ZFP57_MOUSE
ID ZFP57_MOUSE Reviewed; 421 AA.
AC Q8C6P8; Q3UT94; Q62515; Q6JPI1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Zinc finger protein 57;
DE Short=Zfp-57;
GN Name=Zfp57;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=129; TISSUE=Testis;
RX PubMed=8120052; DOI=10.1016/s0021-9258(17)37460-4;
RA Okazaki S., Tanase S., Choudhury B.K., Setoyama K., Miura R., Ogawa M.,
RA Setoyama C.;
RT "A novel nuclear protein with zinc fingers down-regulated during early
RT mammalian cell differentiation.";
RL J. Biol. Chem. 269:6900-6907(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND INDUCTION BY LIF.
RC TISSUE=Embryonic stem cell, and Testis;
RX PubMed=15070898; DOI=10.1074/jbc.m400415200;
RA Alonso M.B., Zoidl G., Taveggia C., Bosse F., Zoidl C., Rahman M.,
RA Parmantier E., Dean C.H., Harris B.S., Wrabetz L., Mueller H.W.,
RA Jessen K.R., Mirsky R.;
RT "Identification and characterization of ZFP-57, a novel zinc finger
RT transcription factor in the mammalian peripheral nervous system.";
RL J. Biol. Chem. 279:25653-25664(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Egg, and Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INDUCTION.
RX PubMed=14732407; DOI=10.1016/j.ydbio.2003.09.041;
RA Ahn J.-I., Lee K.-H., Shin D.-M., Shim J.-W., Lee J.-S., Chang S.Y.,
RA Lee Y.-S., Brownstein M.J., Lee S.-H., Lee Y.-S.;
RT "Comprehensive transcriptome analysis of differentiation of embryonic stem
RT cells into midbrain and hindbrain neurons.";
RL Dev. Biol. 265:491-501(2004).
RN [6]
RP INDUCTION.
RX PubMed=15845352; DOI=10.1016/j.bbrc.2005.03.118;
RA Akagi T., Usuda M., Matsuda T., Ko M.S.H., Niwa H., Asano M., Koide H.,
RA Yokota T.;
RT "Identification of Zfp-57 as a downstream molecule of STAT3 and Oct-3/4 in
RT embryonic stem cells.";
RL Biochem. Biophys. Res. Commun. 331:23-30(2005).
RN [7]
RP INDUCTION.
RX PubMed=17938240; DOI=10.1101/gad.1588207;
RA Loh Y.-H., Zhang W., Chen X., George J., Ng H.H.;
RT "Jmjd1a and Jmjd2c histone H3 Lys 9 demethylases regulate self-renewal in
RT embryonic stem cells.";
RL Genes Dev. 21:2545-2557(2007).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18854139; DOI=10.1016/j.devcel.2008.08.014;
RA Li X., Ito M., Zhou F., Youngson N., Zuo X., Leder P., Ferguson-Smith A.C.;
RT "A maternal-zygotic effect gene, Zfp57, maintains both maternal and
RT paternal imprints.";
RL Dev. Cell 15:547-557(2008).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=18622393; DOI=10.1038/ng.187;
RA Mackay D.J.G., Callaway J.L.A., Marks S.M., White H.E., Acerini C.L.,
RA Boonen S.E., Dayanikli P., Firth H.V., Goodship J.A., Haemers A.P.,
RA Hahnemann J.M.D., Kordonouri O., Masoud A.F., Oestergaard E., Storr J.,
RA Ellard S., Hattersley A.T., Robinson D.O., Temple I.K.;
RT "Hypomethylation of multiple imprinted loci in individuals with transient
RT neonatal diabetes is associated with mutations in ZFP57.";
RL Nat. Genet. 40:949-951(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30602440; DOI=10.1101/gad.320069.118;
RA Takahashi N., Coluccio A., Thorball C.W., Planet E., Shi H., Offner S.,
RA Turelli P., Imbeault M., Ferguson-Smith A.C., Trono D.;
RT "ZNF445 is a primary regulator of genomic imprinting.";
RL Genes Dev. 33:49-54(2019).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (0.99 ANGSTROMS) OF 137-195 IN COMPLEX WITH
RP METHYLATED DNA, AND FUNCTION.
RX PubMed=23059534; DOI=10.1101/gad.202200.112;
RA Liu Y., Toh H., Sasaki H., Zhang X., Cheng X.;
RT "An atomic model of Zfp57 recognition of CpG methylation within a specific
RT DNA sequence.";
RL Genes Dev. 26:2374-2379(2012).
CC -!- FUNCTION: Transcription regulator required to maintain maternal and
CC paternal gene imprinting, a process by which gene expression is
CC restricted in a parent of origin-specific manner by epigenetic
CC modification of genomic DNA and chromatin, including DNA methylation.
CC Acts by controlling DNA methylation during the earliest multicellular
CC stages of development at multiple imprinting control regions (ICRs)
CC (PubMed:15070898, PubMed:18854139, PubMed:23059534, PubMed:30602440).
