ID PRDM6_HUMAN Reviewed; 595 AA. AC Q9NQX0; B5MCJ4; Q9NQW9; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 2. DT 27-MAR-2024, entry version 184. DE RecName: Full=Putative histone-lysine N-methyltransferase PRDM6; DE EC=2.1.1.361 {ECO:0000250|UniProtKB:Q3UZD5}; DE AltName: Full=PR domain zinc finger protein 6; DE AltName: Full=PR domain-containing protein 6; GN Name=PRDM6; Synonyms=PFM3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). RX PubMed=10668202; DOI=10.14670/hh-15.109; RA Jiang G.L., Huang S.; RT "The yin-yang of PR-domain family genes in tumorigenesis."; RL Histol. Histopathol. 15:109-117(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [3] RP INVOLVEMENT IN PDA3, AND VARIANTS PDA3 SER-263; ARG-462 AND GLN-549. RX PubMed=27181681; DOI=10.1016/j.ajhg.2016.03.022; RA Li N., Subrahmanyan L., Smith E., Yu X., Zaidi S., Choi M., Mane S., RA Nelson-Williams C., Bahjati M., Kazemi M., Hashemi M., Fathzadeh M., RA Narayanan A., Tian L., Montazeri F., Mani M., Begleiter M.L., Coon B.G., RA Lynch H.T., Olson E.N., Zhao H., Ruland J., Lifton R.P., Mani A.; RT "Mutations in the histone modifier PRDM6 are associated with isolated RT nonsyndromic patent ductus arteriosus."; RL Am. J. Hum. Genet. 98:1082-1091(2016). CC -!- FUNCTION: Putative histone methyltransferase that acts as a CC transcriptional repressor of smooth muscle gene expression. Promotes CC the transition from differentiated to proliferative smooth muscle by CC suppressing differentiation and maintaining the proliferative potential CC of vascular smooth muscle cells. Also plays a role in endothelial cells CC by inhibiting endothelial cell proliferation, survival and CC differentiation. It is unclear whether it has histone methyltransferase CC activity in vivo. According to some authors, it does not act as a CC histone methyltransferase by itself and represses transcription by CC recruiting EHMT2/G9a. According to others, it possesses histone CC methyltransferase activity when associated with other proteins and CC specifically methylates 'Lys-20' of histone H4 in vitro. 'Lys-20' CC methylation represents a specific tag for epigenetic transcriptional CC repression. {ECO:0000250|UniProtKB:Q3UZD5}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) + CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361; CC Evidence={ECO:0000250|UniProtKB:Q3UZD5}; CC -!- SUBUNIT: Interacts with HDAC1, HDAC2, HDAC3, CBX1 and EP300. CC {ECO:0000250|UniProtKB:Q3UZD5}. CC -!- INTERACTION: CC Q9NQX0; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-11320284, EBI-11096309; CC Q9NQX0; P21549: AGXT; NbExp=3; IntAct=EBI-11320284, EBI-727098; CC Q9NQX0; O43865: AHCYL1; NbExp=3; IntAct=EBI-11320284, EBI-2371423; CC Q9NQX0; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-11320284, EBI-8643161; CC Q9NQX0; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-11320284, EBI-11954519; CC Q9NQX0; P29972: AQP1; NbExp=3; IntAct=EBI-11320284, EBI-745213; CC Q9NQX0; Q03989: ARID5A; NbExp=3; IntAct=EBI-11320284, EBI-948603; CC Q9NQX0; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-11320284, EBI-745689; CC Q9NQX0; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-11320284, EBI-1166928; CC Q9NQX0; O95817: BAG3; NbExp=3; IntAct=EBI-11320284, EBI-747185; CC Q9NQX0; Q9H503-2: BANF2; NbExp=3; IntAct=EBI-11320284, EBI-11977289; CC Q9NQX0; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-11320284, EBI-11524452; CC Q9NQX0; O43439-4: CBFA2T2; NbExp=3; IntAct=EBI-11320284, EBI-11954144; CC Q9NQX0; Q9HC52: