PO2F1_PIG
ID PO2F1_PIG Reviewed; 745 AA.
AC Q29076;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=POU domain, class 2, transcription factor 1;
DE AltName: Full=NF-A1;
DE AltName: Full=Octamer-binding protein 1;
DE Short=Oct-1;
DE AltName: Full=Octamer-binding transcription factor 1;
DE Short=OTF-1;
GN Name=POU2F1; Synonyms=OTF1;
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=Brain, and Spleen;
RX PubMed=8535082; DOI=10.1007/bf00352381;
RA Tuggle C.K., Schmitz C.B., Wang L., Rothschild M.F.;
RT "Cloning and mapping of porcine OTF1 extends a synteny group conserved on
RT SSC 4 and HSA 1.";
RL Mamm. Genome 6:673-676(1995).
CC -!- FUNCTION: Transcription factor that binds to the octamer motif (5'-
CC ATTTGCAT-3') and activates the promoters of the genes for some small
CC nuclear RNAs (snRNA) and of genes such as those for histone H2B and
CC immunoglobulins. Modulates transcription transactivation by NR3C1, AR
CC and PGR. {ECO:0000250|UniProtKB:P14859}.
CC -!- SUBUNIT: Interacts with POU2AF1; the interaction increases POU2F1
CC transactivation activity. Interacts with NR3C1, AR, PGR and HCFC1.
CC {ECO:0000250|UniProtKB:P14859}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000255|PROSITE-ProRule:PRU00530}.
CC -!- PTM: Phosphorylated by PRKDC. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2
CC subfamily. {ECO:0000305}.
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DR EMBL; L38524; AAA93523.1; -; mRNA.
DR RefSeq; NP_999429.1; NM_214264.1.
DR AlphaFoldDB; Q29076; -.
DR SMR; Q29076; -.
DR STRING; 9823.ENSSSCP00000006729; -.
DR PaxDb; Q29076; -.
DR PRIDE; Q29076; -.
DR GeneID; 397501; -.
DR KEGG; ssc:397501; -.
DR CTD; 5451; -.
DR eggNOG; KOG3802; Eukaryota.
DR InParanoid; Q29076; -.
DR OrthoDB; 873012at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005634; C:nucleus; IC:AgBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IC:AgBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:AgBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR045703; POU2F1_C.
DR InterPro; IPR000327; POU_dom.
DR InterPro; IPR000972; TF_octamer.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR Pfam; PF19536; POU2F1_C; 1.
DR PRINTS; PR00029; OCTAMER.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Homeobox; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..745
FT /note="POU domain, class 2, transcription factor 1"
FT /id="PRO_0000100710"
FT DOMAIN 280..354
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 381..440
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 270
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 276
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
SQ SEQUENCE 745 AA; 76596 MW; 83564E9CC03741BA CRC64;
MNNPSETSKP SMESGDSNTG TQTNGLDFQK QPVPVGGAIS TAQAQAFLGH LHQVQLAGTS
LQAAAQSLNV QSKSNEESGD SQQPSQPSQQ PSVQAAIPQT QLMLAGGQIT GLTLTPAQQQ
LLLQQAQAQA QLLAAAVQQH SASQQHSAAG ATISASAATP MTQIPLSQPI QIAQDLQQLQ
QLQQQNLNLQ QFVLGHPTTN LQPAQFIISQ TPQGQQGLLQ AQNLLTQLPQ QSQANLLQSQ
PSITLTSQPA TPTRTIAATP IQTLPQSQST PKRIDTPSLE EPSDLEELEQ FAKTFKQRRI
KLGFTQGDVG LAMGKLYGND FSQTTISRFE ALNLSFKNMC KLKPLLEKWL NDAENLSSDS
ALCSPSALNS PGLGVEGLNR RRKKRTSIET NIRVALEKSF LENQKPTSEE ITMIADQLNM
EKEVIRVWFC NRRQKEKRIN PPSSGGTSSS PIKAIFPSPT SLVGTTPSLV TSSAATTLTV
NPVLPLTSAA VTNLSVTGTT DTTSNNTATV ISTAPPASSA VTSPSLSPSP SASGSTSEVS
SASETSTTQT TSTPLSSPLG TSQVMVTASG LQTAAAAALQ GAAQLPANAS LAAMAAAAGL
NPGLMAPSQF AAGGALLSLN PGTLGGALSP ALMSNSTLAT IQALASGGSL PITSLDATGN
LVFGNAGGAP NIVTAPLFLN PQNLSLLTSN PVSLVSAAAA SAGNSGPVAS LHATSTSAES
IQNSLFTVAS ASGAASTTTT ASKAQ
