ID   ZIC2_HUMAN              Reviewed;         532 AA.
AC   O95409; Q5VYA9; Q9H309;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 2.
DT   24-JAN-2024, entry version 201.
DE   RecName: Full=Zinc finger protein ZIC 2;
DE   AltName: Full=Zinc finger protein of the cerebellum 2;
GN   Name=ZIC2;
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 CHARACTERIZATION OF VARIANT HPE5 POLY-ALA
RP   INS.
RX   PubMed=9771712; DOI=10.1038/2484;
RA   Brown S.A., Warburton D., Brown L.Y., Yu C.Y., Roeder E.R.,
RA   Stengel-Rutkowski S., Hennekam R.C.M., Muenke M.;
RT   "Holoprosencephaly due to mutations in ZIC2, a homologue of Drosophila odd-
RT   paired.";
RL   Nat. Genet. 20:180-183(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=10984499; DOI=10.1074/jbc.m007906200;
RA   Yang Y., Hwang C.K., Junn E., Lee G., Mouradian M.M.;
RT   "ZIC2 and Sp3 repress Sp1-induced activation of the human D1A dopamine
RT   receptor gene.";
RL   J. Biol. Chem. 275:38863-38869(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [4]
RP   INTERACTION WITH DHX9.
RX   PubMed=17251188; DOI=10.1074/jbc.m610821200;
RA   Ishiguro A., Ideta M., Mikoshiba K., Chen D.J., Aruga J.;
RT   "ZIC2-dependent transcriptional regulation is mediated by DNA-dependent
RT   protein kinase, poly(ADP-ribose) polymerase, and RNA helicase A.";
RL   J. Biol. Chem. 282:9983-9995(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [6]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-253, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [7]
RP   VARIANTS HPE5 PHE-152 AND ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-470 INS,
RP   AND POLYMORPHISM OF POLY-HIS REGION.
RX   PubMed=11285244; DOI=10.1093/hmg/10.8.791;
RA   Brown L.Y., Odent S., David V., Blayau M., Dubourg C., Apacik C.,
RA   Delgado M.A., Hall B.D., Reynolds J.F., Sommer A., Wieczorek D.,
RA   Brown S.A., Muenke M.;
RT   "Holoprosencephaly due to mutations in ZIC2: alanine tract expansion
RT   mutations may be caused by parental somatic recombination.";
RL   Hum. Mol. Genet. 10:791-796(2001).
RN   [8]
RP   VARIANTS HPE5 PRO-36 AND PHE-152, AND VARIANTS HIS-239 INS AND HIS-239 DEL.
RX   PubMed=15221788; DOI=10.1002/humu.20056;
RA   Dubourg C., Lazaro L., Pasquier L., Bendavid C., Blayau M., Le Duff F.,
RA   Durou M.-R., Odent S., David V.;
RT   "Molecular screening of SHH, ZIC2, SIX3, and TGIF genes in patients with
RT   features of holoprosencephaly spectrum: mutation review and genotype-
RT   phenotype correlations.";
RL   Hum. Mutat. 24:43-51(2004).
RN   [9]
RP   CHARACTERIZATION OF VARIANTS HPE5 PRO-36; PHE-152 AND POLY-ALA INS.
RX   PubMed=15590697; DOI=10.1093/hmg/ddi037;
RA   Brown L., Paraso M., Arkell R., Brown S.;
RT   "In vitro analysis of partial loss-of-function ZIC2 mutations in
RT   holoprosencephaly: alanine tract expansion modulates DNA binding and
RT   transactivation.";
RL   Hum. Mol. Genet. 14:411-420(2005).
RN   [10]
RP   VARIANTS HPE5 ASN-37; ASN-128; ASN-272; LEU-286; GLN-286; TYR-286; TYR-291;
RP   ARG-304; CYS-314; SER-325; LEU-325; TYR-327; PHE-335; PRO-373; ASN-402;
RP   LYS-403; ARG-404; TRP-409 AND GLN-415.
