MYT1_XENLA
ID MYT1_XENLA Reviewed; 1122 AA.
AC P70047;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Myelin transcription factor 1;
DE Short=X-MyT1;
GN Name=myt1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=8980226; DOI=10.1016/s0092-8674(00)81815-2;
RA Bellefroid E.J., Bourguignon C., Hollemann T., Ma Q., Anderson D.J.,
RA Kintner C., Pieler T.;
RT "X-MyT1, a Xenopus C2HC-type zinc finger protein with a regulatory function
RT in neuronal differentiation.";
RL Cell 87:1191-1202(1996).
CC -!- FUNCTION: Transcriptional activator which is essential for neuronal
CC differentiation. Can promote ectotopic neuronal differentiation and
CC confers insensitivity to lateral inhibition, but only in cooperation
CC with bHLH transcription factors. {ECO:0000269|PubMed:8980226}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: First expressed at mid-late gastrulation within
CC the dorsal ectoderm. By the completion of gastrulation its expression
CC is clearly restricted to 3 groups of cells arranged in a radially
CC symmetrical pattern on either side of the dorsal midline of the
CC posterior neural plate, where the ventral, intermediate and dorsal
CC groups of cells differentiate into motor neurons, interneurons and
CC sensory neurons respectively. The same pattern of expression is
CC maintained in later-stage neurula embryos.
CC {ECO:0000269|PubMed:8980226}.
CC -!- INDUCTION: Positively regulated by X-NGNR-1 and negatively regulated by
CC lateral inhibition. {ECO:0000269|PubMed:8980226}.
CC -!- SIMILARITY: Belongs to the MYT1 family. {ECO:0000305}.
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DR EMBL; U67078; AAB40719.1; -; mRNA.
DR RefSeq; NP_001081661.1; NM_001088192.1.
DR AlphaFoldDB; P70047; -.
DR SMR; P70047; -.
DR GeneID; 397982; -.
DR KEGG; xla:397982; -.
DR CTD; 397982; -.
DR Xenbase; XB-GENE-1009978; myt1.S.
DR OrthoDB; 116799at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 397982; Expressed in neurula embryo and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 transcription, DNA-templated; IEA:InterPro.
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 Activator; Developmental protein; Differentiation; DNA-binding;
KW Metal-binding; Neurogenesis; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1122
FT /note="Myelin transcription factor 1"
FT /id="PRO_0000096678"
FT ZN_FING 394..437
FT /note="CCHHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 438..481
FT /note="CCHHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 788..831
FT /note="CCHHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 832..875
FT /note="CCHHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 881..924
FT /note="CCHHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 934..977
FT /note="CCHHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..275
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 797
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="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 815
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 821
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 841
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="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 859
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 865
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 890
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="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 908
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 914
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 943
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="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 961
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 967
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
SQ SEQUENCE 1122 AA; 123862 MW; 70DDA905FF5E8B93 CRC64;
MNVDNVNKGT HTRSKASRVI PSDLIEQEVS LESCPLSRKR KLQESEQENP LSKRKSHPLK
LALDEGFNVD SNGSEETEMK ERDSGTEESE ATLEEIEEDS EPTKPKEAPS PQTAEAESSD
KVEPEETETK TESSPPAKAT YSSYHEIIAN SLLNLGQVAK EALVSEGHLK ESELNNEKPT
SVKSGQAEIE QLMVEEACEK EIIIQTEDAE EVIEVTSEPI SESGTEPRDE VNCEDTEKLQ
KDMIDEEEEE EDDDVDEEDD DDLEEDEEEE EEHSSEMANQ DLPHASQDSP KPHCEGHFSP
KPEYSVIVEV RSDDDKDDDS HSQKSAVTDE SEMYDMMTRG NLGLLEQAIA LKAEQVKVVR
EPSRSSLDNM KNFSADEKQN RPIDTMRKSF YDAGRPEKRD IKCPTPGCDG TGHVTGLYPH
HRSLSGCPHK DRIPPEILAM HENVLKCPTP GCTGQGHVNS NRNTHRSLSG CPIAAAEKLT
RSHEKQQQPG DLSKSSSNSD RILRPMCFVK QLEIPQYGSY RPNMAPATPR ANLAKELEKY
SKVTFDYASF DAQVFGKRLL APKIPSSETS PKAFKSKPFP KASSPCHSPS SSYIKSTSSS
SSSGFDYTHD AEAAHMAATA ILNLSTRCWE MPENLSTKQQ DTPSKSSEIE VDENGTLDLS
MNKHRKREST FPSSSSCSSS PSMKSPDQSQ RQNCTSATSS NMTSPHSSQT SRQDDWDGPI
DYTKPNRQRE EEPEEMEPAA ASFASSEVDE QEMQEMQEMQ EMQEESYEDR KYPGDVTLTN
FKLKFLSKDS KKELLSCPTP GCDGSGHITG NYASHRSLSG CPLADKSLRN LMAAHSADLK
CPTPGCDGSG HITGNYASHR SLSGCPRAKK SGLKITPTKD DKDDPDLMKC PVPGCDGLGH
ISGKYASHRS ASGCPLAARR QKEGALNGSA FSWKSLKTEG PSCPTPGCDG SGHANGSFLT
HRSLSGCPRA SFAGKKGKIS GDELLGTNFK TSDVLENDEE IKQLNKEINE LNESNSEMEA
DMVNLQSQIT TMEKNLKNIE EENKVIEEQN EALFVELSGL SQALIRSLTN IRLPQMEPIS
EQNFDAYVNT LTDMYTNQEC YQNPENKALL ESIKQAVKGI KV
