ID   SPI1_PIG                Reviewed;         270 AA.
AC   Q6PKU1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Transcription factor PU.1;
GN   Name=SPI1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bone marrow;
RA   Ramanathan B., Minton J.E., Ross C.R., Blecha F.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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 RUNX1, SPIB, CEBPD and
CC       NONO. Interacts with GFI1; the interaction represses SPI1
CC       transcriptional activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR   EMBL; AY600299; AAT00590.1; -; mRNA.
DR   RefSeq; NP_001001865.1; NM_001001865.1.
DR   AlphaFoldDB; Q6PKU1; -.
DR   SMR; Q6PKU1; -.
DR   STRING; 9823.ENSSSCP00000014065; -.
DR   PaxDb; Q6PKU1; -.
DR   PRIDE; Q6PKU1; -.
DR   GeneID; 414912; -.
DR   KEGG; ssc:414912; -.
DR   CTD; 6688; -.
DR   eggNOG; KOG3805; Eukaryota.
DR   InParanoid; Q6PKU1; -.
DR   OrthoDB; 1272250at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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   RNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..270
FT                   /note="Transcription factor PU.1"
FT                   /id="PRO_0000204134"
FT   DNA_BIND        170..253
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   REGION          124..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17947"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17947"
SQ   SEQUENCE   270 AA;  31093 MW;  5765E56AEB2209CA CRC64;
     MLQACKMEGF PLVPPPSEDL VPYDTDLYQR QTHEYYPYLS SDGESHSDHY WDFHPHHVHS
     EFESFAENHF TELQSVQPPQ LQQLYRHMEL EQMHVLDTPM APTHASLGHQ VSYLPRMCLL
     YPSLSPAQPS SDEEEGERQS PPLEVSDGEA DGLEPGPGLL HGETGSKKKI RLYQFLLDLL
     RSGDMKDSIW WVDKDKGTFQ FSSKHKEALA HRWGIQKGNR KKMTYQKMAR ALRNYGKTGE
     VKKVKKKLTY QFSGEVLGRG ALVVRRHPPH