ID   ZN217_HUMAN             Reviewed;        1048 AA.
AC   O75362; E1P5Y6; Q14DB8;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 202.
DE   RecName: Full=Zinc finger protein 217;
GN   Name=ZNF217; Synonyms=ZABC1;
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].
RX   PubMed=9671742; DOI=10.1073/pnas.95.15.8703;
RA   Collins C., Rommens J.M., Kowbel D., Godfrey T., Tanner M., Hwang S.-I.,
RA   Polikoff D., Nonet G., Cochran J., Myambo K., Jay K.E., Froula J.,
RA   Cloutier T., Kuo W.-L., Yaswen P., Dairkee S., Giovanola J.,
RA   Hutchinson G.B., Isola J., Kallioniemi O.-P., Palazzolo M., Martin C.,
RA   Ericsson C., Pinkel D., Albertson D., Li W.-B., Gray J.W.;
RT   "Positional cloning of ZNF217 and NABC1: genes amplified at 20q13.2 and
RT   overexpressed in breast carcinoma.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8703-8708(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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   [5]
RP   IDENTIFICATION IN THE BHC COMPLEX WITH GSE1; GTF2I; HDAC1; HDAC2; HMG20B;
RP   KDM1A; PHF21A; RCOR1; ZMYM2 AND ZMYM3.
RX   PubMed=12493763; DOI=10.1074/jbc.m208992200;
RA   Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT   "A candidate X-linked mental retardation gene is a component of a new
RT   family of histone deacetylase-containing complexes.";
RL   J. Biol. Chem. 278:7234-7239(2003).
RN   [6]
RP   FUNCTION.
RX   PubMed=16203743; DOI=10.1093/hmg/ddi352;
RA   Huang G., Krig S., Kowbel D., Xu H., Hyun B., Volik S., Feuerstein B.,
RA   Mills G.B., Stokoe D., Yaswen P., Collins C.;
RT   "ZNF217 suppresses cell death associated with chemotherapy and telomere
RT   dysfunction.";
RL   Hum. Mol. Genet. 14:3219-3225(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=17259635; DOI=10.1074/jbc.m611752200;
RA   Krig S.R., Jin V.X., Bieda M.C., O'Geen H., Yaswen P., Green R.,
RA   Farnham P.J.;
RT   "Identification of genes directly regulated by the oncogene ZNF217 using
RT   chromatin immunoprecipitation (ChIP)-chip assays.";
RL   J. Biol. Chem. 282:9703-9712(2007).
RN   [8]
RP   SUBUNIT, IDENTIFICATION IN A COMPLEX WITH HDAC2; KDM1A AND CTBP1, AND
RP   FUNCTION.
RX   PubMed=18625718; DOI=10.1128/mcb.00246-08;
RA   Thillainadesan G., Isovic M., Loney E., Andrews J., Tini M., Torchia J.;
RT   "Genome analysis identifies the p15ink4b tumor suppressor as a direct
RT   target of the ZNF217/CoREST complex.";
RL   Mol. Cell. Biol. 28:6066-6077(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; THR-322; THR-648 AND
RP   SER-662, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-795, AND
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-407; SER-593 AND
RP   SER-662, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [12]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-819, 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   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 752-760 IN COMPLEX WITH CTBP1,
RP   INTERACTION WITH CTBP1 AND CTBP2, AND FUNCTION.
RX   PubMed=16940172; DOI=10.1128/mcb.00680-06;
RA   Quinlan K.G.R., Nardini M., Verger A., Francescato P., Yaswen P., Corda D.,
RA   Bolognesi M., Crossley M.;
RT   "Specific recognition of ZNF217 and other zinc finger proteins at a surface
RT   groove of C-terminal binding proteins.";
RL   Mol. Cell. Biol. 26:8159-8172(2006).
RN   [14]
RP   VARIANT [LARGE SCALE ANALYSIS] ASN-323.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Binds to the promoters of target genes and functions as
CC       repressor. Promotes cell proliferation and antagonizes cell death.
CC       Promotes phosphorylation of AKT1 at 'Ser-473'.
CC       {ECO:0000269|PubMed:16203743, ECO:0000269|PubMed:16940172,
CC       ECO:0000269|PubMed:17259635, ECO:0000269|PubMed:18625718}.
