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Database: UniProt
Entry: A0A3B4HD45_9CICH
LinkDB: A0A3B4HD45_9CICH
Original site: A0A3B4HD45_9CICH 
ID   A0A3B4HD45_9CICH        Unreviewed;       978 AA.
AC   A0A3B4HD45;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Myelin transcription factor 1 {ECO:0000313|Ensembl:ENSPNYP00000031968.1};
GN   Name=MYT1 {ECO:0000313|Ensembl:ENSPNYP00000031968.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000031968.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000031968.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the MYT1 family.
CC       {ECO:0000256|ARBA:ARBA00010194}.
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DR   AlphaFoldDB; A0A3B4HD45; -.
DR   STRING; 303518.ENSPNYP00000031968; -.
DR   Ensembl; ENSPNYT00000032733.1; ENSPNYP00000031968.1; ENSPNYG00000024123.1.
DR   GeneTree; ENSGT00940000156364; -.
DR   Proteomes; UP000261460; Unplaced.
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 DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 4.10.320.30; -; 6.
DR   InterPro; IPR013681; Myelin_TF.
DR   InterPro; IPR002515; Znf_C2H2C.
DR   InterPro; IPR036060; Znf_C2H2C_sf.
DR   PANTHER; PTHR10816:SF15; MYELIN TRANSCRIPTION FACTOR 1-LIKE; 1.
DR   PANTHER; PTHR10816; MYELIN TRANSCRIPTION FACTOR 1-RELATED; 1.
DR   Pfam; PF08474; MYT1; 2.
DR   Pfam; PF01530; zf-C2HC; 6.
DR   SUPFAM; SSF103637; CCHHC domain; 6.
DR   PROSITE; PS51802; ZF_CCHHC; 6.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01143}.
FT   DOMAIN          471..528
FT                   /note="Myelin transcription factor 1"
FT                   /evidence="ECO:0000259|Pfam:PF08474"
FT   DOMAIN          528..637
FT                   /note="Myelin transcription factor 1"
FT                   /evidence="ECO:0000259|Pfam:PF08474"
FT   REGION          46..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          850..919
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        46..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..185
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..299
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..586
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   978 AA;  108112 MW;  53FF54983741E8D9 CRC64;
     MTQKKQSVAM TFICTLNSTA EASQVTKVTA VCPSADLDKH ISAKAENKTV SEKVGEEVKP
     ADDLQQEETE TKDVKDACLM TKNQPSAEPA ELTGIPDLKE TKEAEEAEEQ EENGQQKSPE
     NIVEERVIER QVISQKNSDH QYSSGDYGHL AKESKQHKRE ADEEEVEEEE EEEEEEEEED
     GTDREVLQEV DTPYTLSPRT QGSETEVSLR EEKICTPMTE EEEDEEQEGE REGEDHRQEK
     EDSEILGEEE EDQDSSKASP TTLVIEVRSE EDDDDDDDDE DEEEEEEEEE EEEEGEEQDR
     VSEGSGITDD SENWDMTRGN LGLLEQAIAL KAEEVKEVKC ERVCIEKKKE VKCPTPGCDG
     TGHVTGLYPH HRSLSGCPHK DRIPPEILAM HENVLKCPTP GCTGQGHVNS NRNTHRSLSG
     CPIAAAAKLN KNQDKQVHLQ ASASEPSSNS DRVLRPMCFV KQLEIPQYGS YRPNTVTTTP
     RANLAKELEK YSKVSFDYAS FDGQVFGKRT LIPKTPSTAE TSPKAFKNAE AAHMAATAIL
     NLSTRCWERP ETLSTKTREP CTKADIEVDE NGTLDLSMKK TKREGVQSPE PSSSLSSSSQ
     HVGAIASQGQ TQQEWEGPLD FTKMGGVKEE DHEEVSRDLL TTLICECVLD PRCPTPGCDG
     SGHITGNYAS HRSLSGCPLA DKSLRTLMAA HTAELKCPTP GCDGSGHITG NYASHRSLSG
     CPRAKKSGVK STPTKDDKED SELLRCPVPG CDSLGHISGK YATHRSAYGC PLAARRQKEG
     LLNGTPFSWK AFKTEGPSCP TPGCDGSGHA NGSFLTHRSL SGCPRASANK KRAKFPGDEY
     ITAKFRASDV LDNDEDIKQL NKEINELNES NSEMEADMIN LHTQISSMEK NLKSMEEENK
     QIEERNEALF LELSGLSQAL IRSLANISLP TMEPLSEQNF DSYVDTLTHM FTNKDCYQNP
     ENRALLESIN QAVKGIEV
//
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