MYT1L_HUMAN
ID MYT1L_HUMAN Reviewed; 1186 AA.
AC Q9UL68; A7E2C7; B2RP54; Q6IQ17; Q9UPP6;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Myelin transcription factor 1-like protein {ECO:0000303|Ref.1};
DE Short=MyT1-L {ECO:0000303|Ref.1};
DE Short=MyT1L {ECO:0000303|Ref.1};
GN Name=MYT1L {ECO:0000303|Ref.1, ECO:0000312|HGNC:HGNC:7623};
GN Synonyms=KIAA1106 {ECO:0000303|PubMed:10470851};
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] (ISOFORM 1).
RA Wege I., Wilhelm C., Schulz-Schaeffer W., von Beust G., Bink K.,
RA Laccone F.;
RT "Cloning and expression of the human homologous of the MyT1-L C2HC zinc
RT finger gene.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Testis;
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 [6]
RP INVOLVEMENT IN MRD39.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
RN [7]
RP INVOLVEMENT IN MRD39.
RX PubMed=23160955; DOI=10.1126/science.1227764;
RA O'Roak B.J., Vives L., Fu W., Egertson J.D., Stanaway I.B., Phelps I.G.,
RA Carvill G., Kumar A., Lee C., Ankenman K., Munson J., Hiatt J.B.,
RA Turner E.H., Levy R., O'Day D.R., Krumm N., Coe B.P., Martin B.K.,
RA Borenstein E., Nickerson D.A., Mefford H.C., Doherty D., Akey J.M.,
RA Bernier R., Eichler E.E., Shendure J.;
RT "Multiplex targeted sequencing identifies recurrently mutated genes in
RT autism spectrum disorders.";
RL Science 338:1619-1622(2012).
CC -!- FUNCTION: Transcription factor that plays a key role in neuronal
CC differentiation by specifically repressing expression of non-neuronal
CC genes during neuron differentiation. In contrast to other transcription
CC repressors that inhibit specific lineages, mediates repression of
CC multiple differentiation programs. Also represses expression of
CC negative regulators of neurogenesis, such as members of the Notch
CC signaling pathway, including HES1. The combination of three
CC transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to
CC reprogram fibroblasts and other somatic cells into induced neuronal
CC (iN) cells in vitro. Directly binds the 5'-AAGTT-3' core motif present
CC on the promoter of target genes and represses transcription by
CC recruiting a multiprotein complex containing SIN3B. The 5'-AAGTT-3'
CC core motif is absent from the promoter of neural genes.
CC {ECO:0000250|UniProtKB:P97500}.
CC -!- SUBUNIT: Interacts with SIN3B. {ECO:0000250|UniProtKB:P97500}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P97500}.
CC Chromosome {ECO:0000250|UniProtKB:P97500}. Note=Preferentially binds to
CC DNA binding sites that are in an open chromatin configuration.
CC {ECO:0000250|UniProtKB:P97500}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UL68-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9UL68-3; Sequence=VSP_015722, VSP_015725;
CC Name=4;
CC IsoId=Q9UL68-4; Sequence=VSP_015724;
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 39
CC (MRD39) [MIM:616521]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRD39
CC patients show delayed psychomotor development and autistic features.
CC {ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23160955}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the MYT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14051.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAI50282.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAA83058.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA83058.2; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AF036943; AAF14051.1; ALT_FRAME; mRNA.
DR EMBL; AB029029; BAA83058.2; ALT_SEQ; mRNA.
DR EMBL; AC008276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC071612; AAH71612.1; -; mRNA.
DR EMBL; BC137272; AAI37273.1; -; mRNA.
DR EMBL; BC137273; AAI37274.1; -; mRNA.
DR EMBL; BC150281; AAI50282.1; ALT_SEQ; mRNA.
DR CCDS; CCDS46222.1; -. [Q9UL68-4]
DR CCDS; CCDS77378.1; -. [Q9UL68-1]
DR RefSeq; NP_001289981.1; NM_001303052.1. [Q9UL68-1]
DR RefSeq; NP_001316773.1; NM_001329844.1. [Q9UL68-1]
DR RefSeq; NP_001316774.1; NM_001329845.1. [Q9UL68-1]
DR RefSeq; NP_001316776.1; NM_001329847.1. [Q9UL68-4]
DR RefSeq; NP_001316777.1; NM_001329848.1. [Q9UL68-4]
DR RefSeq; NP_055840.2; NM_015025.3. [Q9UL68-4]
DR AlphaFoldDB; Q9UL68; -.
