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Database: UniProt
Entry: A0A452GK69_9SAUR
LinkDB: A0A452GK69_9SAUR
Original site: A0A452GK69_9SAUR 
ID   A0A452GK69_9SAUR        Unreviewed;       462 AA.
AC   A0A452GK69;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   18-JUN-2025, entry version 30.
DE   RecName: Full=BHLH domain-containing protein {ECO:0000259|PROSITE:PS50888};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000002009.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000002009.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the MiT/TFE family.
CC       {ECO:0000256|ARBA:ARBA00008289}.
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DR   AlphaFoldDB; A0A452GK69; -.
DR   STRING; 38772.ENSGAGP00000002009; -.
DR   Ensembl; ENSGAGT00000002287.1; ENSGAGP00000002009.1; ENSGAGG00000000269.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:TreeGrafter.
DR   GO; GO:0006959; P:humoral immune response; IEA:InterPro.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:InterPro.
DR   CDD; cd18928; bHLHzip_TFE3; 1.
DR   FunFam; 4.10.280.10:FF:000003; microphthalmia-associated transcription factor isoform X1; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR024100; bHLHzip_TFE3.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR021802; MiT/TFE_C.
DR   InterPro; IPR031867; MiT/TFE_N.
DR   PANTHER; PTHR45776; MIP04163P; 1.
DR   PANTHER; PTHR45776:SF3; TRANSCRIPTION FACTOR E3; 1.
DR   Pfam; PF11851; DUF3371; 1.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF15951; MITF_TFEB_C_3_N; 2.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          253..306
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          306..340
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        9..19
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..41
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..154
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..462
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   462 AA;  49352 MW;  04CA5FF127CAA617 CRC64;
     MAGAGFCTSP LMSLTLSVSP SPPAAPLQPP APPAPGDPPG PSMSSSRVLL RQQLMRAQTQ
     EQERREQQQA AQFLPPNSMP PTPAISVSSP LPRPSAQVPV EVLKVRSTPL LHRPHPLFAC
     LLYTSSPQAG SAPEPHSLPP RQQPASGPGS APNSPMAMLH ISSNSEKEID DVIDEIISLE
     SSYNDEMLNY MSVDGGLQLP STLPVAGNLL EIYSSPGLTD PTVPVSNSCP ADLPNIKTEL
     SENEAKALMK ERQKKDNHNL IERRRRFNIN DRIKELGTLI PKSNDPEMRW NKGTILKASV
     DYIRKLQKEQ QRSKEMELRQ RKLEQANRSL QLRVQELEMQ AQLHGLPLTS SAGLLPLGCS
     GEGAKPEGPG PPPFRGGPSC APAPTSSAAC LLDLAFPSEE LGEAGLGFPL GLGVDGGLED
     ILMEDGGPLS PLGASDPLLS SLSPGASKGS SRRSSFSMEE DS
//
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