CBX8; NbExp=3; IntAct=EBI-11320284, EBI-712912; CC Q9NQX0; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-11320284, EBI-744556; CC Q9NQX0; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-11320284, EBI-10961624; CC Q9NQX0; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-11320284, EBI-10175300; CC Q9NQX0; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-11320284, EBI-2836773; CC Q9NQX0; Q8IYX8: CEP57L1; NbExp=3; IntAct=EBI-11320284, EBI-1104570; CC Q9NQX0; P10606: COX5B; NbExp=3; IntAct=EBI-11320284, EBI-1053725; CC Q9NQX0; P33240: CSTF2; NbExp=3; IntAct=EBI-11320284, EBI-711360; CC Q9NQX0; Q14241: ELOA; NbExp=3; IntAct=EBI-11320284, EBI-742350; CC Q9NQX0; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-11320284, EBI-744099; CC Q9NQX0; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-11320284, EBI-371876; CC Q9NQX0; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-11320284, EBI-6658203; CC Q9NQX0; Q14192: FHL2; NbExp=3; IntAct=EBI-11320284, EBI-701903; CC Q9NQX0; Q9NU39: FOXD4L1; NbExp=3; IntAct=EBI-11320284, EBI-11320806; CC Q9NQX0; O43559: FRS3; NbExp=3; IntAct=EBI-11320284, EBI-725515; CC Q9NQX0; Q9C0B1-2: FTO; NbExp=3; IntAct=EBI-11320284, EBI-18138793; CC Q9NQX0; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-11320284, EBI-372506; CC Q9NQX0; P55040: GEM; NbExp=3; IntAct=EBI-11320284, EBI-744104; CC Q9NQX0; O95872: GPANK1; NbExp=3; IntAct=EBI-11320284, EBI-751540; CC Q9NQX0; A8MXD5: GRXCR1; NbExp=3; IntAct=EBI-11320284, EBI-5235612; CC Q9NQX0; P31273: HOXC8; NbExp=3; IntAct=EBI-11320284, EBI-1752118; CC Q9NQX0; Q14005-2: IL16; NbExp=3; IntAct=EBI-11320284, EBI-17178971; CC Q9NQX0; Q8NA54: IQUB; NbExp=3; IntAct=EBI-11320284, EBI-10220600; CC Q9NQX0; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-11320284, EBI-2556193; CC Q9NQX0; Q92993: KAT5; NbExp=3; IntAct=EBI-11320284, EBI-399080; CC Q9NQX0; Q7L273: KCTD9; NbExp=3; IntAct=EBI-11320284, EBI-4397613; CC Q9NQX0; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-11320284, EBI-14069005; CC Q9NQX0; P25800: LMO1; NbExp=3; IntAct=EBI-11320284, EBI-8639312; CC Q9NQX0; P25791-3: LMO2; NbExp=3; IntAct=EBI-11320284, EBI-11959475; CC Q9NQX0; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-11320284, EBI-2341787; CC Q9NQX0; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-11320284, EBI-5662487; CC Q9NQX0; O43639: NCK2; NbExp=3; IntAct=EBI-11320284, EBI-713635; CC Q9NQX0; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-11320284, EBI-11750983; CC Q9NQX0; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-11320284, EBI-10271199; CC Q9NQX0; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-11320284, EBI-11022007; CC Q9NQX0; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-11320284, EBI-10232538; CC Q9NQX0; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-11320284, EBI-11320284; CC Q9NQX0; P54646: PRKAA2; NbExp=3; IntAct=EBI-11320284, EBI-1383852; CC Q9NQX0; Q13882: PTK6; NbExp=3; IntAct=EBI-11320284, EBI-1383632; CC Q9NQX0; P47897: QARS1; NbExp=3; IntAct=EBI-11320284, EBI-347462; CC Q9NQX0; O75771: RAD51D; NbExp=3; IntAct=EBI-11320284, EBI-1055693; CC Q9NQX0; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-11320284, EBI-1378139; CC Q9NQX0; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-11320284, EBI-11984663; CC Q9NQX0; Q9UPU9-3: SAMD4A; NbExp=3; IntAct=EBI-11320284, EBI-11986417; CC Q9NQX0; O75716: STK16; NbExp=3; IntAct=EBI-11320284, EBI-749295; CC Q9NQX0; Q9Y4C2-2: TCAF1; NbExp=3; IntAct=EBI-11320284, EBI-11974855; CC Q9NQX0; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-11320284, EBI-750487; CC