DR SMR; Q9UL68; -.
DR BioGRID; 116679; 5.
DR IntAct; Q9UL68; 7.
DR STRING; 9606.ENSP00000396103; -.
DR iPTMnet; Q9UL68; -.
DR PhosphoSitePlus; Q9UL68; -.
DR BioMuta; MYT1L; -.
DR DMDM; 327478568; -.
DR jPOST; Q9UL68; -.
DR MassIVE; Q9UL68; -.
DR MaxQB; Q9UL68; -.
DR PaxDb; Q9UL68; -.
DR PeptideAtlas; Q9UL68; -.
DR PRIDE; Q9UL68; -.
DR ProteomicsDB; 84961; -. [Q9UL68-1]
DR ProteomicsDB; 84963; -. [Q9UL68-3]
DR ProteomicsDB; 84964; -. [Q9UL68-4]
DR Antibodypedia; 62900; 61 antibodies from 24 providers.
DR DNASU; 23040; -.
DR Ensembl; ENST00000399161.8; ENSP00000382114.3; ENSG00000186487.21. [Q9UL68-4]
DR Ensembl; ENST00000407844.6; ENSP00000384219.1; ENSG00000186487.21. [Q9UL68-3]
DR Ensembl; ENST00000428368.7; ENSP00000396103.3; ENSG00000186487.21. [Q9UL68-1]
DR Ensembl; ENST00000647694.1; ENSP00000497722.1; ENSG00000186487.21. [Q9UL68-1]
DR Ensembl; ENST00000647738.2; ENSP00000497479.2; ENSG00000186487.21. [Q9UL68-1]
DR Ensembl; ENST00000648316.1; ENSP00000497870.1; ENSG00000186487.21. [Q9UL68-4]
DR Ensembl; ENST00000648928.1; ENSP00000497017.1; ENSG00000186487.21. [Q9UL68-4]
DR Ensembl; ENST00000649207.1; ENSP00000496986.1; ENSG00000186487.21. [Q9UL68-4]
DR GeneID; 23040; -.
DR KEGG; hsa:23040; -.
DR MANE-Select; ENST00000647738.2; ENSP00000497479.2; NM_001303052.2; NP_001289981.1.
DR UCSC; uc002qxd.4; human. [Q9UL68-1]
DR CTD; 23040; -.
DR DisGeNET; 23040; -.
DR GeneCards; MYT1L; -.
DR HGNC; HGNC:7623; MYT1L.
DR HPA; ENSG00000186487; Group enriched (brain, pituitary gland).
DR MalaCards; MYT1L; -.
DR MIM; 613084; gene.
DR MIM; 616521; phenotype.
DR neXtProt; NX_Q9UL68; -.
DR OpenTargets; ENSG00000186487; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA31427; -.
DR VEuPathDB; HostDB:ENSG00000186487; -.
DR eggNOG; KOG3803; Eukaryota.
DR GeneTree; ENSGT00940000155671; -.
DR HOGENOM; CLU_1622834_0_0_1; -.
DR InParanoid; Q9UL68; -.
DR OMA; KVQTRDM; -.
DR OrthoDB; 116799at2759; -.
DR PhylomeDB; Q9UL68; -.
DR TreeFam; TF317299; -.
DR PathwayCommons; Q9UL68; -.
DR SignaLink; Q9UL68; -.
DR SIGNOR; Q9UL68; -.
DR BioGRID-ORCS; 23040; 39 hits in 1097 CRISPR screens.
DR ChiTaRS; MYT1L; human.
DR GenomeRNAi; 23040; -.
DR Pharos; Q9UL68; Tbio.
DR PRO; PR:Q9UL68; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UL68; protein.
DR Bgee; ENSG00000186487; Expressed in endothelial cell and 134 other tissues.
DR ExpressionAtlas; Q9UL68; baseline and differential.
DR Genevisible; Q9UL68; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0048663; P:neuron fate commitment; ISS:UniProtKB.
DR GO; GO:0048665; P:neuron fate specification; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR InterPro; IPR013681; Myelin_TF.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR Pfam; PF08474; MYT1; 1.
DR Pfam; PF01530; zf-C2HC; 6.
DR SUPFAM; SSF103637; SSF103637; 6.
DR PROSITE; PS51802; ZF_CCHHC; 6.
