MYT1_HUMAN
ID MYT1_HUMAN Reviewed; 1121 AA.
AC Q01538; E1P5H0; F5H7M8; O94922; Q7Z5W2; Q9UPV2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Myelin transcription factor 1;
DE Short=MyT1;
DE AltName: Full=Myelin transcription factor I;
DE Short=MyTI;
DE AltName: Full=PLPB1;
DE AltName: Full=Proteolipid protein-binding protein;
GN Name=MYT1; Synonyms=KIAA0835, KIAA1050, MTF1, MYTI, PLPB1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-1121 (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-1121 (ISOFORM 2).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 424-1121 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=1280325; DOI=10.1128/mcb.12.12.5632-5639.1992;
RA Kim J.G., Hudson L.D.;
RT "Novel member of the zinc finger superfamily: a C2-HC finger that
RT recognizes a glia-specific gene.";
RL Mol. Cell. Biol. 12:5632-5639(1992).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=8530187; DOI=10.1002/glia.440140407;
RA Armstrong R.C., Kim J.G., Hudson L.D.;
RT "Expression of myelin transcription factor I (MyTI), a 'zinc-finger' DNA-
RT binding protein, in developing oligodendrocytes.";
RL Glia 14:303-321(1995).
RN [8]
RP INTERACTION WITH STEAP3.
RX PubMed=12606722; DOI=10.1073/pnas.0530298100;
RA Passer B.J., Nancy-Portebois V., Amzallag N., Prieur S., Cans C.,
RA Roborel de Climens A., Fiucci G., Bouvard V., Tuynder M., Susini L.,
RA Morchoisne S., Crible V., Lespagnol A., Dausset J., Oren M., Amson R.,
RA Telerman A.;
RT "The p53-inducible TSAP6 gene product regulates apoptosis and the cell
RT cycle and interacts with Nix and the Myt1 kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2284-2289(2003).
RN [9]
RP FUNCTION.
RX PubMed=14962745; DOI=10.1016/j.mcn.2003.10.001;
RA Nielsen J.A., Berndt J.A., Hudson L.D., Armstrong R.C.;
RT "Myelin transcription factor 1 (Myt1) modulates the proliferation and
RT differentiation of oligodendrocyte lineage cells.";
RL Mol. Cell. Neurosci. 25:111-123(2004).
CC -!- FUNCTION: Binds to the promoter region of genes encoding proteolipid
CC proteins of the central nervous system. May play a role in the
CC development of neurons and oligodendroglia in the CNS. May regulate a
CC critical transition point in oligodendrocyte lineage development by
CC modulating oligodendrocyte progenitor proliferation relative to
CC terminal differentiation and up-regulation of myelin gene
CC transcription. {ECO:0000269|PubMed:14962745}.
CC -!- SUBUNIT: Interacts with STEAP3. {ECO:0000269|PubMed:12606722}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q01538-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01538-2; Sequence=VSP_054313;
CC -!- TISSUE SPECIFICITY: Mostly in developing nervous system. Expressed in
CC neural progenitors and oligodendrocyte lineage cells. More highly
CC expressed in oligodendrocyte progenitors than in differentiated
CC oligodendrocytes. {ECO:0000269|PubMed:8530187}.
CC -!- DOMAIN: Contains 7 zinc fingers of the C2HC class arranged in two
CC widely separated clusters. These two domains of DNA binding can
CC function independently and recognize the same DNA sequence.
CC -!- SIMILARITY: Belongs to the MYT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74858.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB020642; BAA74858.2; ALT_INIT; mRNA.
DR EMBL; AL121581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75155.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75157.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75158.1; -; Genomic_DNA.
DR EMBL; AB028973; BAA83002.1; -; mRNA.
DR EMBL; BC053638; AAH53638.1; -; mRNA.
DR EMBL; M96980; AAA59897.1; -; mRNA.
DR CCDS; CCDS13558.1; -. [Q01538-1]
DR RefSeq; NP_004526.1; NM_004535.2. [Q01538-1]
DR AlphaFoldDB; Q01538; -.
