ZIC1_HUMAN
ID ZIC1_HUMAN Reviewed; 447 AA.
AC Q15915; Q2M3N1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Zinc finger protein ZIC 1;
DE AltName: Full=Zinc finger protein 201;
DE AltName: Full=Zinc finger protein of the cerebellum 1;
GN Name=ZIC1; Synonyms=ZIC, ZNF201;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Cerebellum;
RX PubMed=8542595;
RA Yokota N., Aruga J., Takai S., Yamada K., Hamazaki M., Iwase T.,
RA Sugimura H., Mikoshiba K.;
RT "Predominant expression of human zic in cerebellar granule cell lineage and
RT medulloblastoma.";
RL Cancer Res. 56:377-383(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 INVOLVEMENT IN CRS6, VARIANT CRS6 ARG-400, INVOLVEMENT IN BAIDCS, VARIANTS
RP BAIDCS 388-SER--VAL-447 DEL; 389-GLN--VAL-447 DEL AND 402-GLU--VAL-447 DEL,
RP AND VARIANT ALA-414.
RX PubMed=26340333; DOI=10.1016/j.ajhg.2015.07.007;
RG WGS500 Consortium;
RA Twigg S.R., Forecki J., Goos J.A., Richardson I.C., Hoogeboom A.J.,
RA van den Ouweland A.M., Swagemakers S.M., Lequin M.H., Van Antwerp D.,
RA McGowan S.J., Westbury I., Miller K.A., Wall S.A., van der Spek P.J.,
RA Mathijssen I.M., Pauws E., Merzdorf C.S., Wilkie A.O.;
RT "Gain-of-function mutations in ZIC1 are associated with coronal
RT craniosynostosis and learning disability.";
RL Am. J. Hum. Genet. 97:378-388(2015).
RN [5]
RP INVOLVEMENT IN BAIDCS.
RX PubMed=30391508; DOI=10.1016/j.ejmg.2018.10.018;
RA Vandervore L.V., Schot R., Hoogeboom A.J.M., Lincke C., de Coo I.F.,
RA Lequin M.H., Dremmen M., van Unen L.M.A., Saris J.J., Jansen A.C.,
RA van Slegtenhorst M.A., Wilke M., Mancini G.M.S.;
RT "Mutated zinc finger protein of the cerebellum 1 leads to microcephaly,
RT cortical malformation, callosal agenesis, cerebellar dysplasia, tethered
RT cord and scoliosis.";
RL Eur. J. Med. Genet. 61:783-789(2018).
CC -!- FUNCTION: Acts as a transcriptional activator. Involved in
CC neurogenesis. Plays important roles in the early stage of organogenesis
CC of the CNS, as well as during dorsal spinal cord development and
CC maturation of the cerebellum. Involved in the spatial distribution of
CC mossy fiber (MF) neurons within the pontine gray nucleus (PGN). Plays a
CC role in the regulation of MF axon pathway choice. Promotes MF migration
CC towards ipsilaterally-located cerebellar territories. May have a role
CC in shear flow mechanotransduction in osteocytes. Retains nuclear GLI1
CC and GLI3 in the cytoplasm. Binds to the minimal GLI-consensus sequence
CC 5'-TGGGTGGTC-3' (By similarity). {ECO:0000250|UniProtKB:P46684}.
CC -!- SUBUNIT: Interacts (via the C2H2-type domains 3, 4 and 5) with MDFIC
CC (via the C2H2-type domains 3, 4 and 5). Interacts with GLI1; the
CC interaction enhances transcription activation. Interacts with GLI2.
