ID SMBT_DROME Reviewed; 1220 AA. AC Q9VK33; Q7KTB5; Q9VK32; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 2. DT 03-MAY-2023, entry version 170. DE RecName: Full=Polycomb protein Sfmbt; DE AltName: Full=Scm-like with four MBT domain-containing protein 1; DE AltName: Full=dSfmbt; GN Name=Sfmbt {ECO:0000303|PubMed:16618800}; ORFNames=CG16975; 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] {ECO:0000312|EMBL:AAF53249.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132}; 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 [2] {ECO:0000305, ECO:0000312|EMBL:AAF53249.2} 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 [3] {ECO:0000305, ECO:0000312|EMBL:AAO74694.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO74694.1}; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A., RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000305} RP FUNCTION, INTERACTION WITH PHO, AND SUBCELLULAR LOCATION. RC TISSUE=Embryo {ECO:0000269|PubMed:16618800}; RX PubMed=16618800; DOI=10.1101/gad.377406; RA Klymenko T., Papp B., Fischle W., Koecher T., Schelder M., Fritsch C., RA Wild B., Wilm M., Mueller J.; RT "A Polycomb group protein complex with sequence-specific DNA-binding and RT selective methyl-lysine-binding activities."; RL Genes Dev. 20:1110-1122(2006). CC -!- FUNCTION: Polycomb group (PcG) protein that binds to the Polycomb CC response elements (PREs) found in the regulatory regions of many genes. CC PcG proteins act by forming multiprotein complexes, which are required CC to maintain the transcriptionally repressive state of homeotic genes CC throughout development. PcG proteins are not required to initiate CC repression, but to maintain it during later stages of development. They CC probably act via the methylation of histones, rendering chromatin CC heritably changed in its expressibility. Necessary but not sufficient CC to recruit a functional PcG repressive complex that represses target CC genes, suggesting that the recruitment of the distinct PRC1 complex is CC also required to allow a subsequent repression. CC {ECO:0000269|PubMed:16618800}. CC -!- SUBUNIT: Interacts with pho as a component of the pho-repressive CC complex (PhoRC). {ECO:0000269|PubMed:16618800}. CC -!- INTERACTION: CC Q9VK33; Q8ST83: pho; NbExp=6; IntAct=EBI-117801, EBI-125201; CC Q9VK33; Q9VSZ3: phol; NbExp=2; IntAct=EBI-117801, EBI-176113; CC Q9VK33; P84243: H3-3B; Xeno; NbExp=15; IntAct=EBI-117801, EBI-120658; CC Q9VK33; P62805: H4C9; Xeno; NbExp=10; IntAct=EBI-117801, EBI-302023; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16618800}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B {ECO:0000269|PubMed:10731132}; CC IsoId=Q9VK33-1; Sequence=Displayed; CC Name=A {ECO:0000269|PubMed:10731132}; CC IsoId=Q9VK33-2; Sequence=VSP_052548; CC -!- DOMAIN: MBT repeats have unique discriminatory binding activity for CC methylated Lys residues in H3 and H4; the MBT repeats bind mono- and CC dimethylated H3K9Me1, H3K9Me2, H4K20Me1 and H4K20Me2 but fail to CC interact with these residues if they are unmodified or trimethylated. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014134; AAF53249.2; -; Genomic_DNA. DR EMBL; AE014134; AAF53250.2; -; Genomic_DNA. DR EMBL; BT006011; AAO74694.1; -; mRNA. DR RefSeq; NP_001260432.1; NM_001273503.1. [Q9VK33-1] DR RefSeq; NP_609606.2; NM_135762.3. [Q9VK33-1] DR RefSeq; NP_723786.1; NM_165026.2. [Q9VK33-2] DR PDB; 3H6Z; X-ray; 2.80 A; A/B=535-977. DR PDB; 4C5E; X-ray; 1.95 A; A/B/C/D=531-980. DR PDB; 4C5G; X-ray; 2.10 A; A=531-980. DR PDB; 4C5H; X-ray; 3.20 A; A=531-980. DR PDB; 5J8Y; X-ray; 1.98 A; C/D=1137-1220. DR PDBsum; 3H6Z; -. DR PDBsum; 4C5E; -. DR PDBsum; 4C5G; -. DR PDBsum; 4C5H; -. DR PDBsum; 5J8Y; -. DR AlphaFoldDB; Q9VK33; -. DR SMR; Q9VK33; -. DR BioGRID; 60747; 25. DR IntAct; Q9VK33; 8. DR MINT; Q9VK33; -. DR STRING; 7227.FBpp0288419; -. DR PaxDb; Q9VK33; -. DR EnsemblMetazoa; FBtr0080491; FBpp0080069; FBgn0032475. [Q9VK33-2] DR EnsemblMetazoa; FBtr0080492; FBpp0080070; FBgn0032475. [Q9VK33-1] DR