MYT1_MOUSE
ID MYT1_MOUSE Reviewed; 1127 AA.
AC Q8CFC2; B0R0C3; B0R0C4; O08995; Q8CFH1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Myelin transcription factor 1;
DE Short=MyT1;
DE AltName: Full=Neural zinc finger factor 2;
DE Short=NZF-2;
GN Name=Myt1; Synonyms=Kiaa0835, Nzf2;
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 2), AND FUNCTION.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=12351189; DOI=10.1016/s0925-4773(02)00250-2;
RA Matsushita F., Kameyama T., Marunouchi T.;
RT "NZF-2b is a novel predominant form of mouse NZF-2/MyT1, expressed in
RT differentiated neurons especially at higher levels in newly generated
RT ones.";
RL Mech. Dev. 118:209-213(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal 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 [4]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 [7]
RP PROTEIN SEQUENCE OF 537-543, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [8]
RP STRUCTURE BY NMR OF 837-878, AND DNA-BINDING.
RX PubMed=18073212; DOI=10.1074/jbc.m703772200;
RA Gamsjaeger R., Swanton M.K., Kobus F.J., Lehtomaki E., Lowry J.A.,
RA Kwan A.H., Matthews J.M., Mackay J.P.;
RT "Structural and biophysical analysis of the DNA binding properties of
RT myelin transcription factor 1.";
RL J. Biol. Chem. 283:5158-5167(2008).
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 transcription
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:9373037}.
CC -!- SUBUNIT: Interacts with STEAP3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NZF-2b;
CC IsoId=Q8CFC2-1; Sequence=Displayed;
CC Name=2; Synonyms=NZF-2a;
CC IsoId=Q8CFC2-2; Sequence=VSP_015720;
CC Name=3;
CC IsoId=Q8CFC2-3; Sequence=VSP_015721;
CC -!- TISSUE SPECIFICITY: Isoform 1 is more predominant than isoform 2 at all
CC stages of development and adulthood. Expressed in differentiated
CC neurons especially at higher levels in newly generated ones.
CC {ECO:0000269|PubMed:12351189}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is detected in the earliest born
CC neurons. At 9.5 dpc it is detected in the ventrolateral part of the
CC spinal cord, which later become motor neurons and is also detected in
CC the dispersed cells of the alar plate interneurons. During spinal cord
CC development, the expression is highest in the latest born neurons (the
CC subventricular zone). Detected in the early differentiated neurons
CC within the neuroepithelium and the neural crest cells at 9.5 dpc. At
CC 12.5 dpc, detected in the differentiated neurons within the forebrain,
CC midbrain, and hindbrain. In these neurons, the expression level is
CC highest in the latest born neurons and is also detected in the
CC differentiated neurons of the sensory organs and the peripheral
CC ganglia. {ECO:0000269|PubMed:12351189}.
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=BAC41451.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF004294; AAC53456.1; -; mRNA.
DR EMBL; AB082378; BAC16512.1; -; mRNA.
DR EMBL; AB093267; BAC41451.2; ALT_INIT; mRNA.
DR EMBL; AL845173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063252; AAH63252.1; -; mRNA.
DR CCDS; CCDS17223.1; -. [Q8CFC2-1]
DR CCDS; CCDS50857.1; -. [Q8CFC2-3]
DR PIR; T42712; T42712.
DR RefSeq; NP_001165086.1; NM_001171615.1.
DR RefSeq; NP_001165087.1; NM_001171616.1. [Q8CFC2-3]
DR RefSeq; NP_032691.2; NM_008665.4. [Q8CFC2-1]
DR RefSeq; XP_006500640.2; XM_006500577.3. [Q8CFC2-1]
DR RefSeq; XP_006500642.2; XM_006500579.3. [Q8CFC2-3]
DR PDB; 2JX1; NMR; -; A=843-873.
DR PDB; 2JYD; NMR; -; A=837-878.
DR PDB; 2MF8; NMR; -; A=792-878.
DR PDBsum; 2JX1; -.
DR PDBsum; 2JYD; -.
DR PDBsum; 2MF8; -.