CC Interacts with GLI3; the interaction enhances transcription activation
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q15915; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-11963196, EBI-12318443;
CC Q15915; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-11963196, EBI-357530;
CC Q15915; Q9NXR5-2: ANKRD10; NbExp=3; IntAct=EBI-11963196, EBI-12102070;
CC Q15915; Q03989: ARID5A; NbExp=3; IntAct=EBI-11963196, EBI-948603;
CC Q15915; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-11963196, EBI-12811889;
CC Q15915; Q9NR55: BATF3; NbExp=3; IntAct=EBI-11963196, EBI-10312707;
CC Q15915; Q96RK4: BBS4; NbExp=3; IntAct=EBI-11963196, EBI-1805814;
CC Q15915; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-11963196, EBI-2548012;
CC Q15915; Q9H5F2: C11orf1; NbExp=3; IntAct=EBI-11963196, EBI-718615;
CC Q15915; Q6NVV7: CDPF1; NbExp=3; IntAct=EBI-11963196, EBI-2802782;
CC Q15915; O43186: CRX; NbExp=3; IntAct=EBI-11963196, EBI-748171;
CC Q15915; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11963196, EBI-3867333;
CC Q15915; A0PJW8: DAPL1; NbExp=3; IntAct=EBI-11963196, EBI-12840152;
CC Q15915; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-11963196, EBI-742054;
CC Q15915; Q96AZ1: EEF1AKMT3; NbExp=3; IntAct=EBI-11963196, EBI-12108304;
CC Q15915; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-11963196, EBI-12193763;
CC Q15915; O75593: FOXH1; NbExp=3; IntAct=EBI-11963196, EBI-1759806;
CC Q15915; Q86XJ1: GAS2L3; NbExp=3; IntAct=EBI-11963196, EBI-9248152;
CC Q15915; Q5TA45: INTS11; NbExp=3; IntAct=EBI-11963196, EBI-748258;
CC Q15915; Q53HC5: KLHL26; NbExp=3; IntAct=EBI-11963196, EBI-724915;
CC Q15915; Q15323: KRT31; NbExp=3; IntAct=EBI-11963196, EBI-948001;
CC Q15915; O76011: KRT34; NbExp=3; IntAct=EBI-11963196, EBI-1047093;
CC Q15915; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-11963196, EBI-10171774;
CC Q15915; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-11963196, EBI-1052037;
CC Q15915; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-11963196, EBI-10210845;
CC Q15915; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-11963196, EBI-11953846;
CC Q15915; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-11963196, EBI-11992140;
CC Q15915; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-11963196, EBI-12811111;
CC Q15915; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-11963196, EBI-12196745;
CC Q15915; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-11963196, EBI-1048945;
CC Q15915; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-11963196, EBI-10241353;
CC Q15915; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-11963196, EBI-18395721;
CC Q15915; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-11963196, EBI-751260;
CC Q15915; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-11963196, EBI-12111050;
CC Q15915; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-11963196, EBI-11962084;
CC Q15915; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-11963196, EBI-18394498;
CC Q15915; Q8IUC2: KRTAP8-1; NbExp=5; IntAct=EBI-11963196, EBI-10261141;
CC Q15915; Q99732: LITAF; NbExp=3; IntAct=EBI-11963196, EBI-725647;
CC Q15915; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-11963196, EBI-716006;
CC Q15915; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-11963196, EBI-8487781;
CC Q15915; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-11963196, EBI-10271199;
CC Q15915; O43482: OIP5; NbExp=5; IntAct=EBI-11963196, EBI-536879;
CC Q15915; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-11963196, EBI-12813389;
CC Q15915; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-11963196, EBI-11022007;
CC Q15915; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-11963196, EBI-724639;
CC Q15915; Q9HDD0: PLAAT1; NbExp=3; IntAct=EBI-11963196, EBI-12387058;
CC Q15915; Q9NRY6: PLSCR3; NbExp=3; IntAct=EBI-11963196, EBI-750734;
CC Q15915; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-11963196, EBI-740343;
CC Q15915; Q04864-2: REL; NbExp=3; IntAct=EBI-11963196, EBI-10829018;
CC Q15915; P35250-2: RFC2; NbExp=3; IntAct=EBI-11963196, EBI-12936957;
CC Q15915; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-11963196, EBI-6257312;
CC Q15915; Q13485: SMAD4; NbExp=3; IntAct=EBI-11963196, EBI-347263;
CC Q15915; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-11963196, EBI-12275818;
CC Q15915; Q9H7B4: SMYD3; NbExp=3; IntAct=EBI-11963196, EBI-347919;
CC Q15915; Q99932-2: SPAG8; NbExp=5; IntAct=EBI-11963196, EBI-11959123;
CC Q15915; Q496A3: SPATS1; NbExp=3; IntAct=EBI-11963196, EBI-3923692;
CC Q15915; Q9UMX1: SUFU; NbExp=3; IntAct=EBI-11963196, EBI-740595;
CC Q15915; O60806: TBX19; NbExp=3; IntAct=EBI-11963196, EBI-12096770;
CC Q15915; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-11963196, EBI-11139477;
CC Q15915; Q08117-2: TLE5; NbExp=3; IntAct=EBI-11963196, EBI-11741437;
CC Q15915; Q13077: TRAF1; NbExp=3; IntAct=EBI-11963196, EBI-359224;
CC Q15915; Q15654: TRIP6; NbExp=3; IntAct=EBI-11963196, EBI-742327;
CC Q15915; Q86WV8: TSC1; NbExp=3; IntAct=EBI-11963196, EBI-12806590;
CC Q15915; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-11963196, EBI-10180829;
CC Q15915; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-11963196, EBI-12068150;
CC Q15915; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-11963196, EBI-12040603;
CC Q15915; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-11963196, EBI-17269964;
CC Q15915; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-11963196, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Localizes
CC in the cytoplasm in presence of MDFIC overexpression. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: CNS. A high level expression is seen in the
CC cerebellum. Detected in the nuclei of the cerebellar granule cell
CC lineage from the progenitor cells of the external germinal layer to the
CC postmigrated cells of the internal granular layer. Detected in
CC medulloblastoma (26/29 cases), but not present in all other tumors
CC examined. {ECO:0000269|PubMed:8542595}.