CC Acts together with ZNF445, but ZFP57 plays the predominant role in
CC imprinting maintenance. In contrast, in humans, ZNF445 seems to be the
CC major factor early embryonic imprinting maintenance (PubMed:30602440).
CC Required for the establishment of maternal methylation imprints at
CC SNRPN locus. Acts as a transcriptional repressor in Schwann cells.
CC Binds to a 5'-TGCCGC-3' consensus sequence and recognizes the
CC methylated CpG within this element (PubMed:15070898, PubMed:18854139,
CC PubMed:23059534). {ECO:0000269|PubMed:15070898,
CC ECO:0000269|PubMed:18854139, ECO:0000269|PubMed:23059534,
CC ECO:0000269|PubMed:30602440}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15070898,
CC ECO:0000269|PubMed:18854139, ECO:0000269|PubMed:8120052}. Note=Binds
CC various differentially methylated regions (DMR), including the Snrpn
CC DMR.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C6P8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C6P8-2; Sequence=VSP_026331;
CC -!- TISSUE SPECIFICITY: Expressed in oocytes and in a subset of adult
CC tissues. Expressed at high levels in testis, and at low levels in
CC cerebellum. Present in sciatic nerve and spinal cord (at protein
CC level). {ECO:0000269|PubMed:15070898, ECO:0000269|PubMed:8120052}.
CC -!- DEVELOPMENTAL STAGE: Expression peaks between 11 dpc and 17 dpc, and
CC decreases from P0 to P28. Expressed in lung throughout embryonic
CC development. At 12 dpc, expressed in spinal cord, dorsal root ganglia
CC and sciatic nerve. At 15 dpc, highly expressed in all neural tissues.
CC At P0, expressed in brain and spinal cord. Present in Schwann cells at
CC 16 dpc and P0 (at protein level). Maternal product is present in
CC preimplantation embryos. Expressed in pluripotent embryonic stem cells.
CC Down-regulated when embryonic stem cells differentiate.
CC {ECO:0000269|PubMed:15070898, ECO:0000269|PubMed:18622393,
CC ECO:0000269|PubMed:18854139, ECO:0000269|PubMed:8120052}.
CC -!- INDUCTION: Up-regulated by LIF. Down-regulated during differentiation
CC of embryonic stem cells, or during retinoic acid-induced
CC differentiation of F9 cells (at protein level). Regulated by JMJD1A,
CC which mediates histone H3K9Me2 demethylation at its promoter, thereby
CC activating expression. {ECO:0000269|PubMed:14732407,
CC ECO:0000269|PubMed:15070898, ECO:0000269|PubMed:15845352,
CC ECO:0000269|PubMed:17938240, ECO:0000269|PubMed:8120052}.
CC -!- DOMAIN: The KRAB domain is required for function as transcriptional
CC repressor.
CC -!- DOMAIN: Zinc fingers 2 and 3 mediate recognition of the target element,
CC ZF2 interacting with the 5' half (TGC) and ZF3 interacting with the 3'
CC half (CGC).
CC -!- DISRUPTION PHENOTYPE: Affects the maintenance of DNA methylation
CC imprints. The absence of just the zygotic function causes partial
CC neonatal lethality, whereas eliminating both the maternal and zygotic
CC functions results in a highly penetrant embryonic lethality. In
CC oocytes, its absence results in failure to establish maternal
CC methylation imprints at the Snrpn imprinted region. Intriguingly,
CC methylation imprints are reacquired specifically at the maternally
CC derived Snrpn imprinted region when the zygotic Zfp57 is present in
CC embryos (PubMed:18854139, PubMed:30602440). Double zygotic mutations of
CC ZFP57 and ZNF445 are embryonically lethal and embryos show no gross
CC morphological abnormalities but significant reduction in size and
CC weight at 11.5 dpc, a phenotype more pronounced than in ZFP57 mutant
CC mice with a more severe loss of impinting (PubMed:30602440).
CC {ECO:0000269|PubMed:18854139, ECO:0000269|PubMed:30602440}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR04560.1; Type=Miscellaneous discrepancy; Note=Numerous sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; D21850; BAA04876.1; -; mRNA.
DR EMBL; AY344233; AAR04560.1; ALT_SEQ; mRNA.
DR EMBL; AK054083; BAC35649.1; -; mRNA.
DR EMBL; AK136241; BAE22892.1; -; mRNA.
DR EMBL; AK139625; BAE24086.1; -; mRNA.
DR EMBL; AK145368; BAE26393.1; -; mRNA.
DR EMBL; BC052028; AAH52028.1; -; mRNA.
DR CCDS; CCDS28733.1; -. [Q8C6P8-1]
DR CCDS; CCDS50106.1; -. [Q8C6P8-2]
DR PIR; A54375; A54375.
