ID   DMRT3_TAKRU             Reviewed;         468 AA.
AC   Q90WM5; Q4AE30;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Doublesex- and mab-3-related transcription factor 3;
GN   Name=dmrt3;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11543627; DOI=10.1006/geno.2001.6615;
RA   Brunner B., Hornung U., Shan Z., Nanda I., Kondo M., Zend-Ajusch E.,
RA   Haaf T., Ropers H.-H., Shima A., Schmid M., Kalscheuer V.M., Schartl M.;
RT   "Genomic organization and expression of the doublesex-related gene cluster
RT   in vertebrates and detection of putative regulatory regions for DMRT1.";
RL   Genomics 77:8-17(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Yamaguchi A.;
RT   "Expression of the DMRT gene and its roles in early gonadal development of
RT   the Japanese pufferfish Takifugu rubripes.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable transcription factor that plays a role in
CC       configuring the spinal circuits controlling motion in vertebrates.
CC       Involved in neuronal specification within specific subdivision of
CC       spinal cord neurons and in the development of a coordinated locomotor
CC       network controlling movements. May regulate transcription (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}.
CC   -!- SIMILARITY: Belongs to the DMRT family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ295039; CAC42779.1; -; Genomic_DNA.
DR   EMBL; AB201463; BAE16954.1; -; mRNA.
DR   RefSeq; NP_001033034.1; NM_001037945.1.
DR   AlphaFoldDB; Q90WM5; -.
DR   SMR; Q90WM5; -.
DR   STRING; 31033.ENSTRUP00000040103; -.
DR   GeneID; 654277; -.
DR   KEGG; tru:654277; -.
DR   CTD; 450035; -.
DR   eggNOG; KOG3815; Eukaryota.
DR   InParanoid; Q90WM5; -.
DR   OrthoDB; 897429at2759; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 4.10.1040.10; -; 1.
DR   InterPro; IPR001275; DM_DNA-bd.
DR   InterPro; IPR036407; DM_DNA-bd_sf.
DR   InterPro; IPR005173; DMA.
DR   InterPro; IPR026607; DMRT.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR12322; PTHR12322; 1.
DR   Pfam; PF00751; DM; 1.
DR   Pfam; PF03474; DMA; 1.
DR   SMART; SM00301; DM; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF82927; SSF82927; 1.
DR   PROSITE; PS40000; DM_1; 1.
DR   PROSITE; PS50809; DM_2; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..468
FT                   /note="Doublesex- and mab-3-related transcription factor 3"
FT                   /id="PRO_0000277796"
FT   DOMAIN          234..269
FT                   /note="DMA"
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        28..75
FT                   /note="DM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00070"
FT   REGION          96..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        15
FT                   /note="V -> G (in Ref. 2; BAE16954)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="P -> S (in Ref. 2; BAE16954)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        362..363
FT                   /note="ML -> IV (in Ref. 1; CAC42779)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393..394
FT                   /note="QL -> HV (in Ref. 1; CAC42779)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408
FT                   /note="R -> A (in Ref. 2; BAE16954)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   468 AA;  50953 MW;  2EC9E7188C0727C5 CRC64;
     MNGYGSPYLY MGAPVSQPRA PLQRTPKCAR CRNHGVLSWL KGHKRYCRFK DCTCEKCILI
     IERQRVMAAQ VALRRQQANE SLESLIPESL RVLPGIGMTA GGEGNQAAPP RTEELELRWS
     SPEPQAAPPT CAEATEDTEE VSGGENGGSS SDREQDVSSP EGSKPNSCYT PEPPETPSHP
     EEARYSLPKA DNSEKQPKAE SPPRKYPVSP AEQSVLIEGL GGSINLPFSL RANRPPLEVL
     KKIFPAHKPP VLELILRGCG GDLVGAIEVL LSSRSADGSA HPHADPHPDT LVVPSNGHLF
     EHTLASYHPV SSSAKWSVGS AFRVPETLRF SSDSSAGVVS STPLGVPMQH SPFPQHTRYP
     LMLRNSLTRS QASPFVHNDV TLWNTMALQQ QYQLRSAAQY VSPFSPARSG GTVFRSSPIL
     SPRPPEEQRV SLQEESCTLG PKPGLYSPEE EYEERSDSAD SRIINASS