ID ZFAT_HUMAN Reviewed; 1243 AA. AC Q9P243; B7ZL15; E9PER3; Q3MIM5; Q6PJ01; Q75PJ6; Q75PJ7; Q75PJ9; Q86X64; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 2. DT 27-MAR-2024, entry version 190. DE RecName: Full=Zinc finger protein ZFAT; DE AltName: Full=Zinc finger gene in AITD susceptibility region; DE AltName: Full=Zinc finger protein 406; GN Name=ZFAT; Synonyms=KIAA1485, ZFAT1, ZNF406; 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] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, AND RP VARIANTS ARG-64 AND SER-102. RX PubMed=15294872; DOI=10.1093/hmg/ddh245; RA Shirasawa S., Harada H., Furugaki K., Akamizu T., Ishikawa N., Ito K., RA Ito K., Tamai H., Kuma K., Kubota S., Hiratani H., Tsuchiya T., Baba I., RA Ishikawa M., Tanaka M., Sakai K., Aoki M., Yamamoto K., Sasazuki T.; RT "SNPs in the promoter of a B cell-specific antisense transcript, SAS-ZFAT, RT determine susceptibility to autoimmune thyroid disease."; RL Hum. Mol. Genet. 13:2221-2231(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANTS RP ARG-64 AND SER-102. RC TISSUE=Brain, Placenta, and Skin; 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 [LARGE SCALE MRNA] OF 140-1243 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10819331; DOI=10.1093/dnares/7.2.143; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:143-150(2000). RN [5] {ECO:0007744|PDB:2ELM, ECO:0007744|PDB:2ELN, ECO:0007744|PDB:2ELO, ECO:0007744|PDB:2ELP, ECO:0007744|PDB:2ELQ, ECO:0007744|PDB:2ELR, ECO:0007744|PDB:2ELS, ECO:0007744|PDB:2ELT, ECO:0007744|PDB:2ELU, ECO:0007744|PDB:2ELV, ECO:0007744|PDB:2RSH} RP STRUCTURE BY NMR OF 269-381; 402-430; 768-857 AND 878-963 IN COMPLEX WITH RP ZN(2+), AND ZINC FINGERS. RX PubMed=25801860; DOI=10.1007/s10969-015-9196-3; RA Tochio N., Umehara T., Nakabayashi K., Yoneyama M., Tsuda K., Shirouzu M., RA Koshiba S., Watanabe S., Kigawa T., Sasazuki T., Shirasawa S., Yokoyama S.; RT "Solution structures of the DNA-binding domains of immune-related zinc- RT finger protein ZFAT."; RL J. Struct. Funct. Genomics 16:55-65(2015). RN [6] RP VARIANT GLN-400. RX PubMed=28940097; DOI=10.1007/s00439-017-1843-2; RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A., RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M., RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A., RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S., RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T., RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C., RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M., RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.; RT "Expanding the genetic heterogeneity of intellectual disability."; RL Hum. Genet. 136:1419-1429(2017). RN [7] RP ERRATUM OF PUBMED:28940097. RX PubMed=29288388; DOI=10.1007/s00439-017-1859-7; RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A., RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M., RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A., RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S., RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T., RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C., RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M., RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.; RT "Correction to: Expanding the genetic heterogeneity of intellectual RT disability."; RL Hum. Genet. 137:105-109(2018). CC -!- FUNCTION: May be involved in transcriptional regulation. Overexpression CC causes down-regulation of a number of genes involved in the immune CC response. Some genes are also up-regulated (By similarity). CC {ECO:0000250}. CC -!