DR RefSeq; NP_001013767.1; NM_001013745.2. [Q8C6P8-1]
DR RefSeq; NP_001161973.1; NM_001168501.1. [Q8C6P8-1]
DR RefSeq; NP_001161974.1; NM_001168502.1. [Q8C6P8-2]
DR RefSeq; XP_006524287.1; XM_006524224.1. [Q8C6P8-1]
DR RefSeq; XP_017172947.1; XM_017317458.1.
DR RefSeq; XP_017172948.1; XM_017317459.1. [Q8C6P8-2]
DR PDB; 4GZN; X-ray; 0.99 A; C=137-195.
DR PDB; 4M9V; X-ray; 0.97 A; C/F=137-195.
DR PDBsum; 4GZN; -.
DR PDBsum; 4M9V; -.
DR AlphaFoldDB; Q8C6P8; -.
DR SMR; Q8C6P8; -.
DR BioGRID; 204670; 8.
DR STRING; 10090.ENSMUSP00000065811; -.
DR iPTMnet; Q8C6P8; -.
DR PhosphoSitePlus; Q8C6P8; -.
DR MaxQB; Q8C6P8; -.
DR PaxDb; Q8C6P8; -.
DR PeptideAtlas; Q8C6P8; -.
DR PRIDE; Q8C6P8; -.
DR ProteomicsDB; 275358; -. [Q8C6P8-1]
DR ProteomicsDB; 275359; -. [Q8C6P8-2]
DR Antibodypedia; 26080; 219 antibodies from 19 providers.
DR DNASU; 22715; -.
DR Ensembl; ENSMUST00000069250; ENSMUSP00000065811; ENSMUSG00000036036. [Q8C6P8-1]
DR Ensembl; ENSMUST00000089968; ENSMUSP00000087414; ENSMUSG00000036036. [Q8C6P8-2]
DR Ensembl; ENSMUST00000174524; ENSMUSP00000134418; ENSMUSG00000036036. [Q8C6P8-1]
DR Ensembl; ENSMUST00000174672; ENSMUSP00000133821; ENSMUSG00000036036. [Q8C6P8-1]
DR GeneID; 22715; -.
DR KEGG; mmu:22715; -.
DR UCSC; uc008clu.2; mouse. [Q8C6P8-2]
DR UCSC; uc008clv.2; mouse. [Q8C6P8-1]
DR CTD; 346171; -.
DR MGI; MGI:99204; Zfp57.
DR VEuPathDB; HostDB:ENSMUSG00000036036; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00390000002599; -.
DR HOGENOM; CLU_677857_0_0_1; -.
DR InParanoid; Q8C6P8; -.
DR OMA; CGKLFWS; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8C6P8; -.
DR TreeFam; TF337947; -.
DR BioGRID-ORCS; 22715; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Zfp57; mouse.
DR PRO; PR:Q8C6P8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8C6P8; protein.
DR Bgee; ENSMUSG00000036036; Expressed in cortical plate and 136 other tissues.
DR ExpressionAtlas; Q8C6P8; baseline and differential.
DR Genevisible; Q8C6P8; MM.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043045; P:DNA methylation involved in embryo development; IMP:UniProtKB.
DR GO; GO:0071514; P:genomic imprinting; IMP:MGI.
DR GO; GO:0010216; P:maintenance of DNA methylation; IGI:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IMP:UniProtKB.
DR GO; GO:2000653; P:regulation of genetic imprinting; IGI:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..421
FT /note="Zinc finger protein 57"
FT /id="PRO_0000291965"
FT DOMAIN 15..88
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 90..113
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 140..162
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 168..190
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 264..286
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 313..332
FT /note="C2H2-type 5; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 191..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 178
FT /note="Crucial for 5-methylcytosine recognition"
FT VAR_SEQ 7..9
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026331"
FT CONFLICT 75
FT /note="E -> K (in Ref. 1; BAA04876)"
FT /evidence="ECO:0000305"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4M9V"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:4M9V"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:4M9V"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:4M9V"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:4M9V"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:4M9V"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:4M9V"
SQ SEQUENCE 421 AA; 47959 MW; C341340FFB5B490A CRC64;
MAARKQSSQP SRTPVSYEDV AVSFTQEEWE YLTSTQKTLY QKVMSETFKN LTFVGSKKKP
QEPSSDLQDK NEEQEKSSSC TGVFKGGPFF FCLTCGKCFK KNTFLFNHQF PVRSRRLAVT
NPQSRKGKGY KAQHRGERPF FCNFCGKTYR DASGLSRHRR AHLGYRPRSC PECGKCFRDQ
SEVNRHLKVH QNKPAASNQA GNQASNQRLK SRVPPTTPRS QAPALKYVKV IQGPVARAKA
RNSGASTLNV RSNSITVVRS REKISCPYCH ITFTMRTCLL THLKIHFRRQ PNQHFCCKES
AHSSNTLRMQ KIYTCPVCDS SFRGKESLLD HLCCQRPIRF SKCWEILGHL LGYLHEPVVL
GNIFKVRDSS GKRMESRRRR RKRACTENPE TEGLSGKGRV APWEMEGATS PESPVTEEDS
D