CC   -!- SUBUNIT: Component of a histone deacetylase complex that contains
CC       HDAC2, KDM1A, CTBP1 and ZNF217. May be a component of a BHC histone
CC       deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A,
CC       RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC       Interacts with CTBP1 and CTBP2. {ECO:0000269|PubMed:12493763,
CC       ECO:0000269|PubMed:16940172, ECO:0000269|PubMed:18625718}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42875/ZNF217";
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DR   EMBL; AF041259; AAC39895.1; -; mRNA.
DR   EMBL; AL157838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW75580.1; -; Genomic_DNA.
DR   EMBL; BC113427; AAI13428.1; -; mRNA.
DR   CCDS; CCDS13443.1; -.
DR   RefSeq; NP_006517.1; NM_006526.2.
DR   RefSeq; XP_016883548.1; XM_017028059.1.
DR   PDB; 2HU2; X-ray; 2.85 A; B=752-760.
DR   PDB; 3UK3; X-ray; 2.10 A; C/D=469-523.
DR   PDB; 4F2J; X-ray; 2.64 A; C=469-523.
DR   PDB; 4IS1; X-ray; 2.10 A; C/D=469-523.
DR   PDBsum; 2HU2; -.
DR   PDBsum; 3UK3; -.
DR   PDBsum; 4F2J; -.
DR   PDBsum; 4IS1; -.
DR   AlphaFoldDB; O75362; -.
DR   SMR; O75362; -.
DR   BioGRID; 113547; 85.
DR   CORUM; O75362; -.
DR   IntAct; O75362; 28.
DR   MINT; O75362; -.
DR   STRING; 9606.ENSP00000360526; -.
DR   GlyGen; O75362; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; O75362; -.
DR   PhosphoSitePlus; O75362; -.
DR   SwissPalm; O75362; -.
DR   BioMuta; ZNF217; -.
DR   EPD; O75362; -.
DR   jPOST; O75362; -.
DR   MassIVE; O75362; -.
DR   MaxQB; O75362; -.
DR   PaxDb; 9606-ENSP00000360526; -.
DR   PeptideAtlas; O75362; -.
DR   ProteomicsDB; 49925; -.
DR   Pumba; O75362; -.
DR   Antibodypedia; 28736; 393 antibodies from 35 providers.
DR   DNASU; 7764; -.
DR   Ensembl; ENST00000302342.3; ENSP00000304308.3; ENSG00000171940.14.
DR   Ensembl; ENST00000371471.7; ENSP00000360526.2; ENSG00000171940.14.
DR   GeneID; 7764; -.
DR   KEGG; hsa:7764; -.
DR   MANE-Select; ENST00000371471.7; ENSP00000360526.2; NM_006526.3; NP_006517.1.
DR   UCSC; uc002xwq.5; human.
DR   AGR; HGNC:13009; -.
DR   CTD; 7764; -.
DR   DisGeNET; 7764; -.
DR   GeneCards; ZNF217; -.
DR   HGNC; HGNC:13009; ZNF217.
DR   HPA; ENSG00000171940; Low tissue specificity.
DR   MIM; 602967; gene.
DR   neXtProt; NX_O75362; -.
DR   OpenTargets; ENSG00000171940; -.
DR   PharmGKB; PA37588; -.
DR   VEuPathDB; HostDB:ENSG00000171940; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000159884; -.
DR   HOGENOM; CLU_010747_0_0_1; -.
DR   InParanoid; O75362; -.
DR   OMA; IHKNCRS; -.
DR   OrthoDB; 3849084at2759; -.
DR   PhylomeDB; O75362; -.
DR   TreeFam; TF332241; -.
DR   PathwayCommons; O75362; -.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   SignaLink; O75362; -.
DR   SIGNOR; O75362; -.
DR   BioGRID-ORCS; 7764; 279 hits in 1214 CRISPR screens.
DR   ChiTaRS; ZNF217; human.
DR   EvolutionaryTrace; O75362; -.
DR   GeneWiki; ZNF217; -.
DR   GenomeRNAi; 7764; -.
DR   Pharos; O75362; Tbio.
DR   PRO; PR:O75362; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; O75362; Protein.
