ID A0A1S3ENQ4_DIPOR Unreviewed; 526 AA.
AC A0A1S3ENQ4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Microphthalmia-associated transcription factor isoform X1 {ECO:0000313|RefSeq:XP_012866001.1};
GN Name=Mitf {ECO:0000313|RefSeq:XP_012866001.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012866001.1};
RN [1] {ECO:0000313|RefSeq:XP_012866001.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012866001.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MiT/TFE family.
CC {ECO:0000256|ARBA:ARBA00008289}.
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DR RefSeq; XP_012866001.1; XM_013010547.1.
DR AlphaFoldDB; A0A1S3ENQ4; -.
DR STRING; 10020.ENSDORP00000003119; -.
DR GeneID; 105981384; -.
DR KEGG; dord:105981384; -.
DR CTD; 4286; -.
DR InParanoid; A0A1S3ENQ4; -.
DR OMA; GIPMANT; -.
DR OrthoDB; 3061893at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0070888; F:E-box binding; IEA:Ensembl.
DR GO; GO:0046983; F:protein dimerization activity; IEA:Ensembl.
DR GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
DR GO; GO:1902362; P:melanocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription initiation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
DR CDD; cd18926; bHLHzip_MITF; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR021802; MiT/TFE_C.
DR InterPro; IPR031867; MiT/TFE_N.
DR PANTHER; PTHR45776:SF4; MICROPHTHALMIA-ASSOCIATED TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR45776; MIP04163P; 1.
DR Pfam; PF11851; DUF3371; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF15951; MITF_TFEB_C_3_N; 1.
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 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:UP000081671};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 311..364
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..88
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 357..398
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 58720 MW; AC382BDF8BB249FA CRC64;
MQSESGIVPD FEVGEEFHEE PKTYYELKSQ PLKSSSSAEH PGASKPPISS SSMTSRILLR
QQLMREQMQE QERREQQQKL QAAQFMQQRV PVSQTPAINV SVPTTLPSAP QVPMEVLKVQ
THLENPTKYH IQQAQRQQVK QYLSTTLAHK HANQVLSLPC PNQPGDHVTP PVPGSSAPNS
PMAMLTLNSN CEKEGFYKFE EQNRAESECP SMNTHSRASC MQMDDVIDDI ISLESSYNEE
ILGLMDPALQ MANTLPVSGN LMDLYSNQGL PPPGLTISNS CPANLPNIKR ELTACIFPTE
SEARALAKER QKKDNHNLIE RRRRFNINDR IKELGTLIPK SNDPDMRWNK GTILKASVDY
IRKLQREQQR AKELENRQKK LEHANRHLLL RIQELEMQAR AHGLSLIPST GLCSPDLVNR
IIKQEPVLEN CSQDLLQHQA ELTCTTTLDL TDGTITFNSS LGTGPDSNPA YSVPTKMGSK
LEDILMDDTL SPVGVTDPLL SSVSPGASKA SSRRSSMSME ETEHAC
//
