ID   ZN423_MOUSE             Reviewed;        1292 AA.
AC   Q80TS5; B2RSW4; Q6PCP2; Q6X497; Q8CIQ1; Q9ESD2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Zinc finger protein 423;
DE   AltName: Full=Early B-cell factor-associated zinc finger protein;
DE   AltName: Full=Olf1/EBF-associated zinc finger protein;
DE   AltName: Full=Smad- and Olf-interacting zinc finger protein;
GN   Name=Znf423; Synonyms=Ebfaz, Kiaa0760, Nur12, Oaz, Zfp423;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=15048087; DOI=10.1038/sj.onc.1207452;
RA   Warming S., Suzuki T., Yamaguchi T.P., Jenkins N.A., Copeland N.G.;
RT   "Early B-cell factor-associated zinc-finger gene is a frequent target of
RT   retroviral integration in murine B-cell lymphomas.";
RL   Oncogene 23:2727-2731(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 92-1292.
RA   Croci L., Corradi A., Vauti F., Wurst W., Rocchi M., Consalez G.G.;
RT   "cDNA sequence and map assignment of Ebfaz, orthologous to the zinc finger
RT   transcription factor gene Roaz.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH PARP1.
RX   PubMed=14623329; DOI=10.1016/j.bbrc.2003.10.053;
RA   Ku M.-C., Stewart S., Hata A.;
RT   "Poly(ADP-ribose) polymerase 1 interacts with OAZ and regulates BMP-target
RT   genes.";
RL   Biochem. Biophys. Res. Commun. 311:702-707(2003).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=16943432; DOI=10.1128/mcb.02255-05;
RA   Warming S., Rachel R.A., Jenkins N.A., Copeland N.G.;
RT   "Zfp423 is required for normal cerebellar development.";
RL   Mol. Cell. Biol. 26:6913-6922(2006).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=17151198; DOI=10.1073/pnas.0609184103;
RA   Alcaraz W.A., Gold D.A., Raponi E., Gent P.M., Concepcion D.,
RA   Hamilton B.A.;
RT   "Zfp423 controls proliferation and differentiation of neural precursors in
RT   cerebellar vermis formation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:19424-19429(2006).
RN   [8]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=17524391; DOI=10.1016/j.ydbio.2007.04.005;
RA   Cheng L.E., Zhang J., Reed R.R.;
RT   "The transcription factor Zfp423/OAZ is required for cerebellar development
RT   and CNS midline patterning.";
RL   Dev. Biol. 307:43-52(2007).
RN   [9]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17521568; DOI=10.1016/j.neuron.2007.04.029;
RA   Cheng L.E., Reed R.R.;
RT   "Zfp423/OAZ participates in a developmental switch during olfactory
RT   neurogenesis.";
RL   Neuron 54:547-557(2007).
CC   -!- FUNCTION: Transcription factor that can both act as an activator or a
CC       repressor depending on the context. Plays a central role in BMP
CC       signaling and olfactory neurogenesis. Associates with SMADs in response
CC       to BMP2 leading to activate transcription of BMP target genes. Acts as
CC       a transcriptional repressor via its interaction with EBF1, a
CC       transcription factor involved in terminal olfactory receptor neurons
CC       differentiation; this interaction preventing EBF1 to bind DNA and
CC       activate olfactory-specific genes. Involved in olfactory neurogenesis
CC       by participating in a developmental switch that regulates the
CC       transition from differentiation to maturation in olfactory receptor
CC       neurons. Controls proliferation and differentiation of neural
CC       precursors in cerebellar vermis formation.
CC       {ECO:0000269|PubMed:16943432, ECO:0000269|PubMed:17151198,
CC       ECO:0000269|PubMed:17521568, ECO:0000269|PubMed:17524391}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with SMAD1 and SMAD4.
CC       Interacts with EBF1 (By similarity). Interacts with PARP1. Interacts
CC       with CEP290 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80TS5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TS5-2; Sequence=VSP_029008;
CC   -!- TISSUE SPECIFICITY: Within the cerebellum, Zfp423 is expressed in both
CC       ventricular and external germinal zones. Transiently expressed in newly
CC       differentiating olfactory-receptor neurons.
CC       {ECO:0000269|PubMed:16943432, ECO:0000269|PubMed:17151198,
CC       ECO:0000269|PubMed:17521568}.
CC   -!- DEVELOPMENTAL STAGE: During embryogenesis, it is highly expressed at
CC       the dorsal neuroepithelium flanking the roof plate.
CC       {ECO:0000269|PubMed:17524391}.