- INTERACTION: CC Q9P243; Q9UER7: DAXX; NbExp=5; IntAct=EBI-3943507, EBI-77321; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=ZFAT-1; CC IsoId=Q9P243-1; Sequence=Displayed; CC Name=2; Synonyms=ZFAT-2, ZFAT-3; CC IsoId=Q9P243-2; Sequence=VSP_016959; CC Name=3; Synonyms=TR-ZFAT; CC IsoId=Q9P243-3; Sequence=VSP_016959, VSP_034938, VSP_034939; CC Name=4; CC IsoId=Q9P243-4; Sequence=VSP_045461; CC -!- TISSUE SPECIFICITY: Isoform 1 is strongly expressed in placenta, CC spleen, kidney, testis and peripheral blood leukocytes. Expressed in CC CD4+ and CD8+ T-cells, CD19+ B-cells and CB14+ monocytes. Isoform 3 is CC strongly expressed in placenta, ovary, tonsil, CD19+ B-cells and CD14+ CC monocytes. {ECO:0000269|PubMed:15294872}. 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; AB167738; BAD12567.1; -; mRNA. DR EMBL; AB167739; BAD12568.1; -; mRNA. DR EMBL; AB167740; BAD12569.1; -; mRNA. DR EMBL; AB167741; BAD12570.1; -; mRNA. DR EMBL; AC015599; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC087045; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC135075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC025423; AAH25423.1; -; mRNA. DR EMBL; BC046180; AAH46180.1; -; mRNA. DR EMBL; BC101766; AAI01767.1; -; mRNA. DR EMBL; BC101768; AAI01769.1; -; mRNA. DR EMBL; BC143519; AAI43520.1; -; mRNA. DR EMBL; AB040918; BAA96009.1; -; mRNA. DR CCDS; CCDS43768.2; -. [Q9P243-2] DR CCDS; CCDS47924.1; -. [Q9P243-1] DR CCDS; CCDS55276.1; -. [Q9P243-4] DR RefSeq; NP_001025110.2; NM_001029939.3. [Q9P243-2] DR RefSeq; NP_001167628.1; NM_001174157.1. [Q9P243-4] DR RefSeq; NP_001276323.1; NM_001289394.1. [Q9P243-2] DR RefSeq; NP_065914.2; NM_020863.3. [Q9P243-1] DR RefSeq; XP_011515505.1; XM_011517203.1. DR PDB; 2ELM; NMR; -; A=768-797. DR PDB; 2ELN; NMR; -; A=796-826. DR PDB; 2ELO; NMR; -; A=828-857. DR PDB; 2ELP; NMR; -; A=878-907. DR PDB; 2ELQ; NMR; -; A=907-935. DR PDB; 2ELR; NMR; -; A=935-963. DR PDB; 2ELS; NMR; -; A=269-297. DR PDB; 2ELT; NMR; -; A=297-325. DR PDB; 2ELU; NMR; -; A=352-381. DR PDB; 2ELV; NMR; -; A=402-430. DR PDB; 2RSH; NMR; -; A=324-353. DR PDB; 2RSI; NMR; -; A=297-381. DR PDB; 2RSJ; NMR; -; A=269-353. DR PDB; 2RUT; NMR; -; A=269-297. DR PDB; 2RUU; NMR; -; A=297-325. DR PDB; 2RUV; NMR; -; A=323-353. DR PDB; 2RUW; NMR; -; A=352-381. DR PDB; 2RUX; NMR; -; A=402-430. DR PDB; 2RUY; NMR; -; A=768-797. DR PDB; 2RUZ; NMR; -; A=796-826. DR PDB; 2RV0; NMR; -; A=828-857. DR PDB; 2RV1; NMR; -; A=878-907. DR PDB; 2RV2; NMR; -; A=907-935. DR PDB; 2RV3; NMR; -; A=935-963. DR PDB; 2RV6; NMR; -; A=269-353. DR PDB; 2RV7; NMR; -; A=297-381. DR PDBsum; 2ELM; -. DR PDBsum; 2ELN; -. DR PDBsum; 2ELO; -. DR PDBsum; 2ELP; -. DR PDBsum; 2ELQ; -. DR PDBsum; 2ELR; -. DR PDBsum; 2ELS; -. DR PDBsum; 2ELT; -. DR PDBsum; 2ELU; -. DR PDBsum; 2ELV; -. DR PDBsum; 2RSH; -. DR PDBsum; 2RSI; -. DR PDBsum; 2RSJ; -. DR PDBsum; 2RUT; -. DR PDBsum; 2RUU; -. DR PDBsum; 2RUV; -. DR PDBsum; 2RUW; -. DR PDBsum; 2RUX; -. DR PDBsum; 2RUY; -. DR PDBsum; 2RUZ; -. DR PDBsum; 2RV0; -. DR PDBsum; 2RV1; -. DR PDBsum; 2RV2; -. DR PDBsum; 2RV3; -. DR PDBsum; 2RV6; -. DR PDBsum; 2RV7; -. DR AlphaFoldDB; Q9P243; -. DR BMRB; Q9P243; -. DR SMR; Q9P243; -. DR BioGRID; 121669; 11. DR IntAct; Q9P243; 5. DR STRING; 9606.ENSP00000367069; -. DR GlyGen; Q9P243; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9P243; -. DR PhosphoSitePlus; Q9P243; -. DR BioMuta; ZFAT; -. DR DMDM; 85681862; -. DR EPD; Q9P243; -. DR jPOST; Q9P243; -. DR MassIVE; Q9P243; -. DR MaxQB; Q9P243; -. DR PaxDb; 9606-ENSP00000367069; -. DR PeptideAtlas; Q9P243; -. DR ProteomicsDB; 19945; -. DR ProteomicsDB; 83726; -. [Q9P243-1] DR ProteomicsDB; 83727; -. [Q9P243-2] DR ProteomicsDB; 83728; -. [Q9P243-3] DR Antibodypedia; 27498; 52 antibodies from 16 providers. DR DNASU; 57623; -. DR Ensembl; ENST00000377838.8; ENSP00000367069.3; ENSG00000066827.16. [Q9P243-1] DR Ensembl; ENST00000520214.5; ENSP00000428483.1; ENSG00000066827.16. [Q9P243-2] DR Ensembl; ENST00000520727.5; ENSP00000427831.1; ENSG00000066827.16. [Q9P243-2] DR