DR AlphaFoldDB; Q8CFC2; -.
DR SMR; Q8CFC2; -.
DR BioGRID; 201678; 1.
DR STRING; 10090.ENSMUSP00000079900; -.
DR iPTMnet; Q8CFC2; -.
DR PhosphoSitePlus; Q8CFC2; -.
DR MaxQB; Q8CFC2; -.
DR PaxDb; Q8CFC2; -.
DR PRIDE; Q8CFC2; -.
DR ProteomicsDB; 287548; -. [Q8CFC2-1]
DR ProteomicsDB; 287549; -. [Q8CFC2-2]
DR ProteomicsDB; 287550; -. [Q8CFC2-3]
DR Antibodypedia; 1424; 304 antibodies from 26 providers.
DR DNASU; 17932; -.
DR Ensembl; ENSMUST00000108756; ENSMUSP00000104387; ENSMUSG00000010505. [Q8CFC2-1]
DR Ensembl; ENSMUST00000108757; ENSMUSP00000104388; ENSMUSG00000010505. [Q8CFC2-3]
DR GeneID; 17932; -.
DR KEGG; mmu:17932; -.
DR UCSC; uc008ons.2; mouse. [Q8CFC2-1]
DR UCSC; uc012cmw.1; mouse. [Q8CFC2-3]
DR CTD; 4661; -.
DR MGI; MGI:1100535; Myt1.
DR VEuPathDB; HostDB:ENSMUSG00000010505; -.
DR eggNOG; KOG3803; Eukaryota.
DR GeneTree; ENSGT00940000156364; -.
DR InParanoid; Q8CFC2; -.
DR OMA; IRLPHMD; -.
DR OrthoDB; 116799at2759; -.
DR BioGRID-ORCS; 17932; 3 hits in 76 CRISPR screens.
DR EvolutionaryTrace; Q8CFC2; -.
DR PRO; PR:Q8CFC2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CFC2; protein.
DR Bgee; ENSMUSG00000010505; Expressed in floor plate of midbrain and 143 other tissues.
DR ExpressionAtlas; Q8CFC2; baseline and differential.
DR Genevisible; Q8CFC2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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; IDA:NTNU_SB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001678; P:cellular glucose homeostasis; IMP:MGI.
DR GO; GO:0060539; P:diaphragm development; IMP:MGI.
DR GO; GO:0031018; P:endocrine pancreas development; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0032350; P:regulation of hormone metabolic process; IMP:MGI.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 3D-structure; Alternative splicing; Developmental protein; Differentiation;
KW Direct protein sequencing; DNA-binding; Metal-binding; Neurogenesis;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1127
FT /note="Myelin transcription factor 1"
FT /id="PRO_0000096677"
FT ZN_FING 21..64
FT /note="CCHHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 435..478
FT /note="CCHHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 479..522
FT /note="CCHHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 793..836
FT /note="CCHHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 837..880
FT /note="CCHHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 886..929
FT /note="CCHHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 939..982
FT /note="CCHHC-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..776
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 56..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..311
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..752
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 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 802
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 807
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 820
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 826
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 846
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 851
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 864