DR SMR; Q01538; -.
DR BioGRID; 110744; 11.
DR IntAct; Q01538; 4.
DR MINT; Q01538; -.
DR STRING; 9606.ENSP00000327465; -.
DR BindingDB; Q01538; -.
DR ChEMBL; CHEMBL2331044; -.
DR DrugCentral; Q01538; -.
DR iPTMnet; Q01538; -.
DR PhosphoSitePlus; Q01538; -.
DR BioMuta; MYT1; -.
DR DMDM; 13638422; -.
DR jPOST; Q01538; -.
DR MassIVE; Q01538; -.
DR MaxQB; Q01538; -.
DR PaxDb; Q01538; -.
DR PeptideAtlas; Q01538; -.
DR PRIDE; Q01538; -.
DR ProteomicsDB; 27533; -.
DR ProteomicsDB; 57968; -. [Q01538-1]
DR Antibodypedia; 1424; 304 antibodies from 26 providers.
DR DNASU; 4661; -.
DR Ensembl; ENST00000328439.6; ENSP00000327465.1; ENSG00000196132.14. [Q01538-1]
DR Ensembl; ENST00000536311.5; ENSP00000442412.1; ENSG00000196132.14. [Q01538-2]
DR Ensembl; ENST00000613234.3; ENSP00000477771.2; ENSG00000276876.4. [Q01538-1]
DR Ensembl; ENST00000616648.2; ENSP00000483021.1; ENSG00000276876.4. [Q01538-2]
DR Ensembl; ENST00000650655.1; ENSP00000498616.1; ENSG00000196132.14. [Q01538-1]
DR GeneID; 4661; -.
DR KEGG; hsa:4661; -.
DR MANE-Select; ENST00000328439.6; ENSP00000327465.1; NM_004535.3; NP_004526.1.
DR UCSC; uc002yii.3; human. [Q01538-1]
DR CTD; 4661; -.
DR DisGeNET; 4661; -.
DR GeneCards; MYT1; -.
DR HGNC; HGNC:7622; MYT1.
DR HPA; ENSG00000196132; Tissue enhanced (brain, pituitary gland, retina).
DR MIM; 600379; gene.
DR neXtProt; NX_Q01538; -.
DR OpenTargets; ENSG00000196132; -.
DR PharmGKB; PA31426; -.
DR VEuPathDB; HostDB:ENSG00000196132; -.
DR eggNOG; KOG3803; Eukaryota.
DR GeneTree; ENSGT00940000156364; -.
DR HOGENOM; CLU_007226_0_0_1; -.
DR InParanoid; Q01538; -.
DR OMA; IRLPHMD; -.
DR OrthoDB; 116799at2759; -.
DR PhylomeDB; Q01538; -.
DR TreeFam; TF317299; -.
DR PathwayCommons; Q01538; -.
DR SignaLink; Q01538; -.
DR SIGNOR; Q01538; -.
DR BioGRID-ORCS; 4661; 18 hits in 1092 CRISPR screens.
DR GeneWiki; MYT1; -.
DR GenomeRNAi; 4661; -.
DR Pharos; Q01538; Tchem.
DR PRO; PR:Q01538; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q01538; protein.
DR Bgee; ENSG00000196132; Expressed in ganglionic eminence and 80 other tissues.
DR ExpressionAtlas; Q01538; baseline and differential.
DR Genevisible; Q01538; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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; NAS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR InterPro; IPR013681; Myelin_TF.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR Pfam; PF08474; MYT1; 2.
DR Pfam; PF01530; zf-C2HC; 7.
DR SUPFAM; SSF103637; SSF103637; 7.
