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DLX5_RAT
ID   DLX5_RAT                Reviewed;         289 AA.
AC   P50575;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 145.
DE   RecName: Full=Homeobox protein DLX-5;
DE   AltName: Full=Homeobox protein DLX-3;
DE   AltName: Full=RDLX;
GN   Name=Dlx5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7915995; DOI=10.1016/0014-5793(94)00896-5;
RA   Shirasawa T., Sakamoto K., Takahashi H.;
RT   "Molecular cloning and evolutional analysis of a mammalian homologue of the
RT   Distal-less 3 (Dlx-3) homeobox gene.";
RL   FEBS Lett. 351:380-384(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Cartilage;
RX   PubMed=7913069; DOI=10.1006/dbio.1994.1178;
RA   Zhao G.-Q., Zhao S., Zhou X., Eberspaecher H., Solursh M.,
RA   de Crombrugghe B.;
RT   "rDlx, a novel distal-less-like homeoprotein is expressed in developing
RT   cartilages and discrete neuronal tissues.";
RL   Dev. Biol. 164:37-51(1994).
CC   -!- FUNCTION: Transcriptional factor involved in bone development. Acts as
CC       an immediate early BMP-responsive transcriptional activator essential
CC       for osteoblast differentiation. Stimulates ALPL promoter activity in a
CC       RUNX2-independent manner during osteoblast differentiation. Stimulates
CC       SP7 promoter activity during osteoblast differentiation. Promotes cell
CC       proliferation by up-regulating MYC promoter activity. Involved as a
CC       positive regulator of both chondrogenesis and chondrocyte hypertrophy
CC       in the endochondral skeleton. Binds to the homeodomain-response element
CC       of the ALPL and SP7 promoter. Binds to the MYC promoter. Requires the
CC       5'-TAATTA-3' consensus sequence for DNA-binding (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with XRCC6 (Ku70). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in several neuronal tissues and
CC       developing tissues.
CC   -!- DEVELOPMENTAL STAGE: Present at high levels in embryos on embryonic day
CC       14 (E14), in skeletal tissues on E18, and in adult brain. At lower
CC       levels in newborn rib cartilage, embryo soft tissues on E18, newborn
CC       skin and adult heart.
CC   -!- PTM: Phosphorylated. Phosphorylation of Ser-34 and Ser-217 by MAPK14
CC       enhances its transcriptional activity. Phosphorylation by CaMK2
CC       increases its protein stability (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the distal-less homeobox family. {ECO:0000305}.
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DR   EMBL; D31734; BAA06534.1; -; mRNA.
DR   EMBL; L24443; AAA42026.1; -; mRNA.
DR   PIR; I53082; I53082.
DR   PIR; S48664; S48664.
DR   RefSeq; NP_037075.1; NM_012943.1.
DR   AlphaFoldDB; P50575; -.
DR   BMRB; P50575; -.
DR   SMR; P50575; -.
DR   PaxDb; P50575; -.
DR   GeneID; 25431; -.
DR   KEGG; rno:25431; -.
DR   UCSC; RGD:2506; rat.
DR   CTD; 1749; -.
DR   RGD; 2506; Dlx5.
DR   eggNOG; KOG0850; Eukaryota.
DR   InParanoid; P50575; -.
DR   OrthoDB; 1416398at2759; -.
DR   PhylomeDB; P50575; -.
DR   TreeFam; TF350606; -.
DR   PRO; PR:P50575; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0071837; F:HMG box domain binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; ISO:RGD.
DR   GO; GO:0007411; P:axon guidance; ISO:RGD.
DR   GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR   GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR   GO; GO:0060349; P:bone morphogenesis; ISO:RGD.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0071773; P:cellular response to BMP stimulus; ISO:RGD.
DR   GO; GO:0043583; P:ear development; ISO:RGD.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR   GO; GO:0001958; P:endochondral ossification; ISS:UniProtKB.
DR   GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR   GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR   GO; GO:0060322; P:head development; ISO:RGD.
DR   GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR   GO; GO:0097376; P:interneuron axon guidance; ISO:RGD.
DR   GO; GO:0021889; P:olfactory bulb interneuron differentiation; ISO:RGD.
DR   GO; GO:0060166; P:olfactory pit development; ISO:RGD.
DR   GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR022135; Distal-less_N.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR020479; Homeobox_metazoa.
DR   InterPro; IPR000047; HTH_motif.
DR   Pfam; PF12413; DLL_N; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   PRINTS; PR00031; HTHREPRESSR.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; Developmental protein; DNA-binding; Homeobox; Nucleus;
KW   Osteogenesis; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..289
FT                   /note="Homeobox protein DLX-5"
FT                   /id="PRO_0000049033"
FT   DNA_BIND        137..196
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         34
FT                   /note="Phosphoserine; by MAPK14; in vitro"
FT                   /evidence="ECO:0000250|UniProtKB:P70396"
FT   MOD_RES         217
FT                   /note="Phosphoserine; by MAPK14; in vitro"
FT                   /evidence="ECO:0000250|UniProtKB:P70396"
FT   CONFLICT        67
FT                   /note="G -> R (in Ref. 2; AAA42026)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242
FT                   /note="P -> T (in Ref. 2; AAA42026)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   289 AA;  31426 MW;  A1B41BB44FD15DA2 CRC64;
     MTGVFDRRVP SIRSGDFQAP FPTSAAMHHP SQESPTLPES SATDSDYYSP AGAAPHGYCS
     PTSASYGKAL NPYQYQYHSV NGSAAGYPAK AYADYGYASP YHQYGGAYNR VPSATSQPEK
     EVAEPEVRMV NGKPKKVRKP RTIYSSFQLA ALQRRFQKTQ YLALPERAEL AASLGLTQTQ
     VKIWFQNKRS KIKKIMKNGE MPPEHSPSSS DPMACNSPQS PAVWEPQGSS RSLSHHPHAH
     PPTSNQSPAS SYLENSASWY PSAASSINSH LPPPGSLQHP LALASGTLY
 
 
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