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 870
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 913
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 919
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 948
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 953
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 966
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 972
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT VAR_SEQ 1..152
FT /note="MSSESDDKRARTRSKTLRGPPETTGADLSCPTPGCTGSGHVRGKYSRHRSLQ
FT SCPLAKKRKLEDAETEHLVSKRKSHPLRLALDEGYRMDSDGSEDAEVKDVSVSDESEGP
FT LEEAEAEMSGQEEIHHPQTAEGKSLIKPHFDSNPTSSPSGF -> MMDGIGIRTEKYQS
FT NLAKIDSFLVFESRQKADRMAYSSFPYFLSYSAESGQVGIGGELATVGSRDLETFPHAL
FT FKAPLFLVLCRKKPHQAPFLLQPHKQPFWL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9373037"
FT /id="VSP_015720"
FT VAR_SEQ 508..545
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12465718"
FT /id="VSP_015721"
FT CONFLICT 238
FT /note="P -> R (in Ref. 1; AAC53456)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="T -> A (in Ref. 1; AAC53456)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="N -> Y (in Ref. 1; AAC53456)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="D -> G (in Ref. 1; AAC53456)"
FT /evidence="ECO:0000305"
FT CONFLICT 879
FT /note="K -> R (in Ref. 1; AAC53456)"
FT /evidence="ECO:0000305"
FT CONFLICT 1022
FT /note="E -> G (in Ref. 1; AAC53456)"
FT /evidence="ECO:0000305"
FT CONFLICT 1039
FT /note="K -> R (in Ref. 1; AAC53456)"
FT /evidence="ECO:0000305"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:2MF8"
FT STRAND 813..816
FT /evidence="ECO:0007829|PDB:2MF8"
FT STRAND 821..824
FT /evidence="ECO:0007829|PDB:2MF8"
FT STRAND 853..855
FT /evidence="ECO:0007829|PDB:2JYD"
FT STRAND 857..860
FT /evidence="ECO:0007829|PDB:2JX1"
FT STRAND 865..869
FT /evidence="ECO:0007829|PDB:2JX1"
FT TURN 871..874
FT /evidence="ECO:0007829|PDB:2JYD"
SQ SEQUENCE 1127 AA; 123576 MW; CB46958837E50008 CRC64;
MSSESDDKRA RTRSKTLRGP PETTGADLSC PTPGCTGSGH VRGKYSRHRS LQSCPLAKKR
KLEDAETEHL VSKRKSHPLR LALDEGYRMD SDGSEDAEVK DVSVSDESEG PLEEAEAEMS
GQEEIHHPQT AEGKSLIKPH FDSNPTSSPS GFSKSSYSSY QGIIATSLLN LGQIAEEALV
KEDSVSVAKL SPTVVHQLQD EAAMGVNSDE GEKDLFIQPE DVEEVIEVTS ERSQEPCPQS
LKDMVSEESS KQKGVLGHEE EGEEEEEDEE EEDEEEEEEG EEGEEEEEEE EEEEEEEDEE
EEEEEEEAAP NVIFGEDTSH TSVQKASPEF RGPELSSPKP EYSVIVEVRS DDDKDEDSRS
QKSAVTDESE MYDMMTRGNL GLLEQAIALK AEQVRAVCES GCPPAEQGHL GPGEPGKMAK
PLDVVRKSCY SKDPSRVEKR EIKCPTPGCD GTGHVTGLYP HHRSLSGCPH KDRIPPEILA
MHENVLKCPT PGCTGQGHVN SNRNTHRSLS GCPIAAAEKL AKSHEKQQLQ TGDPPKNNSN
SDRILRPMCF VKQLEVPPYG SYRPNVAPAT PRANLAKELE KFSKVTFDYA SFDAQVFGKR
MLAPKIQTSE TSPKAFQCFD YSHDAEAAHM AATAILNLST RCWEMPENLS TKPQDLPSKA
VDIEVDENGT LDLSMHKHRK RENTFPSSSS CSSSPGVKSP DVSQRQSSTS APSSSMTSPQ
SSQASRQDEW DRPLDYTKPS RLREEEPEES EPAAHSFASS EADDQEVSEE NFEERKYPGE
VTLTNFKLKF LSKDIKKELL TCPTPGCDGS GHITGNYASH RSLSGCPLAD KSLRNLMAAH
SADLKCPTPG CDGSGHITGN YASHRSLSGC PRAKKSGLKV APTKDDKEDP ELMKCPVPGC
VGLGHISGKY ASHRSASGCP LAARRQKEGA LNGSSFSWKS LKNEGPTCPT PGCDGSGHAN
GSFLTHRSLS GCPRATFAGK KGKLSGDEIL SPKFKTSDVL ENDEEIKQLN QEIRDLNESN
SEMEAAMVQL QSQISSMEKN LKNIEEENKL IEEQNEALFL ELSGLSQALI QSLANIRLPH
MEPICEQNFD AYVNTLTDMY SNQDCYQNPE NKGLLETIKQ AVRGIQV