DR PROSITE; PS51802; ZF_CCHHC; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation; DNA-binding;
KW Metal-binding; Neurogenesis; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1121
FT /note="Myelin transcription factor 1"
FT /id="PRO_0000096676"
FT ZN_FING 21..64
FT /note="CCHHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 433..476
FT /note="CCHHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 477..520
FT /note="CCHHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 791..834
FT /note="CCHHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 835..878
FT /note="CCHHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 884..927
FT /note="CCHHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 937..980
FT /note="CCHHC-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..311
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 491
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 800
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 805
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 818
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 824
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 844
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 849
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 862
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 868
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 911
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 917
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 946
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 951
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 964
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 970
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT VAR_SEQ 616
FT /note="C -> SKPFPKASSPRHSPSSSYVRSTSSSSAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1280325,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_054313"
FT CONFLICT 567..574
FT /note="ATPRANLA -> RHTQGQLG (in Ref. 6; AAA59897)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="A -> T (in Ref. 6; AAA59897)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="G -> D (in Ref. 6; AAA59897)"
FT /evidence="ECO:0000305"
FT CONFLICT 957..958
FT /note="AN -> TI (in Ref. 6; AAA59897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1075
FT /note="R -> H (in Ref. 6; AAA59897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1088..1089
FT /note="DA -> VP (in Ref. 6; AAA59897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1102
FT /note="D -> A (in Ref. 6; AAA59897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1121 AA; 122329 MW; D4AF1F8C7D4EC01E CRC64;
MSLENEDKRA RTRSKALRGP PETTAADLSC PTPGCTGSGH VRGKYSRHRS LQSCPLAKKR
KLEGAEAEHL VSKRKSHPLK LALDEGYGVD SDGSEDTEVK DASVSDESEG TLEGAEAETS
GQDEIHRPET AEGRSPVKSH FGSNPIGSAT ASSKGSYSSY QGIIATSLLN LGQIAEETLV
EEDLGQAAKP GPGIVHLLQE AAEGAASEEG EKGLFIQPED AEEVVEVTTE RSQDLCPQSL
EDAASEESSK QKGILSHEEE DEEEEEEEEE EEEDEEEEEE EEEEEEEEEE EEEEEEEEEE
EEEEEEAAPD VIFQEDTSHT SAQKAPELRG PESPSPKPEY SVIVEVRSDD DKDEDTHSRK
STVTDESEMQ DMMTRGNLGL LEQAIALKAE QVRTVCEPGC PPAEQSQLGL GEPGKAAKPL
DTVRKSYYSK DPSRAEKREI KCPTPGCDGT GHVTGLYPHH RSLSGCPHKD RIPPEILAMH
ENVLKCPTPG CTGQGHVNSN RNTHRSLSGC PIAAAEKLAK SHEKQQPQTG DPSKSSSNSD
RILRPMCFVK QLEVPPYGSY RPNVAPATPR ANLAKELEKF SKVTFDYASF DAQVFGKRML
APKIQTSETS PKAFQCFDYS QDAEAAHMAA TAILNLSTRC WEMPENLSTK PQDLPSKSVD
IEVDENGTLD LSMHKHRKRE NAFPSSSSCS SSPGVKSPDA SQRHSSTSAP SSSMTSPQSS
QASRQDEWDR PLDYTKPSRL REEEPEESEP AAHSFASSEA DDQEVSEENF EERKYPGEVT
LTNFKLKFLS KDIKKELLTC PTPGCDGSGH ITGNYASHRS LSGCPLADKS LRNLMAAHSA
DLKCPTPGCD GSGHITGNYA SHRSLSGCPR AKKSGVKVAP TKDDKEDPEL MKCPVPGCVG
LGHISGKYAS HRSASGCPLA ARRQKEGSLN GSSFSWKSLK NEGPTCPTPG CDGSGHANGS
FLTHRSLSGC PRATFAGKKG KLSGDEVLSP KFKTSDVLEN DEEIKQLNQE IRDLNESNSE
MEAAMVQLQS QISSMEKNLK NIEEENKLIE EQNEALFLEL SGLSQALIQS LANIRLPHME
PICEQNFDAY VSTLTDMYSN QDPENKDLLE SIKQAVRGIQ V