CC   -!- DOMAIN: Uses different DNA- and protein-binding zinc fingers to
CC       regulate the distinct BMP-Smad and Olf signaling pathways. C2H2-type
CC       zinc fingers 14-19 mediate the interaction with SMAD1 and SMAD4, while
CC       zinc fingers 28-30 mediate the interaction with EBF1. zinc fingers 2-8
CC       bind the 5'-CCGCCC-3' DNA sequence in concert with EBF1, while zinc
CC       fingers 9-13 bind BMP target gene promoters in concert with SMADs (By
CC       similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice are runted and ataxic, the cerebellum is
CC       underdeveloped, and the vermis is severely reduced, resulting in
CC       diminished proliferation by granule cell precursors in the external
CC       germinal layer, especially near the midline, and abnormal
CC       differentiation and migration of ventricular zone-derived neurons and
CC       Bergmann glia. In the remaining cerebellar structures, the Purkinje
CC       cells are poorly developed and mislocalized.
CC       {ECO:0000269|PubMed:16943432, ECO:0000269|PubMed:17151198}.
CC   -!- MISCELLANEOUS: Znf423 gene is a frequent target of retroviral
CC       integration in murine B-cell lymphomas.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG17053.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH59234.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
CC       Sequence=BAC65647.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY147407; AAN39840.1; -; mRNA.
DR   EMBL; AY256893; AAP33073.1; -; mRNA.
DR   EMBL; AK122365; BAC65647.1; ALT_INIT; mRNA.
DR   EMBL; BC059234; AAH59234.1; ALT_SEQ; mRNA.
DR   EMBL; BC139028; AAI39029.1; -; mRNA.
DR   EMBL; BC139030; AAI39031.1; -; mRNA.
DR   EMBL; AF188609; AAG17053.1; ALT_INIT; mRNA.
DR   CCDS; CCDS52627.1; -. [Q80TS5-1]
DR   RefSeq; NP_201584.2; NM_033327.2. [Q80TS5-1]
DR   AlphaFoldDB; Q80TS5; -.
DR   BMRB; Q80TS5; -.
DR   BioGRID; 220465; 42.
DR   IntAct; Q80TS5; 2.
DR   STRING; 10090.ENSMUSP00000105282; -.
DR   iPTMnet; Q80TS5; -.
DR   PhosphoSitePlus; Q80TS5; -.
DR   MaxQB; Q80TS5; -.
DR   PaxDb; 10090-ENSMUSP00000105282; -.
DR   ProteomicsDB; 275013; -. [Q80TS5-1]
DR   ProteomicsDB; 275014; -. [Q80TS5-2]
DR   ABCD; Q80TS5; 1 sequenced antibody.
DR   Antibodypedia; 28187; 140 antibodies from 26 providers.
DR   DNASU; 94187; -.
DR   Ensembl; ENSMUST00000052250.15; ENSMUSP00000052379.9; ENSMUSG00000045333.16. [Q80TS5-2]
DR   Ensembl; ENSMUST00000109655.9; ENSMUSP00000105282.3; ENSMUSG00000045333.16. [Q80TS5-1]
DR   GeneID; 94187; -.
DR   KEGG; mmu:94187; -.
DR   UCSC; uc009mqv.1; mouse. [Q80TS5-1]
DR   AGR; MGI:1891217; -.
DR   CTD; 94187; -.
DR   MGI; MGI:1891217; Zfp423.
DR   VEuPathDB; HostDB:ENSMUSG00000045333; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000158492; -.
DR   InParanoid; Q80TS5; -.
DR   OMA; RDEGQGW; -.
DR   OrthoDB; 3073634at2759; -.
DR   PhylomeDB; Q80TS5; -.
DR   TreeFam; TF331504; -.
DR   BioGRID-ORCS; 94187; 2 hits in 82 CRISPR screens.
DR   ChiTaRS; Zfp423; mouse.
DR   PRO; PR:Q80TS5; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q80TS5; Protein.
DR   Bgee; ENSMUSG00000045333; Expressed in embryonic post-anal tail and 213 other cell types or tissues.
DR   ExpressionAtlas; Q80TS5; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IMP:MGI.
DR   GO; GO:0050873; P:brown fat cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IMP:MGI.
DR   GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IDA:UniProtKB.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB.
DR   GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR   GO; GO:0050872; P:white fat cell differentiation; IMP:BHF-UCL.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 13.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24406:SF8; C2H2-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR24406; TRANSCRIPTIONAL REPRESSOR CTCFL-RELATED; 1.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   Pfam; PF13912; zf-C2H2_6; 2.
DR   SMART; SM00355; ZnF_C2H2; 30.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 10.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 27.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 23.
