MYT1L_MOUSE
ID MYT1L_MOUSE Reviewed; 1187 AA.
AC P97500; A2RRK5; D3Z1P7; O08996; Q33DP0; Q8C643; Q8C7L4; Q8CHB4;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Myelin transcription factor 1-like protein {ECO:0000303|PubMed:9373037};
DE Short=MyT1-L {ECO:0000303|PubMed:9373037};
DE Short=MyT1L {ECO:0000303|PubMed:9373037};
DE AltName: Full=Neural zinc finger factor 1 {ECO:0000250|UniProtKB:P70475};
DE Short=NZF-1 {ECO:0000250|UniProtKB:P70475};
DE AltName: Full=Postmitotic neural gene 1 protein {ECO:0000303|PubMed:9130664};
DE AltName: Full=Zinc finger protein Png-1 {ECO:0000303|PubMed:9130664};
GN Name=Myt1l {ECO:0000303|PubMed:9373037, ECO:0000312|MGI:MGI:1100511};
GN Synonyms=Kiaa1106 {ECO:0000303|PubMed:12465718},
GN Nzf1 {ECO:0000250|UniProtKB:P70475}, Png1 {ECO:0000303|PubMed:9130664};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP INDUCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9130664;
RX DOI=10.1002/(sici)1096-9861(19970505)381:2<130::aid-cne2>3.0.co;2-4;
RA Weiner J.A., Chun J.;
RT "Png-1, a nervous system-specific zinc finger gene, identifies regions
RT containing postmitotic neurons during mammalian embryonic development.";
RL J. Comp. Neurol. 381:130-142(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9373037;
RX DOI=10.1002/(sici)1097-4547(19971015)50:2<272::aid-jnr16>3.0.co;2-a;
RA Kim J.G., Armstrong R.C., Agoston D.V., Robinsky A., Wiese C., Nagle J.,
RA Hudson L.D.;
RT "Myelin transcription factor 1 (Myt1) of the oligodendrocyte lineage, along
RT with a closely related CCHC zinc finger, is expressed in developing neurons
RT in the mammalian central nervous system.";
RL J. Neurosci. Res. 50:272-290(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=21540077; DOI=10.1016/j.neulet.2011.04.033;
RA Kameyama T., Matsushita F., Kadokawa Y., Marunouchi T.;
RT "Myt/NZF family transcription factors regulate neuronal differentiation of
RT P19 cells.";
RL Neurosci. Lett. 497:74-79(2011).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION.
RX PubMed=20107439; DOI=10.1038/nature08797;
RA Vierbuchen T., Ostermeier A., Pang Z.P., Kokubu Y., Suedhof T.C.,
RA Wernig M.;
RT "Direct conversion of fibroblasts to functional neurons by defined
RT factors.";
RL Nature 463:1035-1041(2010).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24243019; DOI=10.1016/j.cell.2013.09.028;
RA Wapinski O.L., Vierbuchen T., Qu K., Lee Q.Y., Chanda S., Fuentes D.R.,
RA Giresi P.G., Ng Y.H., Marro S., Neff N.F., Drechsel D., Martynoga B.,
RA Castro D.S., Webb A.E., Suedhof T.C., Brunet A., Guillemot F., Chang H.Y.,
RA Wernig M.;
RT "Hierarchical mechanisms for direct reprogramming of fibroblasts to
RT neurons.";
RL Cell 155:621-635(2013).
RN [11]
RP FUNCTION.
RX PubMed=27281220; DOI=10.1038/nature18323;
RA Treutlein B., Lee Q.Y., Camp J.G., Mall M., Koh W., Shariati S.A., Sim S.,
RA Neff N.F., Skotheim J.M., Wernig M., Quake S.R.;
RT "Dissecting direct reprogramming from fibroblast to neuron using single-
RT cell RNA-seq.";
RL Nature 534:391-395(2016).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, AND INTERACTION WITH SIN3B.
