: Full=Protein posterior sex combs;
GN Name=Psc; ORFNames=CG3886;
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], AND FUNCTION.
RX PubMed=1833647; DOI=10.1038/353351a0;
RA Brunk B.P., Martin E.C., Sharp E., Adler P.N.;
RT "Drosophila genes Posterior Sex Combs and Suppressor two of zeste encode
RT proteins with homology to the murine bmi-1 oncogene.";
RL Nature 353:351-353(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Psce25;
RX PubMed=16024794; DOI=10.1128/mcb.25.15.6578-6591.2005;
RA King I.F.G., Emmons R.B., Francis N.J., Wild B., Mueller J., Kingston R.E.,
RA Wu C.-T.;
RT "Analysis of a polycomb group protein defines regions that link repressive
RT activity on nucleosomal templates to in vivo function.";
RL Mol. Cell. Biol. 25:6578-6591(2005).
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 IDENTIFICATION IN THE PRC1 COMPLEX WITH SCE; PC AND PH.
RX PubMed=11493925; DOI=10.1038/35088096;
RA Saurin A.J., Shao Z., Erdjument-Bromage H., Tempst P., Kingston R.E.;
RT "A Drosophila Polycomb group complex includes Zeste and dTAFII proteins.";
RL Nature 412:655-660(2001).
RN [6]
RP IDENTIFICATION IN A PCG COMPLEX WITH SCE; PC AND PH.
RX PubMed=11583617; DOI=10.1016/s1097-2765(01)00316-1;
RA Francis N.J., Saurin A.J., Shao Z., Kingston R.E.;
RT "Reconstitution of a functional core polycomb repressive complex.";
RL Mol. Cell 8:545-556(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656; SER-658; SER-1139;
RP THR-1222; THR-1236; THR-1251; SER-1253; SER-1266 AND SER-1274, AND
RP 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: Polycomb group (PcG) protein. PcG proteins act by forming
CC multiprotein complexes, which are required to maintain the
CC transcriptionally repressive state of homeotic genes throughout
CC development. PcG proteins are not required to initiate repression, but
CC to maintain it during later stages of development. Component of the PcG
CC multiprotein PRC1 complex, a complex that acts via chromatin remodeling
CC and modification of histones; it mediates monoubiquitination of histone
CC H2A 'Lys-118', rendering chromatin heritably changed in its
CC expressibility. Needed to maintain expression patterns of the homeotic
CC selector genes of the Antennapedia (Antp-C) and Bithorax (BX-C)
CC complexes, and hence for the maintenance of segmental determination.
CC {ECO:0000269|PubMed:1833647}.
CC -!- SUBUNIT: Component of PRC1 complex, which contains many PcG proteins
CC like Pc, ph, Scm, Psc, Sce and also chromatin-remodeling proteins such
CC as histone deacetylases. This complex is distinct from the Esc/E(z)
CC complex, at least composed of esc, E(z), Su(z)12, HDAC1/Rpd3 and Caf1-
CC 55. The 2 complexes however cooperate and interact together during the
CC first 3 hours of development to establish PcG silencing.
CC {ECO:0000269|PubMed:11493925, ECO:0000269|PubMed:11583617}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; X59275; CAA41965.1; -; mRNA.
DR EMBL; DQ022542; AAZ20646.1; -; mRNA.
DR EMBL; AE013599; AAF58434.1; -; Genomic_DNA.
DR PIR; S17983; S17983.
DR RefSeq; NP_001286368.1; NM_001299439.1.
DR RefSeq; NP_001286369.1; NM_001299440.1.
DR RefSeq; NP_523725.2; NM_079001.3.
DR AlphaFoldDB; P35820; -.
DR SMR; P35820; -.
DR BioGRID; 62201; 42.
DR IntAct; P35820; 7.
DR STRING; 7227.FBpp0086911; -.
DR iPTMnet; P35820; -.
DR PaxDb; P35820; -.
DR DNASU; 36431; -.
DR EnsemblMetazoa; FBtr0087798; FBpp0086911; FBgn0005624.
DR EnsemblMetazoa; FBtr0345196; FBpp0311395; FBgn0005624.
DR EnsemblMetazoa; FBtr0345375; FBpp0311526; FBgn0005624.
DR GeneID; 36431; -.
DR KEGG; dme:Dmel_CG3886; -.
DR CTD; 100653366; -.
DR FlyBase; FBgn0005624; Psc.
DR VEuPathDB; VectorBase:FBgn0005624; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000173039; -.
DR HOGENOM; CLU_257256_0_0_1; -.
DR InParanoid; P35820; -.
DR OMA; FVYDKFE; -.
DR OrthoDB; 1203951at2759; -.
DR PhylomeDB; P35820; -.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DME-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; P35820; -.
DR BioGRID-ORCS; 36431; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Psc; fly.
DR GenomeRNAi; 36431; -.
DR PRO; PR:P35820; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0005624; Expressed in eye disc (Drosophila) and 22 other tissues.
