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};
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; 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 Genevisible; Q80TS5; MM.
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.
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
//