Ensembl; ENST00000523399.5; ENSP00000429091.1; ENSG00000066827.16. [Q9P243-4] DR GeneID; 57623; -. DR KEGG; hsa:57623; -. DR MANE-Select; ENST00000377838.8; ENSP00000367069.3; NM_020863.4; NP_065914.2. DR UCSC; uc003yun.4; human. [Q9P243-1] DR AGR; HGNC:19899; -. DR CTD; 57623; -. DR DisGeNET; 57623; -. DR GeneCards; ZFAT; -. DR HGNC; HGNC:19899; ZFAT. DR HPA; ENSG00000066827; Tissue enhanced (placenta). DR MalaCards; ZFAT; -. DR MIM; 610931; gene. DR neXtProt; NX_Q9P243; -. DR OpenTargets; ENSG00000066827; -. DR PharmGKB; PA162409638; -. DR VEuPathDB; HostDB:ENSG00000066827; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000156658; -. DR HOGENOM; CLU_008355_0_0_1; -. DR InParanoid; Q9P243; -. DR OMA; ACELCDH; -. DR OrthoDB; 3085502at2759; -. DR PhylomeDB; Q9P243; -. DR TreeFam; TF350017; -. DR PathwayCommons; Q9P243; -. DR SignaLink; Q9P243; -. DR BioGRID-ORCS; 57623; 50 hits in 1183 CRISPR screens. DR ChiTaRS; ZFAT; human. DR EvolutionaryTrace; Q9P243; -. DR GenomeRNAi; 57623; -. DR Pharos; Q9P243; Tbio. DR PRO; PR:Q9P243; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q9P243; Protein. DR Bgee; ENSG00000066827; Expressed in placenta and 112 other cell types or tissues. DR ExpressionAtlas; Q9P243; baseline and differential. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl. 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:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0060712; P:spongiotrophoblast layer development; IEA:Ensembl. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 11. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24388:SF53; COMBGAP, ISOFORM L-RELATED; 1. DR PANTHER; PTHR24388; ZINC FINGER PROTEIN; 1. DR Pfam; PF00096; zf-C2H2; 4. DR Pfam; PF13909; zf-H2C2_5; 1. DR SMART; SM00355; ZnF_C2H2; 19. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 8. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13. DR Genevisible; Q9P243; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding; Metal-binding; KW Nucleus; Reference proteome; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..1243 FT /note="Zinc finger protein ZFAT" FT /id="PRO_0000047566" FT ZN_FING 12..35 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 116..141 FT /note="C2H2-type 2; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 271..293 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000269|PubMed:25801860, ECO:0007744|PDB:2ELS, FT ECO:0007744|PDB:2RUT" FT ZN_FING 299..321 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000269|PubMed:25801860, ECO:0007744|PDB:2ELT, FT ECO:0007744|PDB:2RUU" FT ZN_FING 326..349 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000269|PubMed:25801860, ECO:0007744|PDB:2RSH, FT ECO:0007744|PDB:2RUV" FT ZN_FING 354..377 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000269|PubMed:25801860, ECO:0007744|PDB:2ELU, FT ECO:0007744|PDB:2RUW" FT ZN_FING 404..426 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000269|PubMed:25801860, ECO:0007744|PDB:2ELV, FT ECO:0007744|PDB:2RUX" FT ZN_FING 432..454 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 458..481 FT /note="C2H2-type 9" FT /evidence="ECO:0000250|UniProtKB:Q7TS63" FT ZN_FING 742..764 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 770..793 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000269|PubMed:25801860, ECO:0007744|PDB:2ELM, FT ECO:0007744|PDB:2RUY" FT ZN_FING 798..822 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000269|PubMed:25801860, ECO:0007744|PDB:2ELN, FT ECO:0007744|PDB:2RUZ" FT ZN_FING 830..853 FT /note="C2H2-type 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000269|PubMed:25801860, ECO:0007744|PDB:2ELO, FT ECO:0007744|PDB:2RV0" FT ZN_FING 880..903 FT /note="C2H2-type 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000269|PubMed:25801860, ECO:0007744|PDB:2ELP, FT