CC -!- DOMAIN: The C2H2-type 3, 4 and 5 zinc finger domains are necessary for
CC transcription activation. {ECO:0000250}.
CC -!- DISEASE: Craniosynostosis 6 (CRS6) [MIM:616602]: A form of
CC craniosynostosis, a primary abnormality of skull growth involving
CC premature fusion of one or more cranial sutures. The growth velocity of
CC the skull often cannot match that of the developing brain resulting in
CC an abnormal head shape and, in some cases, increased intracranial
CC pressure, which must be treated promptly to avoid permanent
CC neurodevelopmental disability. {ECO:0000269|PubMed:26340333}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Structural brain anomalies with impaired intellectual
CC development and craniosynostosis (BAIDCS) [MIM:618736]: A disease
CC characterized by microcephaly, agenesis of corpus callosum, abnormal
CC conformation of the ventricles and posterior fossa, hypoplasia of both
CC cerebellar hemispheres, colpocephaly, and partial absence of the
CC cerebellar vermis with fusion of the cerebellar hemispheres.
CC Intellectual development is moderately to severely impaired. Bicoronal
CC synostosis, scoliosis, and tethered cord may be present.
CC {ECO:0000269|PubMed:26340333, ECO:0000269|PubMed:30391508}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; D76435; BAA11179.1; -; mRNA.
DR EMBL; CH471052; EAW78915.1; -; Genomic_DNA.
DR EMBL; BC104848; AAI04849.1; -; mRNA.
DR EMBL; BC104850; AAI04851.1; -; mRNA.
DR CCDS; CCDS3136.1; -.
DR RefSeq; NP_003403.2; NM_003412.3.
DR AlphaFoldDB; Q15915; -.
DR SMR; Q15915; -.
DR BioGRID; 113377; 116.
DR IntAct; Q15915; 110.
DR STRING; 9606.ENSP00000282928; -.
DR iPTMnet; Q15915; -.
DR PhosphoSitePlus; Q15915; -.
DR BioMuta; ZIC1; -.
DR DMDM; 209572702; -.
DR jPOST; Q15915; -.
DR MassIVE; Q15915; -.
DR MaxQB; Q15915; -.
DR PaxDb; Q15915; -.
DR PeptideAtlas; Q15915; -.
DR PRIDE; Q15915; -.
DR ProteomicsDB; 60816; -.
DR Antibodypedia; 1317; 416 antibodies from 33 providers.
DR DNASU; 7545; -.
DR Ensembl; ENST00000282928.5; ENSP00000282928.4; ENSG00000152977.10.
DR GeneID; 7545; -.
DR KEGG; hsa:7545; -.
DR MANE-Select; ENST00000282928.5; ENSP00000282928.4; NM_003412.4; NP_003403.2.
DR UCSC; uc003ewe.4; human.
DR CTD; 7545; -.
DR DisGeNET; 7545; -.
DR GeneCards; ZIC1; -.
DR HGNC; HGNC:12872; ZIC1.
DR HPA; ENSG00000152977; Tissue enriched (brain).
DR MalaCards; ZIC1; -.
DR MIM; 600470; gene.
DR MIM; 616602; phenotype.
DR MIM; 618736; phenotype.