DR   Bgee; ENSG00000171940; Expressed in endometrium epithelium and 177 other cell types or tissues.
DR   ExpressionAtlas; O75362; baseline and differential.
DR   GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR   IDEAL; IID00188; -.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45925; ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR45925:SF4; ZINC FINGER PROTEIN 217; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
DR   Genevisible; O75362; HS.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1048
FT                   /note="Zinc finger protein 217"
FT                   /id="PRO_0000047460"
FT   ZN_FING         65..88
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         128..150
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         156..178
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         216..238
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         375..397
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         471..493
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         499..521
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          242..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          772..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..457
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..845
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         321
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         322
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         593
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         648
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         662
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         795
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   CROSSLNK        819
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         323
FT                   /note="D -> N (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs767530299)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035572"
FT   VARIANT         739
FT                   /note="V -> I (in dbSNP:rs6063966)"
FT                   /id="VAR_052795"
FT   VARIANT         889
FT                   /note="D -> G (in dbSNP:rs34323943)"
FT                   /id="VAR_061939"
FT   TURN            474..476
FT                   /evidence="ECO:0007829|PDB:3UK3"
FT   HELIX           483..494
FT                   /evidence="ECO:0007829|PDB:3UK3"
FT   STRAND          502..505
FT                   /evidence="ECO:0007829|PDB:3UK3"
FT   STRAND          507..510
FT                   /evidence="ECO:0007829|PDB:3UK3"
FT   HELIX           511..521
FT                   /evidence="ECO:0007829|PDB:3UK3"
SQ   SEQUENCE   1048 AA;  115272 MW;  797FC620817D1E1F CRC64;
     MQSKVTGNMP TQSLLMYMDG PEVIGSSLGS PMEMEDALSM KGTAVVPFRA TQEKNVIQIE
     GYMPLDCMFC SQTFTHSEDL NKHVLMQHRP TLCEPAVLRV EAEYLSPLDK SQVRTEPPKE
     KNCKENEFSC EVCGQTFRVA FDVEIHMRTH KDSFTYGCNM CGRRFKEPWF LKNHMRTHNG
     KSGARSKLQQ GLESSPATIN EVVQVHAAES ISSPYKICMV CGFLFPNKES LIEHRKVHTK
     KTAFGTSSAQ TDSPQGGMPS SREDFLQLFN LRPKSHPETG KKPVRCIPQL DPFTTFQAWQ
     LATKGKVAIC QEVKESGQEG STDNDDSSSE KELGETNKGS CAGLSQEKEK CKHSHGEAPS
     VDADPKLPSS KEKPTHCSEC GKAFRTYHQL VLHSRVHKKD RRAGAESPTM SVDGRQPGTC
     SPDLAAPLDE NGAVDRGEGG SEDGSEDGLP EGIHLDKNDD GGKIKHLTSS RECSYCGKFF
     RSNYYLNIHL RTHTGEKPYK CEFCEYAAAQ KTSLRYHLER HHKEKQTDVA AEVKNDGKNQ
     DTEDALLTAD SAQTKNLKRF FDGAKDVTGS PPAKQLKEMP SVFQNVLGSA VLSPAHKDTQ
     DFHKNAADDS ADKVNKNPTP AYLDLLKKRS AVETQANNLI CRTKADVTPP PDGSTTHNLE
     VSPKEKQTET AADCRYRPSV DCHEKPLNLS VGALHNCPAI SLSKSLIPSI TCPFCTFKTF
     YPEVLMMHQR LEHKYNPDVH KNCRNKSLLR SRRTGCPPAL LGKDVPPLSS FCKPKPKSAF
     PAQSKSLPSA KGKQSPPGPG KAPLTSGIDS STLAPSNLKS HRPQQNVGVQ GAATRQQQSE
     MFPKTSVSPA PDKTKRPETK LKPLPVAPSQ PTLGSSNING SIDYPAKNDS PWAPPGRDYF
     CNRSASNTAA EFGEPLPKRL KSSVVALDVD QPGANYRRGY DLPKYHMVRG ITSLLPQDCV
     YPSQALPPKP RFLSSSEVDS PNVLTVQKPY GGSGPLYTCV PAGSPASSST LEGKRPVSYQ
     HLSNSMAQKR NYENFIGNAH YRPNDKKT
//