ECO:0007744|PDB:2RV1" FT ZN_FING 909..931 FT /note="C2H2-type 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000269|PubMed:25801860, ECO:0007744|PDB:2ELQ, FT ECO:0007744|PDB:2RV2" FT ZN_FING 937..959 FT /note="C2H2-type 16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000269|PubMed:25801860, ECO:0007744|PDB:2ELR, FT ECO:0007744|PDB:2RV3" FT ZN_FING 966..988 FT /note="C2H2-type 17" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 994..1017 FT /note="C2H2-type 18" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1041..1064 FT /note="C2H2-type 19" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 51..116 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 147..189 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 534..570 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 603..625 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 638..705 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 153..186 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 537..551 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 638..658 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 273 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELS, ECO:0007744|PDB:2RUT" FT BINDING 276 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELS, ECO:0007744|PDB:2RUT" FT BINDING 289 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELS, ECO:0007744|PDB:2RUT" FT BINDING 293 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELS, ECO:0007744|PDB:2RUT" FT BINDING 301 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELT, ECO:0007744|PDB:2RUU" FT BINDING 304 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELT, ECO:0007744|PDB:2RUU" FT BINDING 317 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELT, ECO:0007744|PDB:2RUU" FT BINDING 321 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELT, ECO:0007744|PDB:2RUU" FT BINDING 328 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2RSH, ECO:0007744|PDB:2RUV" FT BINDING 331 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2RSH, ECO:0007744|PDB:2RUV" FT BINDING 344 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2RSH, ECO:0007744|PDB:2RUV" FT BINDING 349 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2RSH, ECO:0007744|PDB:2RUV" FT BINDING 356 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELU, ECO:0007744|PDB:2RUW" FT BINDING 359 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELU, ECO:0007744|PDB:2RUW" FT BINDING 372 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELU, ECO:0007744|PDB:2RUW" FT BINDING 377 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELU, ECO:0007744|PDB:2RUW" FT BINDING 406 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELV, ECO:0007744|PDB:2RUX" FT BINDING 409 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELV, ECO:0007744|PDB:2RUX" FT BINDING 422 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELV, ECO:0007744|PDB:2RUX" FT BINDING 426 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELV, ECO:0007744|PDB:2RUX" FT BINDING 460 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:Q7TS63" FT BINDING 463 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:Q7TS63" FT BINDING 476 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:Q7TS63" FT BINDING 481 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:Q7TS63" FT BINDING 772 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="7" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELM, ECO:0007744|PDB:2RUY" FT BINDING 775 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="7" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELM, ECO:0007744|PDB:2RUY" FT BINDING 788 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="7" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELM, ECO:0007744|PDB:2RUY" FT BINDING 793 