RX   PubMed=19177455; DOI=10.1002/humu.20982;
RA   Roessler E., Lacbawan F., Dubourg C., Paulussen A., Herbergs J., Hehr U.,
RA   Bendavid C., Zhou N., Ouspenskaia M., Bale S., Odent S., David V.,
RA   Muenke M.;
RT   "The full spectrum of holoprosencephaly-associated mutations within the
RT   ZIC2 gene in humans predicts loss-of-function as the predominant disease
RT   mechanism.";
RL   Hum. Mutat. 30:E541-E554(2009).
CC   -!- FUNCTION: Acts as a transcriptional activator or repressor. Plays
CC       important roles in the early stage of organogenesis of the CNS.
CC       Activates the transcription of the serotonin transporter SERT in
CC       uncrossed ipsilateral retinal ganglion cells (iRGCs) to refine eye-
CC       specific projections in primary visual targets. Its transcriptional
CC       activity is repressed by MDFIC. Involved in the formation of the
CC       ipsilateral retinal projection at the optic chiasm midline. Drives the
CC       expression of EPHB1 on ipsilaterally projecting growth cones. Binds to
CC       the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'. Associates to the
CC       basal SERT promoter region from ventrotemporal retinal segments of
CC       retinal embryos.
CC   -!- SUBUNIT: Interacts with RNF180. Interacts (via the C2H2-type domains 3,
CC       4 and 5) with MDFIC (via the C2H2-type domains 3, 4 and 5); the
CC       interaction reduces its transcriptional activity. Interacts with GLI1
CC       and GLI2 (By similarity). Interacts (via C2H2-type domain 3) with DHX9
CC       (PubMed:17251188). {ECO:0000250|UniProtKB:Q62520,
CC       ECO:0000269|PubMed:17251188}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Localizes
CC       in the cytoplasm in presence of MDFIC overexpression. Both
CC       phosphorylated and unphosphorylated forms are localized in the nucleus
CC       (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The C2H2-type 3, 4 and 5 zinc finger domains are necessary for
CC       transcription activation. {ECO:0000250}.
CC   -!- PTM: Phosphorylated.
CC   -!- PTM: Ubiquitinated by RNF180, leading to its degradation.
CC   -!- POLYMORPHISM: The poly-His region between amino acids 231-239 of ZIC2
CC       is polymorphic and the number of His can vary from 8 to 12.
CC       {ECO:0000269|PubMed:11285244}.
CC   -!- DISEASE: Holoprosencephaly 5 (HPE5) [MIM:609637]: A structural anomaly
CC       of the brain, in which the developing forebrain fails to correctly
CC       separate into right and left hemispheres. Holoprosencephaly is
CC       genetically heterogeneous and associated with several distinct facies
CC       and phenotypic variability. {ECO:0000269|PubMed:11285244,
CC       ECO:0000269|PubMed:15221788, ECO:0000269|PubMed:15590697,
CC       ECO:0000269|PubMed:19177455, ECO:0000269|PubMed:9771712}. 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; AF104902; AAC96325.1; -; mRNA.
DR   EMBL; AF193855; AAG28409.1; -; mRNA.
DR   EMBL; AL355338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS9495.1; -.
DR   RefSeq; NP_009060.2; NM_007129.3.
DR   AlphaFoldDB; O95409; -.
DR   SMR; O95409; -.
DR   BioGRID; 113378; 43.
DR   IntAct; O95409; 5.
DR   MINT; O95409; -.
DR   STRING; 9606.ENSP00000365514; -.
DR   iPTMnet; O95409; -.
DR   PhosphoSitePlus; O95409; -.
DR   BioMuta; ZIC2; -.
DR   EPD; O95409; -.
DR   jPOST; O95409; -.
DR   MassIVE; O95409; -.
DR   MaxQB; O95409; -.
DR   PaxDb; 9606-ENSP00000365514; -.
DR   PeptideAtlas; O95409; -.