Q9NQX0; Q08117-2: TLE5; NbExp=3; IntAct=EBI-11320284, EBI-11741437; CC Q9NQX0; Q14142: TRIM14; NbExp=3; IntAct=EBI-11320284, EBI-2820256; CC Q9NQX0; Q53H54: TRMT12; NbExp=3; IntAct=EBI-11320284, EBI-10242598; CC Q9NQX0; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-11320284, EBI-744794; CC Q9NQX0; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-11320284, EBI-10241197; CC Q9NQX0; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-11320284, EBI-3918381; CC Q9NQX0; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-11320284, EBI-9090990; CC Q9NQX0; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-11320284, EBI-7353612; CC Q9NQX0; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-11320284, EBI-11975223; CC Q9NQX0; Q68DK2-5: ZFYVE26; NbExp=3; IntAct=EBI-11320284, EBI-8656416; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3UZD5}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9NQX0-3; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=Q9NQX0-2; Sequence=VSP_036348, VSP_006929; CC Name=3; Synonyms=A; CC IsoId=Q9NQX0-1; Sequence=VSP_036348; CC -!- DISEASE: Patent ductus arteriosus 3 (PDA3) [MIM:617039]: A congenital CC heart defect characterized by the persistent opening of fetal ductus CC arteriosus that fails to close after birth. Fetal ductus arteriosus CC connects the pulmonary artery to the descending aorta, allowing CC unoxygenated blood to bypass the lung and flow to the placenta. CC Normally, the ductus occludes shortly after birth. CC {ECO:0000269|PubMed:27181681}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF78078.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAF78079.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AF272898; AAF78078.1; ALT_INIT; mRNA. DR EMBL; AF272899; AAF78079.1; ALT_INIT; mRNA. DR EMBL; AC008548; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC106786; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS47259.1; -. [Q9NQX0-3] DR RefSeq; NP_001129711.1; NM_001136239.1. [Q9NQX0-3] DR AlphaFoldDB; Q9NQX0; -. DR SMR; Q9NQX0; -. DR BioGRID; 125009; 83. DR IntAct; Q9NQX0; 72. DR MINT; Q9NQX0; -. DR STRING; 9606.ENSP00000384725; -. DR ChEMBL; CHEMBL5214858; -. DR iPTMnet; Q9NQX0; -. DR PhosphoSitePlus; Q9NQX0; -. DR BioMuta; PRDM6; -. DR DMDM; 223590133; -. DR MassIVE; Q9NQX0; -. DR PaxDb; 9606-ENSP00000384725; -. DR PeptideAtlas; Q9NQX0; -. DR ProteomicsDB; 82215; -. [Q9NQX0-3] DR ProteomicsDB; 82216; -. [Q9NQX0-1] DR Pumba; Q9NQX0; -. DR Antibodypedia; 25663; 120 antibodies from 17 providers. DR DNASU; 93166; -. DR Ensembl; ENST00000407847.5; ENSP00000384725.3; ENSG00000061455.11. [Q9NQX0-3] DR GeneID; 93166; -. DR KEGG; hsa:93166; -. DR MANE-Select; ENST00000407847.5; ENSP00000384725.3; NM_001136239.4; NP_001129711.1. DR UCSC; uc003kti.4; human. [Q9NQX0-3] DR AGR; HGNC:9350; -. DR CTD; 93166; -. DR DisGeNET; 93166; -. DR GeneCards; PRDM6; -. DR HGNC; HGNC:9350; PRDM6. DR HPA; ENSG00000061455; Tissue enhanced (intestine, urinary bladder). DR MalaCards; PRDM6; -. DR MIM; 616982; gene. DR MIM; 617039; phenotype. DR neXtProt; NX_Q9NQX0; -. DR OpenTargets; ENSG00000061455; -. DR Orphanet; 466729; Familial patent arterial duct. DR PharmGKB; PA33718; -. DR VEuPathDB; HostDB:ENSG00000061455; -. DR eggNOG; KOG1721; Eukaryota. DR eggNOG; KOG2461; Eukaryota. DR GeneTree; ENSGT00940000155852; -. DR HOGENOM; CLU_032452_0_0_1; -. DR InParanoid; Q9NQX0; -. DR OMA; NMTVVQY; -. DR OrthoDB; 5342037at2759; -. DR PhylomeDB; Q9NQX0; -. DR TreeFam; TF106403; -. DR BioCyc; MetaCyc:HS00755-MONOMER; -. DR PathwayCommons; Q9NQX0; -. DR SignaLink; Q9NQX0; -. DR BioGRID-ORCS; 93166; 24 hits in 1175 CRISPR screens. DR GenomeRNAi; 93166; -. DR Pharos; Q9NQX0; Tbio. DR PRO; PR:Q9NQX0; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9NQX0; Protein. DR Bgee; ENSG00000061455; Expressed in descending thoracic aorta and 124 other cell types or tissues. DR ExpressionAtlas; Q9NQX0; baseline and differential. