SMBT_DROME
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-AUG-2022, entry version 166.
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.
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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 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 OMA; NDVDNGM; -.
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:0042393; F:histone binding; IBA:GO_Central.
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 assembly; 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:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR CDD; cd09580; SAM_Scm-like-4MBT; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.30.60.160; -; 1.
DR InterPro; IPR004092; Mbt.
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 Pfam; PF02820; MBT; 4.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00561; MBT; 4.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
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