PE 2: Evidence at transcript level;
KW Alternative splicing; Autism spectrum disorder; Chromosome; Coiled coil;
KW Developmental protein; Differentiation; DNA-binding;
KW Intellectual disability; Metal-binding; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1186
FT /note="Myelin transcription factor 1-like protein"
FT /id="PRO_0000096673"
FT ZN_FING 22..65
FT /note="CCHHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 497..540
FT /note="CCHHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 541..584
FT /note="CCHHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 896..939
FT /note="CCHHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 945..988
FT /note="CCHHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 998..1041
FT /note="CCHHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1056..1130
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..169
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 910
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 923
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 929
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 954
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 959
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 972
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 978
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1007
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1012
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1025
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1031
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97500"
FT VAR_SEQ 1..1004
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015722"
FT VAR_SEQ 493..494
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015724"
FT VAR_SEQ 1092
FT /note="Q -> QVT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015725"
FT CONFLICT 108..159
FT /note="Missing (in Ref. 2; BAA83058 and 5; AAI50282)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="N -> S (in Ref. 1; AAF14051)"
FT /evidence="ECO:0000305"
FT CONFLICT 935
FT /note="S -> R (in Ref. 1; AAF14051)"
FT /evidence="ECO:0000305"
FT CONFLICT 987
FT /note="D -> E (in Ref. 1; AAF14051)"
FT /evidence="ECO:0000305"
FT CONFLICT 1110
FT /note="I -> V (in Ref. 1; AAF14051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1186 AA; 133043 MW; AEF068692263FA8C CRC64;
MEVDTEEKRH RTRSKGVRVP VEPAIQELFS CPTPGCDGSG HVSGKYARHR SVYGCPLAKK
RKTQDKQPQE PAPKRKPFAV KADSSSVDEC DDSDGTEDMD EKEEDEGEEY SEDNDEPGDE
DEEDEEGDRE EEEEIEEEDE DDDEDGEDVE DEEEEEEEEE EEEEEEENED HQMNCHNTRI
MQDTEKDDNN NDEYDNYDEL VAKSLLNLGK IAEDAAYRAR TESEMNSNTS NSLEDDSDKN
ENLGRKSELS LDLDSDVVRE TVDSLKLLAQ GHGVVLSENM NDRNYADSMS QQDSRNMNYV
MLGKPMNNGL MEKMVEESDE EVCLSSLECL RNQCFDLARK LSETNPQERN PQQNMNIRQH
VRPEEDFPGR TPDRNYSDML NLMRLEEQLS PRSRVFASCA KEDGCHERDD DTTSVNSDRS
EEVFDMTKGN LTLLEKAIAL ETERAKAMRE KMAMEAGRRD NMRSYEDQSP RQLPGEDRKP
KSSDSHVKKP YYGKDPSRTE KKESKCPTPG CDGTGHVTGL YPHHRSLSGC PHKDRVPPEI
LAMHESVLKC PTPGCTGRGH VNSNRNSHRS LSGCPIAAAE KLAKAQEKHQ SCDVSKSSQA
SDRVLRPMCF VKQLEIPQYG YRNNVPTTTP RSNLAKELEK YSKTSFEYNS YDNHTYGKRA
IAPKVQTRDI SPKGYDDAKR YCKDPSPSSS STSSYAPSSS SNLSCGGGSS ASSTCSKSSF
DYTHDMEAAH MAATAILNLS TRCREMPQNL STKPQDLCAT RNPDMEVDEN GTLDLSMNKQ
RPRDSCCPIL TPLEPMSPQQ QAVMNNRCFQ LGEGDCWDLP VDYTKMKPRR IDEDESKDIT
PEDLDPFQEA LEERRYPGEV TIPSPKPKYP QCKESKKDLI TLSGCPLADK SIRSMLATSS
QELKCPTPGC DGSGHITGNY ASHRSLSGCP RAKKSGIRIA QSKEDKEDQE PIRCPVPGCD
GQGHITGKYA SHRSASGCPL AAKRQKDGYL NGSQFSWKSV KTEGMSCPTP GCDGSGHVSG
SFLTHRSLSG CPRATSAMKK AKLSGEQMLT IKQRASNGIE NDEEIKQLDE EIKELNESNS
QMEADMIKLR TQITTMESNL KTIEEENKVI EQQNESLLHE LANLSQSLIH SLANIQLPHM
DPINEQNFDA YVTTLTEMYT NQDRYQSPEN KALLENIKQA VRGIQV