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="7" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELM, ECO:0007744|PDB:2RUY" FT BINDING 800 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="8" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELN, ECO:0007744|PDB:2RUZ" FT BINDING 805 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="8" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELN, ECO:0007744|PDB:2RUZ" FT BINDING 818 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="8" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELN, ECO:0007744|PDB:2RUZ" FT BINDING 822 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="8" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELN, ECO:0007744|PDB:2RUZ" FT BINDING 832 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="9" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELO, ECO:0007744|PDB:2RV0" FT BINDING 835 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="9" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELO, ECO:0007744|PDB:2RV0" FT BINDING 848 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="9" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELO, ECO:0007744|PDB:2RV0" FT BINDING 853 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="9" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELO, ECO:0007744|PDB:2RV0" FT BINDING 882 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="10" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELP, ECO:0007744|PDB:2RV1" FT BINDING 885 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="10" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELP, ECO:0007744|PDB:2RV1" FT BINDING 899 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="10" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELP, ECO:0007744|PDB:2RV1" FT BINDING 903 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="10" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELP, ECO:0007744|PDB:2RV1" FT BINDING 911 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="11" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELQ, ECO:0007744|PDB:2RV2" FT BINDING 914 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="11" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELQ, ECO:0007744|PDB:2RV2" FT BINDING 927 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="11" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELQ, ECO:0007744|PDB:2RV2" FT BINDING 931 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="11" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELQ, ECO:0007744|PDB:2RV2" FT BINDING 939 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="12" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELR, ECO:0007744|PDB:2RV3" FT BINDING 942 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="12" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELR, ECO:0007744|PDB:2RV3" FT BINDING 955 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="12" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELR, ECO:0007744|PDB:2RV3" FT BINDING 958 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="12" FT /evidence="ECO:0000269|PubMed:25801860, FT ECO:0007744|PDB:2ELR, ECO:0007744|PDB:2RV3" FT VAR_SEQ 1..12 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15294872" FT /id="VSP_016959" FT VAR_SEQ 150..211 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045461" FT VAR_SEQ 826..858 FT /note="DKRSYSCPVCEKSFSEDRLIKSHIKTNHPEVSM -> VSSKPKRQPRLPWVL FT IAFSSLCLYVGVSAAGQP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15294872" FT /id="VSP_034938" FT VAR_SEQ 859..1243 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15294872" FT /id="VSP_034939" FT VARIANT 64 FT /note="G -> R (in dbSNP:rs17778003)" FT /evidence="ECO:0000269|PubMed:15294872, FT ECO:0000269|PubMed:15489334" FT /id="VAR_024840" FT