RX PubMed=28379941; DOI=10.1038/nature21722;
RA Mall M., Kareta M.S., Chanda S., Ahlenius H., Perotti N., Zhou B.,
RA Grieder S.D., Ge X., Drake S., Euong Ang C., Walker B.M., Vierbuchen T.,
RA Fuentes D.R., Brennecke P., Nitta K.R., Jolma A., Steinmetz L.M.,
RA Taipale J., Suedhof T.C., Wernig M.;
RT "Myt1l safeguards neuronal identity by actively repressing many non-
RT neuronal fates.";
RL Nature 544:245-249(2017).
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 (PubMed:28379941). In contrast to
CC other transcription repressors that inhibit specific lineages, mediates
CC repression of multiple differentiation programs (PubMed:28379941). Also
CC represses expression of negative regulators of neurogenesis, such as
CC members of the Notch signaling pathway, including HES1
CC (PubMed:28379941). The combination of three transcription factors,
CC ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram fibroblasts
CC and other somatic cells into induced neuronal (iN) cells in vitro
CC (PubMed:20107439, PubMed:24243019, PubMed:27281220). Directly binds the
CC 5'-AAGTT-3' core motif present on the promoter of target genes and
CC represses transcription by recruiting a multiprotein complex containing
CC SIN3B (PubMed:28379941). The 5'-AAGTT-3' core motif is absent from the
CC promoter of neural genes (PubMed:28379941).
CC {ECO:0000269|PubMed:20107439, ECO:0000269|PubMed:24243019,
CC ECO:0000269|PubMed:27281220, ECO:0000269|PubMed:28379941,
CC ECO:0000269|PubMed:9130664, ECO:0000269|PubMed:9373037}.
CC -!- SUBUNIT: Interacts with SIN3B. {ECO:0000269|PubMed:28379941}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24243019,
CC ECO:0000269|PubMed:28379941, ECO:0000269|PubMed:9373037}. Chromosome
CC {ECO:0000269|PubMed:28379941}. Note=Preferentially binds to DNA binding
CC sites that are in an open chromatin configuration (PubMed:28379941).
CC {ECO:0000269|PubMed:28379941}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P97500-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97500-2; Sequence=VSP_015728;
CC Name=3;
CC IsoId=P97500-3; Sequence=VSP_015726, VSP_015729, VSP_015730,
CC VSP_015731;
CC Name=4;
CC IsoId=P97500-4; Sequence=VSP_015727, VSP_015728, VSP_015730,
CC VSP_015731;
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:9130664}.
CC -!- DEVELOPMENTAL STAGE: Expression is restricted to and present throughout
CC the embryonic CNS and developing peripheral neural structures. In the
CC embryonic CNS, expression is restricted to postmitotic neuronal
CC regions. During the neurogenetic period (11 dpc-17 dpc) expression is
CC associated temporally and spatially with the known generation of the
CC first cortical neurons with known gradients of neuron production.
CC Expression continues in developing postmitotic cortical neurons
CC throughout embryonic development and is expressed within 2 days of
CC neuronal induction in P19 cells. {ECO:0000269|PubMed:9130664}.
CC -!- INDUCTION: Up-regulated by retinoic acid. {ECO:0000269|PubMed:9130664}.
CC -!- SIMILARITY: Belongs to the MYT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53457.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC41467.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U86338; AAC53157.1; -; mRNA.
DR EMBL; AF004295; AAC53457.1; ALT_FRAME; mRNA.
DR EMBL; AB212898; BAE48255.1; -; mRNA.
DR EMBL; AK049967; BAC34010.1; -; mRNA.
DR EMBL; AK076608; BAC36413.1; -; mRNA.
DR EMBL; AB093283; BAC41467.1; ALT_INIT; mRNA.
DR EMBL; AC154318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC166936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131677; AAI31678.1; -; mRNA.
DR CCDS; CCDS49041.1; -. [P97500-2]
DR CCDS; CCDS49042.1; -. [P97500-1]
DR PIR; T30189; T30189.