DR   ProteomicsDB; 50861; -.
DR   Pumba; O95409; -.
DR   Antibodypedia; 10980; 221 antibodies from 31 providers.
DR   DNASU; 7546; -.
DR   Ensembl; ENST00000376335.8; ENSP00000365514.3; ENSG00000043355.12.
DR   GeneID; 7546; -.
DR   KEGG; hsa:7546; -.
DR   MANE-Select; ENST00000376335.8; ENSP00000365514.3; NM_007129.5; NP_009060.2.
DR   UCSC; uc001von.4; human.
DR   AGR; HGNC:12873; -.
DR   CTD; 7546; -.
DR   DisGeNET; 7546; -.
DR   GeneCards; ZIC2; -.
DR   GeneReviews; ZIC2; -.
DR   HGNC; HGNC:12873; ZIC2.
DR   HPA; ENSG00000043355; Tissue enriched (brain).
DR   MalaCards; ZIC2; -.
DR   MIM; 603073; gene.
DR   MIM; 609637; phenotype.
DR   neXtProt; NX_O95409; -.
DR   OpenTargets; ENSG00000043355; -.
DR   Orphanet; 93925; Alobar holoprosencephaly.
DR   Orphanet; 93924; Lobar holoprosencephaly.
DR   Orphanet; 280200; Microform holoprosencephaly.
DR   Orphanet; 93926; Midline interhemispheric variant of holoprosencephaly.
DR   Orphanet; 220386; Semilobar holoprosencephaly.
DR   Orphanet; 280195; Septopreoptic holoprosencephaly.
DR   PharmGKB; PA37462; -.
DR   VEuPathDB; HostDB:ENSG00000043355; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000160645; -.
DR   HOGENOM; CLU_002678_37_1_1; -.
DR   InParanoid; O95409; -.
DR   OMA; HGPHSSQ; -.
DR   OrthoDB; 2900023at2759; -.
DR   PhylomeDB; O95409; -.
DR   TreeFam; TF351425; -.
DR   PathwayCommons; O95409; -.
DR   Reactome; R-HSA-9823739; Formation of the anterior neural plate.
DR   SignaLink; O95409; -.
DR   SIGNOR; O95409; -.
DR   BioGRID-ORCS; 7546; 30 hits in 1186 CRISPR screens.
DR   ChiTaRS; ZIC2; human.
DR   GeneWiki; ZIC2; -.
DR   GenomeRNAi; 7546; -.
DR   Pharos; O95409; Tbio.
DR   PRO; PR:O95409; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; O95409; Protein.
DR   Bgee; ENSG00000043355; Expressed in cerebellar cortex and 116 other cell types or tissues.
DR   ExpressionAtlas; O95409; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
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:0007420; P:brain development; TAS:ProtInc.
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:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; ISS:UniProtKB.