VARIANT 102 FT /note="P -> S (in dbSNP:rs12541381)" FT /evidence="ECO:0000269|PubMed:15294872" FT /id="VAR_045815" FT VARIANT 400 FT /note="R -> Q (found in a patient with global developmental FT delay; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28940097" FT /id="VAR_084658" FT VARIANT 672 FT /note="R -> K (in dbSNP:rs35003767)" FT /id="VAR_052819" FT TURN 274..276 FT /evidence="ECO:0007829|PDB:2ELS" FT STRAND 279..282 FT /evidence="ECO:0007829|PDB:2ELS" FT HELIX 283..293 FT /evidence="ECO:0007829|PDB:2ELS" FT STRAND 298..300 FT /evidence="ECO:0007829|PDB:2ELT" FT STRAND 302..305 FT /evidence="ECO:0007829|PDB:2ELT" FT STRAND 307..310 FT /evidence="ECO:0007829|PDB:2ELT" FT HELIX 311..321 FT /evidence="ECO:0007829|PDB:2ELT" FT STRAND 329..331 FT /evidence="ECO:0007829|PDB:2RSH" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:2RSI" FT HELIX 338..347 FT /evidence="ECO:0007829|PDB:2RSH" FT TURN 357..359 FT /evidence="ECO:0007829|PDB:2ELU" FT STRAND 362..365 FT /evidence="ECO:0007829|PDB:2RSI" FT HELIX 366..375 FT /evidence="ECO:0007829|PDB:2ELU" FT STRAND 407..409 FT /evidence="ECO:0007829|PDB:2ELV" FT STRAND 412..415 FT /evidence="ECO:0007829|PDB:2ELV" FT HELIX 416..423 FT /evidence="ECO:0007829|PDB:2ELV" FT TURN 424..426 FT /evidence="ECO:0007829|PDB:2ELV" FT STRAND 769..771 FT /evidence="ECO:0007829|PDB:2ELM" FT STRAND 773..776 FT /evidence="ECO:0007829|PDB:2ELM" FT STRAND 778..780 FT /evidence="ECO:0007829|PDB:2ELM" FT HELIX 782..792 FT /evidence="ECO:0007829|PDB:2ELM" FT STRAND 801..804 FT /evidence="ECO:0007829|PDB:2ELN" FT STRAND 808..810 FT /evidence="ECO:0007829|PDB:2ELN" FT HELIX 812..822 FT /evidence="ECO:0007829|PDB:2ELN" FT TURN 833..836 FT /evidence="ECO:0007829|PDB:2ELO" FT STRAND 838..841 FT /evidence="ECO:0007829|PDB:2RV0" FT HELIX 842..852 FT /evidence="ECO:0007829|PDB:2ELO" FT HELIX 854..856 FT /evidence="ECO:0007829|PDB:2RV0" FT STRAND 883..886 FT /evidence="ECO:0007829|PDB:2ELP" FT HELIX 894..904 FT /evidence="ECO:0007829|PDB:2ELP" FT STRAND 908..910 FT /evidence="ECO:0007829|PDB:2ELQ" FT STRAND 912..915 FT /evidence="ECO:0007829|PDB:2ELQ" FT STRAND 917..919 FT /evidence="ECO:0007829|PDB:2ELQ" FT HELIX 921..930 FT /evidence="ECO:0007829|PDB:2ELQ" FT TURN 940..942 FT /evidence="ECO:0007829|PDB:2ELR" FT STRAND 945..948 FT /evidence="ECO:0007829|PDB:2RV3" FT HELIX 949..959 FT /evidence="ECO:0007829|PDB:2ELR" SQ SEQUENCE 1243 AA; 139034 MW; AF3E5339ED38D91C CRC64; METRAAENTA IFMCKCCNLF SPNQSELLSH VSEKHMEEGV NVDEIIIPLR PLSTPEPPNS SKTGDEFLVM KRKRGRPKGS TKKSSTEEEL AENIVSPTED SPLAPEEGNS LPPSSLECSK CCRKFSNTRQ LRKHICIIVL NLGEEEGEAG NESDLELEKK CKEDDREKAS KRPRSQKTEK VQKISGKEAR QLSGAKKPII SVVLTAHEAI PGATKIVPVE AGPPETGATN SETTSADLVP RRGYQEYAIQ QTPYEQPMKS SRLGPTQLKI FTCEYCNKVF KFKHSLQAHL RIHTNEKPYK CPQCSYASAI KANLNVHLRK HTGEKFACDY CSFTCLSKGH LKVHIERVHK KIKQHCRFCK KKYSDVKNLI KHIRDAHDPQ DKKVKEALDE LCLMTREGKR QLLYDCHICE RKFKNELDRD RHMLVHGDKW PFACELCGHG ATKYQALELH VRKHPFVYVC AVCRKKFVSS IRLRTHIKEV HGAAQEALVF TSSINQSFCL LEPGGDIQQE ALGDQLQLVE EEFALQGVNA LKEEACPGDT QLEEGRKEPE APGEMPAPAV HLASPQAEST ALPPCELETT VVSSSDLHSQ EVVSDDFLLK NDTSSAEAHA APEKPPDMQH RSSVQTQGEV ITLLLSKAQS AGSDQESHGA QSPLGEGQNM AVLSAGDPDP SRCLRSNPAE ASDLLPPVAG GGDTITHQPD SCKAAPEHRS GITAFMKVLN SLQKKQMNTS LCERIRKVYG DLECEYCGKL FWYQVHFDMH VRTHTREHLY YCSQCHYSSI TKNCLKRHVI QKHSNILLKC PTDGCDYSTP DKYKLQAHLK VHTALDKRSY SCPVCEKSFS EDRLIKSHIK TNHPEVSMST ISEVLGRRVQ LKGLIGKRAM KCPYCDFYFM KNGSDLQRHI WAHEGVKPFK CSLCEYATRS KSNLKAHMNR HSTEKTHLCD MCGKKFKSKG TLKSHKLLHT ADGKQFKCTV CDYTAAQKPQ LLRHMEQHVS FKPFRCAHCH YSCNISGSLK RHYNRKHPNE EYANVGTGEL AAEVLIQQGG LKCPVCSFVY GTKWEFNRHL KNKHGLKVVE IDGDPKWETA TEAPEEPSTQ YLHITEAEED VQGTQAAVAA LQDLRYTSES GDRLDPTAVN ILQQIIELGA ETHDATALAS VVAMAPGTVT VVKQVTEEEP SSNHTVMIQE TVQQASVELA EQHHLVVSSD DVEGIETVTV YTQGGEASEF IVYVQEAMQP VEEQAVEQPA QEL //