ID A0A1S3MBD8_SALSA Unreviewed; 1322 AA.
AC A0A1S3MBD8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Myelin transcription factor 1-like protein isoform X5 {ECO:0000313|RefSeq:XP_014000354.1};
GN Name=LOC106571614 {ECO:0000313|RefSeq:XP_014000354.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014000354.1};
RN [1] {ECO:0000313|RefSeq:XP_014000354.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014000354.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_014000354.1; XM_014144879.1.
DR OrthoDB; 3091993at2759; -.
DR Proteomes; UP000087266; Chromosome ssa15.
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:SF15; MYELIN TRANSCRIPTION FACTOR 1-LIKE; 1.
DR PANTHER; PTHR10816; MYELIN TRANSCRIPTION FACTOR 1-RELATED; 1.
DR Pfam; PF08474; MYT1; 1.
DR Pfam; PF01530; zf-C2HC; 6.
DR SUPFAM; SSF103637; CCHHC domain; 6.
DR PROSITE; PS50890; PUA; 1.
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:UP000087266};
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 741..1003
FT /note="Myelin transcription factor 1"
FT /evidence="ECO:0000259|Pfam:PF08474"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1201..1263
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 98..167
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..227
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..456
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 145839 MW; F0806EC9F32221B2 CRC64;
MEVDAVEKRH RTRSKGVRVP VETAAQELFS CPTPGCDGSG HVSGKYARHR SVYGCPLAKK
RKTQEKQPLE PSPKRRPYLT PTDPEVNPAA IFPCYEPEPM DEGEEKEQGE VDGEIQEEGE
EEEGEEGEEV EEIEEEGFSE DNGELGEEEE EGEEADEEEE EVEMEVVGPV EVEQVEEGIE
EDEEADDGDD EEQEEGEEQE EEELEDEGDE DEHEEEEEEE EEEEEVQSHH EPENRHKNGG
QSKHHPTGQK DNINNSAPGP NVGPNGEEYE NYDELVAKSL LNLGKIAEDA AYQAMTESEM
NSNSSNSAGE DDDDDDEDEE GNERGGGRKG KLSVDLDSDV VRETVDSLKL LAQGHGAVLP
DDGYPEGTGL EDGRHPNGRP HHHGVRGQAE ESEEEVCLSS LECLRNQCFD LARKLSETSP
SDRLGHPGLQ HHQAHQNHHP NQSHHHLQHQ TGHHHHQAQH QPPAQAHHLP RYESCQEGQQ
PDERGSLERS YSDMVNLMKL EEQLSPASRG GYSASCHQDG DEDTTSVASD RSDEAFDMTK
GNLSLLEKAI AMESERAKVM RDRMASEGHH MVARRDNHHH HHHGEHSPRQ SSGAEERKSR
MHHDGSKRAY YPKDSARGDK KESKCPTPGC DGTGHVTGLY PHHRSLSGCP HKDRVPPEIL
AMYENVLKCP TPGCSGRGHV NSNRNSHRSL SGCPIAAAEK MVKVQEKHIP CDGGPKSNQA
SDRVLRPMCF VKQLEIPQYG YKNNVSTSTP RSNLAKELEK YSKTSFDYGQ GYDSQQHIYG
GGKRGLVPKP QGRDFSSKGY DAKRYCKSPA SSTTSSYAPS SSSLSCGGGG GGSSASSTCS
KSSFDYTHDM EAAHMAATAI LNLSTRCREM PHGLGGKPQD LLSQSPDGDV DDNSTLDLSV
SRGQPGGPEG SGTVLTPLQP MSPQRQALLN SSRCYQMSEA DCWDLPVDYT KIKRITDDDH
KESSFFSSLH QVDDLDPFQD LLDEQHYGGD VTMPSPKHKY SACKEGKKEL ITLSNCQLAD
KSIRSMMTTN AQDLKCPTPA CDGSGHITGN YASHRRPFPS SLSGCPRAKK SGIKILHSKE
DKDDQEPIRC PVPGCDGQGH VTGKYASHRS ASGCPLAAKR QKDGYVNGSQ FAWKSGKTDG
MSCPTPGCDG SGHVSGSFLT HRSLSGCPRA TSAMKKARMT GVEMLTIKQR ASKGIENDED
IKQLDTEIKD LNESNNQVES DMIKLRTQIT TMETNLKSIE EENKVIEQQN DSLLHELANL
SQSLINSLAN IQLPHMEPMN EQNFDSYVNT LTDMYTHQDQ YQSPENKALL ENIKQAVQGI
QV
//
