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 Genevisible; Q9P243; HS.
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.
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
//