DR   Genevisible; Q80TS5; MM.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Developmental protein; Differentiation;
KW   DNA-binding; Metal-binding; Neurogenesis; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1292
FT                   /note="Zinc finger protein 423"
FT                   /id="PRO_0000308596"
FT   ZN_FING         75..101
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         146..168
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         174..196
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         202..224
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         230..252
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         271..294
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         303..326
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         331..353
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         417..441
FT                   /note="C2H2-type 9; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         449..472
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         488..511
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         525..548
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         571..596
FT                   /note="C2H2-type 13; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         640..662
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         670..692
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         700..723
FT                   /note="C2H2-type 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         728..751
FT                   /note="C2H2-type 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         758..781
FT                   /note="C2H2-type 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         789..811
FT                   /note="C2H2-type 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         815..838
FT                   /note="C2H2-type 20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         894..916
FT                   /note="C2H2-type 21; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         938..960
FT                   /note="C2H2-type 22"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         967..989
FT                   /note="C2H2-type 23"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1028..1050
FT                   /note="C2H2-type 24"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1072..1090
FT                   /note="C2H2-type 25; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1128..1151
FT                   /note="C2H2-type 26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1176..1198
FT                   /note="C2H2-type 27"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1206..1228
FT                   /note="C2H2-type 28"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1237..1260
FT                   /note="C2H2-type 29"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1267..1290
FT                   /note="C2H2-type 30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          33..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1144..1171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1144..1158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M1K9"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M1K9"
FT   MOD_RES         612
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M1K9"
FT   MOD_RES         1062
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M1K9"
FT   VAR_SEQ         1..33
FT                   /note="MSRRKQAKPRSVKVEEGEASDFSLAWDSSVAAA -> MTGAERGPLCYH
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15048087"
FT                   /id="VSP_029008"
FT   CONFLICT        735
FT                   /note="E -> K (in Ref. 4; AAG17053)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1182
FT                   /note="Q -> R (in Ref. 1; AAP33073/AAN39840)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1292 AA;  145351 MW;  6E0EE26DDCF65E63 CRC64;
     MSRRKQAKPR SVKVEEGEAS DFSLAWDSSV AAAGGLEGEP ECDRKTSRAL EDRNSVTSQE
     ERNEDDEDVE DESIYTCDHC QQDFESLADL TDHRAHRCPG DGDDDPQLSW VASSPSSKDV
     ASPTQMIGDG CDLGLGEEEG GTGLPYPCQF CDKSFIRLSY LKRHEQIHSD KLPFKCTFCS
     RLFKHKRSRD RHIKLHTGDK KYHCHECEAA FSRSDHLKIH LKTHSSSKPF KCSVCKRGFS
     STSSLQSHMQ AHKKNKEHLA KSEKEAKKDD FMCDYCEDTF SQTEELEKHV LTLHPQLSEK
     ADLQCIHCPE VFVDESTLLA HIHQAHANQK HKCPMCPEQF SSVEGVYCHL DSHRQPDSSN
     HSVSPDPVLG SVASMSSATP DSSASVERGS TPDSTLKPLR GQKKMRDDGQ SWPKVVYSCP
     YCSKRDFTSL AVLEIHLKTI HADKPQQSHT CQICLDSMPT LYNLNEHVRK LHKSHAYPVM
     QFGNISAFHC NYCPEMFADI NSLQEHIRVS HCGPNANPPD GNNAFFCNQC SMGFLTESSL
     TEHIQQAHCS VGSTKLESPV VQPTQSFMEV YSCPYCTNSP IFGSILKLTK HIKENHKNIP
     LAHSKKSKAE QSPVSSDVEV SSPKRQRLSG SANSISNGEY PCNQCDLKFS NFESFQTHLK
     LHLELLLRKQ ACPQCKEDFD SQESLLQHLT VHYMTTSTHY VCESCDKQFS SVDDLQKHLL
     DMHTFVLYHC TLCQEVFDSK VSIQVHLAVK HSNEKKMYRC TACNWDFRKE ADLQVHVKHS
     HLGNPAKAHK CIFCGETFST EVELQCHITT HSKKYNCRFC SKAFHAVILL EKHLREKHCV
     FDAAAENGTA NGVPPTSTKK AEPADLQGML LKNPEAPNSH EASEDDVDAS EPMYGCDICG
     AAYTMEVLLQ NHRLRDHNIR PGEDDGSRKK AEFIKGSHKC NVCSRTFFSE NGLREHLQTH
     RGPAKHYMCP ICGERFPSLL TLTEHKVTHS KSLDTGTCRI CKMPLQSEEE FIEHCQMHPD
     LRNSLTGFRC VVCMQTVTST LELKIHGTFH MQKLAGSSAA SSPNGQGLQK LYKCALCLKE
     FRSKQDLVRL DVNGLPYGLC AGCMARSANG QVGGLAPPEP ADRPCAGLRC PECNVKFESA
     EDLESHMQVD HRDLTPETSG PRKGAQTSPV PRKKTYQCIK CQMTFENERE IQIHVANHMI
     EEGINHECKL CNQMFDSPAK LLCHLIEHSF EGMGGTFKCP VCFTVFVQAN KLQQHIFAVH
     GQEDKIYDCS QCPQKFFFQT ELQNHTMSQH AQ
//