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Database: UniProt
Entry: L5K135_PTEAL
LinkDB: L5K135_PTEAL
Original site: L5K135_PTEAL 
ID   L5K135_PTEAL            Unreviewed;      1032 AA.
AC   L5K135;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Myelin transcription factor 1 {ECO:0000313|EMBL:ELK04451.1};
GN   ORFNames=PAL_GLEAN10024813 {ECO:0000313|EMBL:ELK04451.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK04451.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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   EMBL; KB031072; ELK04451.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5K135; -.
DR   STRING; 9402.L5K135; -.
DR   eggNOG; KOG3803; Eukaryota.
DR   InParanoid; L5K135; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
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: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: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; 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   Reference proteome {ECO:0000313|Proteomes:UP000010552};
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          470..525
FT                   /note="Myelin transcription factor 1"
FT                   /evidence="ECO:0000259|Pfam:PF08474"
FT   DOMAIN          527..697
FT                   /note="Myelin transcription factor 1"
FT                   /evidence="ECO:0000259|Pfam:PF08474"
FT   REGION          25..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          904..966
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        150..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..239
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..656
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  111129 MW;  676388DF8A7D147B CRC64;
     MLCPVQLGAS LQSCPLAKKR KLDSTEAQHL ASKRKSQPLK LALDEGYSVD SDGSEDAAVK
     DASVSGESEA TLEEDDAEMS GQDEIHRAEP AEGRSPITSR AASGPISSPA GPSRGYQELI
     ATSLLNLGQV AEEALVREDS GQGARRGPGV VHLLRDEPEE GATSDEGDKD IFIQPEEAEE
     VIEVTSERSL EGMSSEESSK PRVTLGDADG AEDEDEDEDE DEDGDADEDE DEDEDAAPGC
     ICEDAAPCAP TPRAPEPASP EPAYSVLVEV RSDDGQDEDS RSQKSAVTDA SEMYDVMTRG
     NLGLLEQAIA LKAEQGQPSP GEPAKGARPL DAPPRTCCGK DSSRAEKREI KCPTPGCDGT
     GHVTGLYPHH RSLSGCPHKD RIPPEILAMH ENVLRCPTPG CTGQGHVNSN RNTHRSLSGC
     PIAAAEKLAK SHEKQQPPTG DPAKSGSSSD RTLRPMCFVK QLEVPPYGSY RPSVAPATPR
     ANLAKELEKF SKVTFDYASF DAQVFGKRML APKMPTSETS PKAFKCFDYT HDAEAAHMAA
     TAILNLSTRC WEMPENLSTK PQEAPRKVVD IEVDENGTLD LSMHKHRRRE GALPGGSSSP
     GVRPPDAPQR RDSGSAPSGS VTSPQPSQAS RQDEWDRPLD YTKPSRQREG EPEESEPAAH
     SFASSEADDQ EALEESFEER RYPGDVTLTS FKLKFLSKDM KKELLTCPTP GCDGSGHITG
     NYASHRSLSG CPLADKSLRN LMAAHSADLK CPTPGCDGSG HITGNYASHR SLSGCPRAKK
     TGAKVTPAKD DKEDPELMKC PVPGCVGLGH ISGKYASHRS ASGCPLAARR QKEGSVNGPS
     FSWKSLKNEG PTCPTPGCDG SGHANGSFLT HRSLSGCPRA TFAGKKGKLS GDEVLSTKFK
     TSDVLDNDEE IKQLNQEIRD LSESNSEMEA AMAQLQSQVS SMERSLRSIE DENRLIEEQN
     EALFLELSGL SQALIRSLAN IRLPHMEPIC EQNFDAYVST LTDMYSNQEC YQDPENKDLL
     ESIKQAVRGI QV
//
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