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:SF27; ZINC FINGER PROTEIN ZIC 2; 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; O95409; HS.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; Developmental protein; Differentiation;
KW   Disease variant; DNA-binding; Holoprosencephaly; Isopeptide bond;
KW   Metal-binding; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..532
FT                   /note="Zinc finger protein ZIC 2"
FT                   /id="PRO_0000047247"
FT   ZN_FING         256..291
FT                   /note="C2H2-type 1; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         300..327
FT                   /note="C2H2-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         333..357
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         363..387
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         393..415
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          100..255
FT                   /note="Necessary for interaction with MDFIC and
FT                   transcriptional activation or repression"
FT                   /evidence="ECO:0000250"
FT   REGION          406..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62520"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62520"
FT   CROSSLNK        253
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         36
FT                   /note="Q -> P (in HPE5; 2-fold increase in luciferase
FT                   activity; dbSNP:rs1185333947)"
FT                   /evidence="ECO:0000269|PubMed:15221788,
FT                   ECO:0000269|PubMed:15590697"
FT                   /id="VAR_023793"
FT   VARIANT         37
FT                   /note="D -> N (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058592"
FT   VARIANT         128
FT                   /note="D -> N (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058593"
FT   VARIANT         152
FT                   /note="D -> F (in HPE5; 50% reduction of luciferase
FT                   activity; requires 2 nucleotide substitutions)"
FT                   /evidence="ECO:0000269|PubMed:11285244,
FT                   ECO:0000269|PubMed:15221788, ECO:0000269|PubMed:15590697"
FT                   /id="VAR_023794"
FT   VARIANT         239
FT                   /note="H -> HH"
FT                   /evidence="ECO:0000269|PubMed:15221788"
FT                   /id="VAR_023795"
FT   VARIANT         239
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:15221788"
FT                   /id="VAR_023796"
FT   VARIANT         272
FT                   /note="S -> N (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058594"
FT   VARIANT         286
FT                   /note="H -> L (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058595"
FT   VARIANT         286
FT                   /note="H -> Q (in HPE5; dbSNP:rs1325393230)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058596"
FT   VARIANT         286
FT                   /note="H -> Y (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058597"
FT   VARIANT         291
FT                   /note="H -> Y (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058598"
FT   VARIANT         304
FT                   /note="W -> R (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058599"
FT   VARIANT         314
FT                   /note="F -> C (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058600"
FT   VARIANT         325
FT                   /note="R -> L (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058601"
FT   VARIANT         325
FT                   /note="R -> S (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058602"
FT   VARIANT         327
FT                   /note="H -> Y (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058603"
FT   VARIANT         335
FT                   /note="C -> F (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058604"
FT   VARIANT         373
FT                   /note="R -> P (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058605"
FT   VARIANT         402
FT                   /note="Y -> N (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058606"
FT   VARIANT         403
FT                   /note="T -> K (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058607"
FT   VARIANT         404
FT                   /note="H -> R (in HPE5)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058608"
FT   VARIANT         409
FT                   /note="R -> W (in HPE5; dbSNP:rs1594291868)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058609"
FT   VARIANT         415
FT                   /note="H -> Q (in HPE5; dbSNP:rs794729641)"
FT                   /evidence="ECO:0000269|PubMed:19177455"
FT                   /id="VAR_058610"
FT   VARIANT         470
FT                   /note="A -> AAAAAAAAAAA (in HPE5; near-complete loss of
FT                   luciferase activity)"
FT                   /id="VAR_008856"
FT   CONFLICT        124..128
FT                   /note="RGFGD -> ARLPGT (in Ref. 1; AAC96325)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   532 AA;  55006 MW;  BA3E6455DAF97EAC CRC64;
     MLLDAGPQFP AIGVGSFARH HHHSAAAAAA AAAEMQDREL SLAAAQNGFV DSAAAHMGAF
     KLNPGAHELS PGQSSAFTSQ GPGAYPGSAA AAAAAAALGP HAAHVGSYSG PPFNSTRDFL
     FRSRGFGDSA PGGGQHGLFG PGAGGLHHAH SDAQGHLLFP GLPEQHGPHG SQNVLNGQMR
     LGLPGEVFGR SEQYRQVASP RTDPYSAAQL HNQYGPMNMN MGMNMAAAAA HHHHHHHHHP
     GAFFRYMRQQ CIKQELICKW IDPEQLSNPK KSCNKTFSTM HELVTHVSVE HVGGPEQSNH
     VCFWEECPRE GKPFKAKYKL VNHIRVHTGE KPFPCPFPGC GKVFARSENL KIHKRTHTGE
     KPFQCEFEGC DRRFANSSDR KKHMHVHTSD KPYLCKMCDK SYTHPSSLRK HMKVHESSPQ
     GSESSPAASS GYESSTPPGL VSPSAEPQSS SNLSPAAAAA AAAAAAAAAA VSAVHRGGGS
     GSGGAGGGSG GGSGSGGGGG GAGGGGGGSS GGGSGTAGGH SGLSSNFNEW YV
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