PRDM6_HUMAN
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 03-AUG-2022, entry version 175.
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; 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; 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; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-11320284, EBI-8643161;
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; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-11320284, EBI-745689;
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};
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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; 82.
DR IntAct; Q9NQX0; 72.
DR MINT; Q9NQX0; -.
DR STRING; 9606.ENSP00000384725; -.
DR iPTMnet; Q9NQX0; -.
DR PhosphoSitePlus; Q9NQX0; -.
DR BioMuta; PRDM6; -.
DR DMDM; 223590133; -.
DR MassIVE; Q9NQX0; -.
DR PaxDb; Q9NQX0; -.
DR PeptideAtlas; Q9NQX0; -.
DR PRIDE; Q9NQX0; -.
DR ProteomicsDB; 82215; -. [Q9NQX0-3]
DR ProteomicsDB; 82216; -. [Q9NQX0-1]
DR Antibodypedia; 25663; 110 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 CTD; 93166; -.
DR DisGeNET; 93166; -.
DR GeneCards; PRDM6; -.
DR HGNC; HGNC:9350; PRDM6.
DR HPA; ENSG00000061455; Tissue enhanced (urinary).
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; IGPFQGI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9NQX0; -.
DR TreeFam; TF106403; -.
DR BioCyc; MetaCyc:HS00755-MON; -.
DR PathwayCommons; Q9NQX0; -.
DR SignaLink; Q9NQX0; -.
DR BioGRID-ORCS; 93166; 24 hits in 1096 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 123 other tissues.
DR ExpressionAtlas; Q9NQX0; baseline and differential.
DR Genevisible; Q9NQX0; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; 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; 2.170.270.10; -; 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 Pfam; PF00856; SET; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
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; unknown pathological 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