EnsemblMetazoa; FBtr0333236; FBpp0305438; FBgn0032475. [Q9VK33-1] DR GeneID; 34709; -. DR KEGG; dme:Dmel_CG16975; -. DR AGR; FB:FBgn0032475; -. DR CTD; 34709; -. DR FlyBase; FBgn0032475; Sfmbt. DR VEuPathDB; VectorBase:FBgn0032475; -. DR eggNOG; KOG3766; Eukaryota. DR GeneTree; ENSGT00940000169237; -. DR HOGENOM; CLU_005352_1_1_1; -. DR InParanoid; Q9VK33; -. DR Reactome; R-DME-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-DME-8953750; Transcriptional Regulation by E2F6. DR SignaLink; Q9VK33; -. DR BioGRID-ORCS; 34709; 0 hits in 3 CRISPR screens. DR EvolutionaryTrace; Q9VK33; -. DR GenomeRNAi; 34709; -. DR PRO; PR:Q9VK33; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0032475; Expressed in cleaving embryo and 33 other tissues. DR ExpressionAtlas; Q9VK33; baseline and differential. DR Genevisible; Q9VK33; DM. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0031519; C:PcG protein complex; IPI:FlyBase. DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0035064; F:methylated histone binding; IDA:FlyBase. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0031507; P:heterochromatin formation; IDA:FlyBase. DR GO; GO:0007446; P:imaginal disc growth; IMP:FlyBase. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase. DR GO; GO:0048477; P:oogenesis; IMP:FlyBase. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR CDD; cd20119; MBT_dSfmbt_rpt1; 1. DR CDD; cd20122; MBT_dSfmbt_rpt2; 1. DR CDD; cd20125; MBT_dSfmbt_rpt3; 1. DR CDD; cd20128; MBT_dSfmbt_rpt4; 1. DR CDD; cd09580; SAM_Scm-like-4MBT; 1. DR Gene3D; 2.30.30.140; -; 4. DR Gene3D; 3.30.60.160; -; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR InterPro; IPR004092; Mbt. DR InterPro; IPR047358; MBT_dSfmbt_rpt1. DR InterPro; IPR047359; MBT_dSfmbt_rpt2. DR InterPro; IPR047360; MBT_dSfmbt_rpt3. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR037605; Sfmbt_SAM. DR InterPro; IPR012313; Znf_FCS. DR InterPro; IPR038603; Znf_FCS_sf. DR PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1. DR PANTHER; PTHR12247:SF104; POLYCOMB PROTEIN SFMBT; 1. DR Pfam; PF02820; MBT; 4. DR Pfam; PF00536; SAM_1; 1. DR SMART; SM00561; MBT; 4. DR SMART; SM00454; SAM; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 4. DR PROSITE; PS51079; MBT; 4. DR PROSITE; PS50105; SAM_DOMAIN; 1. DR PROSITE; PS51024; ZF_FCS; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; DNA-binding; KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..1220 FT /note="Polycomb protein Sfmbt" FT /id="PRO_0000306371" FT REPEAT 536..647 FT /note="MBT 1" FT /evidence="ECO:0000255" FT REPEAT 655..753 FT /note="MBT 2" FT /evidence="ECO:0000255" FT REPEAT 761..871 FT /note="MBT 3" FT /evidence="ECO:0000255" FT REPEAT 879..975 FT /note="MBT 4" FT /evidence="ECO:0000255" FT DOMAIN 1140..1203 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT ZN_FING 322..357 FT /note="FCS-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT REGION 371..399 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 464..483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 976..1024 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1050..1092 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1006..1022 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1052..1066 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1071..1092 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 331 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT BINDING 334 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT BINDING 351 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT BINDING 355 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT VAR_SEQ 1..352 FT /note="Missing (in isoform A)" FT /evidence="ECO:0000303|PubMed:10731132" FT /id="VSP_052548" FT HELIX 539..542 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 552..554 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 561..566 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 572..576 