DR PIR; T46608; T46608.
DR RefSeq; NP_001087244.1; NM_001093775.1. [P97500-1]
DR RefSeq; XP_011242129.1; XM_011243827.2. [P97500-1]
DR RefSeq; XP_011242131.1; XM_011243829.2.
DR RefSeq; XP_017170459.1; XM_017314970.1.
DR AlphaFoldDB; P97500; -.
DR SMR; P97500; -.
DR STRING; 10090.ENSMUSP00000058264; -.
DR iPTMnet; P97500; -.
DR PhosphoSitePlus; P97500; -.
DR MaxQB; P97500; -.
DR PaxDb; P97500; -.
DR PRIDE; P97500; -.
DR ProteomicsDB; 287544; -. [P97500-1]
DR ProteomicsDB; 287545; -. [P97500-2]
DR ProteomicsDB; 287546; -. [P97500-3]
DR ProteomicsDB; 287547; -. [P97500-4]
DR Antibodypedia; 62900; 61 antibodies from 24 providers.
DR DNASU; 17933; -.
DR Ensembl; ENSMUST00000021009; ENSMUSP00000021009; ENSMUSG00000061911. [P97500-2]
DR Ensembl; ENSMUST00000049784; ENSMUSP00000058264; ENSMUSG00000061911. [P97500-1]
DR Ensembl; ENSMUST00000218198; ENSMUSP00000151919; ENSMUSG00000061911. [P97500-3]
DR Ensembl; ENSMUST00000218583; ENSMUSP00000151588; ENSMUSG00000061911. [P97500-2]
DR GeneID; 17933; -.
DR KEGG; mmu:17933; -.
DR UCSC; uc007ngi.1; mouse. [P97500-3]
DR CTD; 23040; -.
DR MGI; MGI:1100511; Myt1l.
DR VEuPathDB; HostDB:ENSMUSG00000061911; -.
DR eggNOG; KOG3803; Eukaryota.
DR GeneTree; ENSGT00940000155671; -.
DR InParanoid; P97500; -.
DR OMA; KVQTRDM; -.
DR PhylomeDB; P97500; -.
DR TreeFam; TF317299; -.
DR ChiTaRS; Myt1l; mouse.
DR PRO; PR:P97500; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P97500; protein.
DR Bgee; ENSMUSG00000061911; Expressed in caudate-putamen and 158 other tissues.
DR ExpressionAtlas; P97500; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0050897; F:cobalt ion binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IDA:UniProtKB.
DR GO; GO:0048666; P:neuron development; IDA:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IDA:UniProtKB.
DR GO; GO:0048663; P:neuron fate commitment; IDA:UniProtKB.
DR GO; GO:0048665; P:neuron fate specification; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; Developmental protein;
KW Differentiation; DNA-binding; Metal-binding; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1187
FT /note="Myelin transcription factor 1-like protein"
FT /id="PRO_0000096674"
FT ZN_FING 22..65
FT /note="CCHHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 498..541
FT /note="CCHHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 542..585
FT /note="CCHHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 897..940
FT /note="CCHHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 946..989
FT /note="CCHHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 999..1042
FT /note="CCHHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1058..1132
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..508
FT /note="Basic and acidic 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 507
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 531
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 551
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 556
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 911
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 924
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 930
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 955
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 960
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 973
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 979