DR neXtProt; NX_Q15915; -.
DR OpenTargets; ENSG00000152977; -.
DR Orphanet; 269212; Isolated Dandy-Walker malformation with hydrocephalus.
DR Orphanet; 269215; Isolated Dandy-Walker malformation without hydrocephalus.
DR Orphanet; 35099; Non-syndromic bicoronal craniosynostosis.
DR PharmGKB; PA37461; -.
DR VEuPathDB; HostDB:ENSG00000152977; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160269; -.
DR HOGENOM; CLU_002678_37_1_1; -.
DR InParanoid; Q15915; -.
DR OMA; MKVHSKS; -.
DR OrthoDB; 768287at2759; -.
DR PhylomeDB; Q15915; -.
DR TreeFam; TF351425; -.
DR PathwayCommons; Q15915; -.
DR SignaLink; Q15915; -.
DR SIGNOR; Q15915; -.
DR BioGRID-ORCS; 7545; 13 hits in 1095 CRISPR screens.
DR ChiTaRS; ZIC1; human.
DR GeneWiki; ZIC1; -.
DR GenomeRNAi; 7545; -.
DR Pharos; Q15915; Tbio.
DR PRO; PR:Q15915; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q15915; protein.
DR Bgee; ENSG00000152977; Expressed in paraflocculus and 142 other tissues.
DR ExpressionAtlas; Q15915; baseline and differential.
DR Genevisible; Q15915; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
DR GO; GO:0098727; P:maintenance of cell number; IEA:Ensembl.
DR GO; GO:0021772; P:olfactory bulb development; IEA:Ensembl.
DR GO; GO:0007389; P:pattern specification process; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR041643; Znf_ZIC.
DR Pfam; PF00096; zf-C2H2; 3.
DR Pfam; PF18366; zf_ZIC; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Activator; Craniosynostosis; Cytoplasm; Developmental protein;
KW Differentiation; Disease variant; DNA-binding; Intellectual disability;
KW Metal-binding; Neurogenesis; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..447
FT /note="Zinc finger protein ZIC 1"
FT /id="PRO_0000047244"
FT ZN_FING 225..260
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 269..296
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 302..326
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 332..356
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 375..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 388..447
FT /note="Missing (in BAIDCS)"
FT /evidence="ECO:0000269|PubMed:26340333"
FT /id="VAR_083723"
FT VARIANT 389..447
FT /note="Missing (in BAIDCS)"
FT /evidence="ECO:0000269|PubMed:26340333"
FT /id="VAR_083724"
FT VARIANT 400
FT /note="G -> R (in CRS6; dbSNP:rs1057517670)"
FT /evidence="ECO:0000269|PubMed:26340333"
FT /id="VAR_075867"
FT VARIANT 402..447
FT /note="Missing (in BAIDCS)"
FT /evidence="ECO:0000269|PubMed:26340333"
FT /id="VAR_083725"
FT VARIANT 414
FT /note="T -> A (in dbSNP:rs143292136)"
FT /evidence="ECO:0000269|PubMed:26340333"
FT /id="VAR_075868"
FT CONFLICT 377
FT /note="L -> V (in Ref. 1; BAA11179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 48309 MW; 4DA3E32C99BF1AAE CRC64;
MLLDAGPQYP AIGVTTFGAS RHHSAGDVAE RDVGLGINPF ADGMGAFKLN PSSHELASAG
QTAFTSQAPG YAAAAALGHH HHPGHVGSYS SAAFNSTRDF LFRNRGFGDA AAAASAQHSL
FAASAGGFGG PHGHTDAAGH LLFPGLHEQA AGHASPNVVN GQMRLGFSGD MYPRPEQYGQ
VTSPRSEHYA APQLHGYGPM NVNMAAHHGA GAFFRYMRQP IKQELICKWI EPEQLANPKK
SCNKTFSTMH ELVTHVTVEH VGGPEQSNHI CFWEECPREG KPFKAKYKLV NHIRVHTGEK
PFPCPFPGCG KVFARSENLK IHKRTHTGEK PFKCEFEGCD RRFANSSDRK KHMHVHTSDK
PYLCKMCDKS YTHPSSLRKH MKVHESSSQG SQPSPAASSG YESSTPPTIV SPSTDNPTTS
SLSPSSSAVH HTAGHSALSS NFNEWYV
