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 27-MAR-2024, entry version 198. 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; Q6NVV7: CDPF1; NbExp=3; IntAct=EBI-11963196, EBI-2802782; CC Q15915; Q9H5F2: CFAP68; NbExp=3; IntAct=EBI-11963196, EBI-718615; 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}. 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; 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; 109. 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; 9606-ENSP00000282928; -. DR PeptideAtlas; Q15915; -. DR ProteomicsDB; 60816; -. DR Pumba; Q15915; -. DR Antibodypedia; 1317; 459 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 AGR; HGNC:12872; -. 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; 2900023at2759; -. DR PhylomeDB; Q15915; -. DR TreeFam; TF351425; -. DR PathwayCommons; Q15915; -. DR SignaLink; Q15915; -. DR SIGNOR; Q15915; -. DR BioGRID-ORCS; 7545; 13 hits in 1173 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 144 other cell types or tissues. DR ExpressionAtlas; Q15915; baseline and differential. 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:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; 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 Gene3D; 3.30.160.60; Classic Zinc Finger; 4. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR InterPro; IPR041643; Znf_ZIC. DR PANTHER; PTHR19818:SF139; ZINC FINGER PROTEIN ZIC 1; 1. DR PANTHER; PTHR19818; ZINC FINGER PROTEIN ZIC AND GLI; 1. DR Pfam; PF00096; zf-C2H2; 3. DR Pfam; PF18366; zf_ZIC; 1. DR SMART; SM00355; ZnF_C2H2; 5. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4. DR Genevisible; Q15915; HS. 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 //