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 595..604 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 607..612 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 616..618 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 622..625 FT /evidence="ECO:0007829|PDB:4C5E" FT TURN 626..628 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 629..633 FT /evidence="ECO:0007829|PDB:4C5H" FT HELIX 636..639 FT /evidence="ECO:0007829|PDB:4C5E" FT TURN 648..652 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 658..665 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 675..681 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 692..697 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 700..713 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 716..721 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 727..731 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 742..746 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 749..751 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 754..761 FT /evidence="ECO:0007829|PDB:4C5E" FT TURN 762..766 FT /evidence="ECO:0007829|PDB:3H6Z" FT HELIX 777..779 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 786..788 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 803..808 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 811..823 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 828..833 FT /evidence="ECO:0007829|PDB:4C5E" FT TURN 841..844 FT /evidence="ECO:0007829|PDB:3H6Z" FT STRAND 846..849 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 860..863 FT /evidence="ECO:0007829|PDB:4C5E" FT TURN 876..878 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 881..888 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 895..897 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 912..916 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 924..933 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 936..941 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 946..948 FT /evidence="ECO:0007829|PDB:4C5E" FT STRAND 950..953 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 964..968 FT /evidence="ECO:0007829|PDB:4C5E" FT HELIX 1137..1139 FT /evidence="ECO:0007829|PDB:5J8Y" FT HELIX 1142..1151 FT /evidence="ECO:0007829|PDB:5J8Y" FT HELIX 1155..1157 FT /evidence="ECO:0007829|PDB:5J8Y" FT HELIX 1158..1163 FT /evidence="ECO:0007829|PDB:5J8Y" FT HELIX 1168..1171 FT /evidence="ECO:0007829|PDB:5J8Y" FT HELIX 1176..1182 FT /evidence="ECO:0007829|PDB:5J8Y" FT TURN 1183..1185 FT /evidence="ECO:0007829|PDB:5J8Y" FT HELIX 1187..1202 FT /evidence="ECO:0007829|PDB:5J8Y" SQ SEQUENCE 1220 AA; 133666 MW; 2BE2785144CA051F CRC64; MNPSELRMMW MSSQYNSERI TLEDAATLLG HPTVGLSVME DLSAHQPTLD MNPMMSLMGG DFTGQAAATA AALGVQPGTL IATNSNNLYG FAHMGGLQQQ LLQQSAAAAV FQNYAEAMDN DVENGMVGMA MEAVVDDDDQ VYGQRDNNFD DNGSELEPKQ EIINIDDFVM MNEDNNSYDG TDFMTSSDKD ISQSSSSCMA QMPGSLGVPG VEHDLLVPLP DGLLHHKLLG TTLVPAMGTL NGNAFGNIMV STENTSSKQM QRTYSTAKGA NSTATTATCS ASTSSALRSQ RKTRKIEPVN RPGLVLKTPI AYRGNIDPSV IPIQKDGMAV CKRCGAIGVK HTFYTKSRRF CSMACARGEL YSLVLNTKME GDQATTSSPD PGAGSESADL PGDQQQSQSD IELDLHAAHI KNANYRFRIT DQSKITQLNS FGEPMSMGGD AAANNVQMAA DETIAALNGG AVGDATAPGS TEEGASTPNS YLSAAPTPKA LRLFKDIYPQ DDLPQIPKYE RLPVPCPQME KIISIRRRMY DPTHSYDWLP RLSKENFNAA PVTCFPHAPG CEVWDNLGVG MKVEVENTDC DSIEVIQPGQ TPTSFWVATI LEIKGYKALM SYEGFDTDSH DFWVNLCNAE VHSVGWCATR GKPLIPPRTI EHKYKDWKDF LVGRLSGART LPSNFYNKIN DSLQSRFRLG LNLECVDKDR ISQVRLATVT KIVGKRLFLR YFDSDDGFWC HEDSPIIHPV GWATTVGHNL AAPQDYLERM LAGREAMIEV HEDDATIELF KMNFTFDEYY SDGKTNSFVE GMKLEAVDPL NLSSICPATV MAVLKFGYMM IRIDSYQPDA SGSDWFCYHE KSPCIFPAGF CSVNNISVTP PNGYDSRTFT WEGYLRDTGA VAAGQHLFHR IIPDHGFEVG MSLECADLMD PRLVCVATVA RVVGRLLKVH FDGWTDEYDQ WLDCESADIY PVGWCVLVNH KLEGPPRVAH QQAPKPAPKP KIQRKRKPKK GAAGGKTPTD NNTQSVKSRT IALKTTPHLP KLSIKLELKP EHHNAAFYEN NQPEEEGDEE DPDADGDGDG STSHISEQST TQSSSDLIAG SGSGSGSASL VTLATGSNKT NSSATNNKYI PRLADIDSSE PHLELVPDTW NVYDVSQFLR VNDCTAHCDT FSRNKIDGKR LLQLTKDDIM PLLGMKVGPA LKISDLIAQL KCKVNPGRAR SHKTNKSPFL //