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0140944; F:histone H4K20 monomethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL. DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR CDD; cd19191; PR-SET_PRDM6; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3. DR Gene3D; 2.170.270.10; SET domain; 1. DR InterPro; IPR044416; PRDM6_PR-SET. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR16515:SF22; HISTONE-LYSINE N-METHYLTRANSFERASE PRDM6-RELATED; 1. DR PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1. DR Pfam; PF21549; PRDM2_PR; 1. DR Pfam; PF00096; zf-C2H2; 3. DR SMART; SM00317; SET; 1. DR SMART; SM00355; ZnF_C2H2; 4. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2. DR SUPFAM; SSF82199; SET domain; 1. DR PROSITE; PS50280; SET; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4. DR Genevisible; Q9NQX0; HS. PE 1: Evidence at protein level; KW Alternative splicing; Chromatin regulator; Disease variant; Metal-binding; KW Methyltransferase; Nucleus; Reference proteome; Repeat; Repressor; KW S-adenosyl-L-methionine; Transcription; Transcription regulation; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1..595 FT /note="Putative histone-lysine N-methyltransferase PRDM6" FT /id="PRO_0000047762" FT DOMAIN 246..365 FT /note="SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT ZN_FING 473..495 FT /note="C2H2-type 1; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 501..523 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 529..551 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 557..579 FT /note="C2H2-type 4; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 27..90 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 47..71 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 73..90 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..182 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:10668202" FT /id="VSP_036348" FT VAR_SEQ 314..595 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10668202" FT /id="VSP_006929" FT VARIANT 263 FT /note="C -> S (in PDA3; uncertain significance; FT dbSNP:rs879255279)" FT /evidence="ECO:0000269|PubMed:27181681" FT /id="VAR_077014" FT VARIANT 462 FT /note="Q -> R (in PDA3; dbSNP:rs879253872)" FT /evidence="ECO:0000269|PubMed:27181681" FT /id="VAR_077015" FT VARIANT 549 FT /note="R -> Q (in PDA3; dbSNP:rs879255278)" FT /evidence="ECO:0000269|PubMed:27181681" FT /id="VAR_077016" SQ SEQUENCE 595 AA; 64452 MW; DB8D815E7C107451 CRC64; MLKPGDPGGS AFLKVDPAYL QHWQQLFPHG GAGPLKGSGA AGLLSAPQPL QPPPPPPPPE RAEPPPDSLR PRPASLSSAS STPASSSTSA SSASSCAAAA AAAALAGLSA LPVSQLPVFA PLAAAAVAAE PLPPKELCLG ATSGPGPVKC GGGGGGGGEG RGAPRFRCSA EELDYYLYGQ QRMEIIPLNQ HTSDPNNRCD MCADNRNGEC PMHGPLHSLR RLVGTSSAAA AAPPPELPEW LRDLPREVCL CTSTVPGLAY GICAAQRIQQ GTWIGPFQGV LLPPEKVQAG AVRNTQHLWE IYDQDGTLQH FIDGGEPSKS SWMRYIRCAR HCGEQNLTVV QYRSNIFYRA CIDIPRGTEL LVWYNDSYTS FFGIPLQCIA QDENLNVPST VMEAMCRQDA LQPFNKSSKL APTTQQRSVV FPQTPCSRNF SLLDKSGPIE SGFNQINVKN QRVLASPTST SQLHSEFSDW HLWKCGQCFK TFTQRILLQM HVCTQNPDRP YQCGHCSQSF SQPSELRNHV VTHSSDRPFK CGYCGRAFAG ATTLNNHIRT HTGEKPFKCE RCERSFTQAT QLSRHQRMPN ECKPITESPE SIEVD //