DR ExpressionAtlas; P35820; baseline and differential.
DR Genevisible; P35820; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0031519; C:PcG protein complex; IDA:FlyBase.
DR GO; GO:0035102; C:PRC1 complex; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:FlyBase.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF16207; RAWUL; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1601
FT /note="Polycomb group protein Psc"
FT /id="PRO_0000056388"
FT ZN_FING 263..302
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..823
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1192
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1236
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1251
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1266
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1274
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 23
FT /note="T -> TPEAT (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..96
FT /note="AAA -> T (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="T -> A (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="N -> T (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="P -> S (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="I -> T (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="P -> A (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 526..527
FT /note="EQ -> GE (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="M -> L (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 906
FT /note="A -> S (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="S -> T (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="S -> N (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 1279
FT /note="P -> A (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 1289
FT /note="A -> T (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
FT CONFLICT 1364..1366
FT /note="SQP -> PQS (in Ref. 1; CAA41965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1601 AA; 169833 MW; 7C6264A12CDF3D49 CRC64;
MMTPESKAIQ PAAATTKQTA EATATTTMAH TQQKSQLSTL AKTTTTTATN KAAKSVVSNA
NSSGNNSSKK LALSQSQKTT TTTTPPTTTT TTTAAAAAEA TTNADKMQKQ QQLKQQLFAA
CSIKVKSENT LATTANAALA AATTTTTTAT PALATGKAAK TILENGIKKE STPPAVESVE
ASSSSSSSSS SSSSSSSSWP TTRRATSEDA SSNGGASADE EKSEEDPTAA VAASSTATTT
SDLATTSRPR PVLLTAVNPH IICHLCQGYL INATTIVECL HSFCHSCLIN HLRKERFCPR
CEMVINNAKP NIKSDTTLQA IVYKLVPGLY ERELMRKRAF YKDRPEEAAL ATPEQRGDDT
EHLIFSPSDD MSLSLEYAEL GELKTDSEPE LVDTLRPRYL QCPAMCRVSH LKKFVYDKFE
IDAQRFSIDI MYKVKTIVLL DYYTLMDIAY IYTWKRDAPM RFYYRVYESP QPLVKPAPRR
VLPLKLEKQE RENQEQQLAV EVASSKVEPV SLPEDQKAEA SIKVEEQEST REIVKEVIKD
VAATPPTETL KLVINRNMLD KREKSHSPQM SSKSSSKSSP CTPVSSPSEP NIKLKIDLSK
QNSVTIIDMS DPERREIVKP LKPEKESRSK KKDKDGSPKS SSSSSSSSSG ERKRKSPSPL
TVPPLTIRTE RIMSPSGVST LSPRVTSGAF SEDPKSEFLK SFALKPIKVK VESPERTLNN
RAITPPSPSV QQSASPKSKG NNLDDSILMK PPSCMPPKSI ASSKRKSKEP VKAVSKKQKL
SPPLPTVDFK IRLPVTNGNS SGTASPKIEK PLMPPPAKPP MLAPRKLQPS AQFAPPPSPI
HHHAGVQMSA PGNRTPIAKR YQPILPKASR PNPFANIPND VNRLLKDAGT EIKSIGGGSV
ENNSNAAQKP HLYGPKGESK MGPPALPATT PSQGNKNVGK QAGNLPMSAP PNKGNSSNNY
LNLALFNSSK CKGKEAPPGC RTPMYTPNSP IYSPSSPQYV PSYNIPTMPT YKYTPKPTPN
SGSGNGGSGS YLQNMLGGGN GGSLGGLFPS PPTKSDQNTN PAQGGGGSSS ATQSGGNNGI
VNNNIYMPNE DAPEKQQVKV KSLLNSCNIN IPSSLSITIS RDNGDSSSPN NGQHPKHKSP
VNNYIEIVKL PDQPQDQVQA AKEAQKRQSP PAAVPGHLAA KLPPPPPSKA IPSPQHLVSR
MTPPQLPKVA TPPPPSSPRV ITPPKTSPPA NAAKVTPLKP VLTPTQVDKK TPSPEKRTAA
QMGSHSPTAS ENKSPKGGPA GVANSTGGAQ NGDPAAKKFR PILPRQNGMP ELAPKLPTLA
PFVGFNPLQN PAAGKKVPPS KKSPNAGAAA HQSGQQKLVN GGQSQPAQQK TSPPAQKNQQ
QVKKVSKNPT PPPPSLPAVG KMMPHPVMHS QNAPLSIASS ASAAAVASGQ LDLSNFLKEN
LRRVHAAQAA QAAQVAAAAN QSNMMYNLAQ MGHMTPAMYN YQQAYFREQL SRMQRVGNEV
FNDYLQKLKT AAATGGGGPV EGELKPMLPT VTLPSPGATP PAASPKTSPL PAGKLTAAAT
APQTKGNSSS GAANARQQTA ATGNNGATVP AASLPPATKS K
