SPI1_RAT
ID SPI1_RAT Reviewed; 271 AA.
AC Q6BDS1; Q5BK69;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Transcription factor PU.1;
GN Name=Spi1; Synonyms=Sfpi1;
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].
RX PubMed=15304324; DOI=10.1016/j.febslet.2004.07.008;
RA Nishiyama C., Masuoka N., Nishiyama M., Ito T., Yamane H., Okumura K.,
RA Ogawa H.;
RT "Evidence against requirement of Ser41 and Ser45 for function of PU.1:
RT molecular cloning of rat PU.1.";
RL FEBS Lett. 572:57-64(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-
CC 3') that can act as a lymphoid-specific enhancer. This protein is a
CC transcriptional activator that may be specifically involved in the
CC differentiation or activation of macrophages or B-cells. Also binds RNA
CC and may modulate pre-mRNA splicing (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a monomer. Interacts with CEBPD and NONO (By
CC similarity). Interacts with RUNX1 and SPIB. Interacts with GFI1; the
CC interaction represses SPI1 transcriptional activity (By similarity).
CC Interacts with CEBPE (By similarity). {ECO:0000250|UniProtKB:P17433,
CC ECO:0000250|UniProtKB:P17947}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; AB154364; BAD35169.1; -; mRNA.
DR EMBL; BC091185; AAH91185.1; -; mRNA.
DR RefSeq; NP_001005892.1; NM_001005892.2.
DR AlphaFoldDB; Q6BDS1; -.
DR SMR; Q6BDS1; -.
DR BioGRID; 265745; 1.
DR IntAct; Q6BDS1; 1.
DR STRING; 10116.ENSRNOP00000016306; -.
DR iPTMnet; Q6BDS1; -.
DR PhosphoSitePlus; Q6BDS1; -.
DR PaxDb; Q6BDS1; -.
DR GeneID; 366126; -.
DR KEGG; rno:366126; -.
DR UCSC; RGD:1359607; rat.
DR CTD; 6688; -.
DR RGD; 1359607; Spi1.
DR VEuPathDB; HostDB:ENSRNOG00000012172; -.
DR eggNOG; KOG3805; Eukaryota.
DR HOGENOM; CLU_066451_0_0_1; -.
DR InParanoid; Q6BDS1; -.
DR OMA; SYLPRMY; -.
DR OrthoDB; 1272250at2759; -.
DR PhylomeDB; Q6BDS1; -.
DR TreeFam; TF352494; -.
DR PRO; PR:Q6BDS1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000012172; Expressed in spleen and 18 other tissues.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; 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; IDA:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; ISO:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0051525; F:NFAT protein binding; ISO:RGD.
DR GO; GO:0140311; F:protein sequestering activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0097677; F:STAT family protein binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0060033; P:anatomical structure regression; ISO:RGD.
DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
DR GO; GO:0002357; P:defense response to tumor cell; ISO:RGD.
DR GO; GO:0098508; P:endothelial to hematopoietic transition; ISO:RGD.
DR GO; GO:0030218; P:erythrocyte differentiation; ISO:RGD.
DR GO; GO:0002316; P:follicular B cell differentiation; ISO:RGD.
DR GO; GO:0002314; P:germinal center B cell differentiation; ISO:RGD.
DR GO; GO:0030851; P:granulocyte differentiation; ISO:RGD.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:RGD.
DR GO; GO:0044027; P:hypermethylation of CpG island; ISO:RGD.
DR GO; GO:0002327; P:immature B cell differentiation; ISO:RGD.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISO:RGD.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD.
DR GO; GO:0030098; P:lymphocyte differentiation; ISO:RGD.
DR GO; GO:0002320; P:lymphoid progenitor cell differentiation; ISO:RGD.
DR GO; GO:0030225; P:macrophage differentiation; ISO:RGD.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; ISO:RGD.
DR GO; GO:0002573; P:myeloid leukocyte differentiation; ISO:RGD.
DR GO; GO:1904178; P:negative regulation of adipose tissue development; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISO:RGD.
DR GO; GO:0090241; P:negative regulation of histone H4 acetylation; ISO:RGD.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; ISO:RGD.
DR GO; GO:0043314; P:negative regulation of neutrophil degranulation; ISO:RGD.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0120186; P:negative regulation of protein localization to chromatin; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0090402; P:oncogene-induced cell senescence; ISO:RGD.
DR GO; GO:1904238; P:pericyte cell differentiation; ISO:RGD.
DR GO; GO:1905036; P:positive regulation of antifungal innate immune response; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1904151; P:positive regulation of microglial cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:2000529; P:positive regulation of myeloid dendritic cell chemotaxis; ISO:RGD.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:RGD.
DR GO; GO:0002572; P:pro-T cell differentiation; ISO:RGD.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0045646; P:regulation of erythrocyte differentiation; ISO:RGD.
DR GO; GO:1901674; P:regulation of histone H3-K27 acetylation; ISO:RGD.
DR GO; GO:1905453; P:regulation of myeloid progenitor cell differentiation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISO:RGD.
DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0001944; P:vasculature development; ISO:RGD.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..271
FT /note="Transcription factor PU.1"
FT /id="PRO_0000204135"
FT DNA_BIND 171..254
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 124..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17947"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17947"
SQ SEQUENCE 271 AA; 31089 MW; CDD9F21BAD449608 CRC64;
MLQACKMEGF PLVAPPSDEL VTYESELYQR QTHDYYSLIG GDGDSHSDHY WDFSTHHVHS
EFESFPENHF TELQSVQPPQ LQQLYRHMEL EQMHVLDTPM APPHASLSHQ VSYMPRVCFP
YPPLSPAHQQ SSDEEEGERQ SPPLEVSDGE ADGLEPGPGL LHGETGSKKK IRLYQFLLDL
LRSGDMKDSI WWVDKDKGTF QFSSKHKEAL AHRWGIQKGN RKKMTYQKMA RALRNYGKTG
EVKKVKKKLT YQFSGEVLGR GGLAERRLPP H
