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 27-MAR-2024, entry version 204. 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}; 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; 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 PDB; 7Q45; X-ray; 2.10 A; B/D/F=347-360. DR PDBsum; 7Q45; -. DR AlphaFoldDB; Q01538; -. DR SMR; Q01538; -. DR BioGRID; 110744; 11. DR IntAct; Q01538; 4. DR MINT; Q01538; -. DR STRING; 9606.ENSP00000498616; -. 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; 9606-ENSP00000327465; -. DR PeptideAtlas; Q01538; -. DR ProteomicsDB; 27533; -. DR ProteomicsDB; 57968; -. [Q01538-1] DR Antibodypedia; 1424; 323 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 AGR; HGNC:7622; -. DR CTD; 4661; -. DR DisGeNET; 4661; -. DR GeneCards; MYT1; -. DR HGNC; HGNC:7622; MYT1. DR HPA; ENSG00000196132; Tissue enriched (brain). 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; APDVIFE; -. DR OrthoDB; 3091993at2759; -. DR PhylomeDB; Q01538; -. DR TreeFam; TF317299; -. DR PathwayCommons; Q01538; -. DR SignaLink; Q01538; -. DR SIGNOR; Q01538; -. DR BioGRID-ORCS; 4661; 20 hits in 1175 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 81 other cell types or tissues. DR ExpressionAtlas; Q01538; baseline and differential. 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; NAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. 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: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:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. DR Gene3D; 4.10.320.30; -; 7. DR InterPro; IPR013681; Myelin_TF. DR InterPro; IPR002515; Znf_C2H2C. DR InterPro; IPR036060; Znf_C2H2C_sf. DR PANTHER; PTHR10816:SF10; MYELIN TRANSCRIPTION FACTOR 1; 1. DR PANTHER; PTHR10816; MYELIN TRANSCRIPTION FACTOR 1-RELATED; 1. DR Pfam; PF08474; MYT1; 2. DR Pfam; PF01530; zf-C2HC; 7. DR SUPFAM; SSF103637; CCHHC domain; 7. DR PROSITE; PS51802; ZF_CCHHC; 7. DR Genevisible; Q01538; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Developmental protein; Differentiation; KW DNA-binding; Metal-binding; Neurogenesis; Nucleus; Reference proteome; KW Repeat; 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 //