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1008
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1013
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1026
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1032
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..597
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015726"
FT VAR_SEQ 1..426
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015727"
FT VAR_SEQ 494..495
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12465718,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9373037"
FT /id="VSP_015728"
FT VAR_SEQ 598..605
FT /note="SNQASDRV -> MTNRQYFP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015729"
FT VAR_SEQ 906..925
FT /note="CPTPGCDGSGHITGNYASHR -> LPVQGPSAIDHLLMFSDFLN (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015730"
FT VAR_SEQ 926..1187
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015731"
FT CONFLICT 24..25
FT /note="AI -> L (in Ref. 2; AAC53457)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="M -> V (in Ref. 2; AAC53457)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="D -> AS (in Ref. 1; AAC53157)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="E -> D (in Ref. 1; AAC53157, 2; AAC53457, 3;
FT BAE48255, 5; BAC41467 and 7; AAI31678)"
FT CONFLICT 172
FT /note="Missing (in Ref. 2; AAC53457)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="L -> S (in Ref. 2; AAC53457)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="K -> R (in Ref. 2; AAC53457)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="V -> A (in Ref. 2; AAC53457)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="T -> N (in Ref. 4; BAC34010)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="N -> K (in Ref. 4; BAC34010)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="S -> N (in Ref. 3; BAE48255 and 4; BAC34010/
FT BAC36413)"
FT CONFLICT 1072
FT /note="E -> G (in Ref. 2; AAC53457)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1187 AA; 132945 MW; 85A1B239FA198F2E CRC64;
MDVDSEEKRH RTRSKGVRVP VEPAIQELFS CPTPGCDGSG HVSGKYARHR SVYGCPLAKK
RKTQDKQPQE PAPKRKPFAV KADSSSVDEC YESDGTEDMD DKEEDDDEEF SEDNDEQGDD
DDEDEVDRED EEEIEEEDDE EDDDDEDGDD VEEEEEDDDE EEEEEEEEEE NEDHQMSCTR
IMQDTDKDDN NNDEYDNYDE LVAKSLLNLG KIAEDAAYRA RTESEMNSNT SNSLEDDSDK
NENLGRKSEL SLDLDSDVVR ETVDSLKLLA QGHGVVLSEN ISDRSYAEGM SQQDSRNMNY
VMLGKPMNNG LMEKMVEESD EEVCLSSLEC LRNQCFDLAR KLSETNPQDR SQPPNMSVRQ
HVRQEDDFPG RTPDRSYSDM MNLMRLEEQL SPRSRTFSSC AKEDGCHERD DDTTSVNSDR
SEEVFDMTKG NLTLLEKAIA LETERAKAMR EKMAMDAGRR DNLRSYEDQS PRQLAGEDRK
SKSSDSHVKK PYYGKDPSRT EKRESKCPTP GCDGTGHVTG LYPHHRSLSG CPHKDRVPPE
ILAMHENVLK CPTPGCTGRG HVNSNRNSHR SLSGCPIAAA EKLAKAQEKH QSCDVSKSNQ
ASDRVLRPMC FVKQLEIPQY GYRNNVPTTT PRSNLAKELE KYSKTSFEYN SYDNHTYGKR
AIAPKVQTRD ISPKGYDDAK RYCKNASPSS STTSSYAPSS SSNLSCGGGS SASSTCSKSS
FDYTHDMEAA HMAATAILNL STRCREMPQN LSTKPQDLCT ARNPDMEVDE NGTLDLSMNK
QRPRDSCCPV LTPLEPMSPQ QQAVMSSRCF QLSEGDCWDL PVDYTKMKPR RVDEDEPKEI
TPEDLDPFQE ALEERRYPGE VTIPSPKPKY PQCKESKKDL ITLSGCPLAD KSIRSMLATS
SQELKCPTPG CDGSGHITGN YASHRSLSGC PRAKKSGIRI AQSKEDKEDQ EPIRCPVPGC
DGQGHITGKY ASHRSASGCP LAAKRQKDGY LNGSQFSWKS VKTEGMSCPT PGCDGSGHVS
GSFLTHRSLS GCPRATSAMK KAKLSGEQML TIKQRASNGI ENDEEIKQLD EEIKELNESN
SQMEADMIKL RTQITTMESN LKTIEEENKV IEQQNESLLH ELANLSQSLI HSLANIQLPH
MDPINEQNFD AYVTTLTEMY TNQDRYQSPE NKALLENIKQ AVRGIQV
