ID A0A1S3GH74_DIPOR Unreviewed; 559 AA.
AC A0A1S3GH74;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=POU domain protein {ECO:0000256|RuleBase:RU361194};
GN Name=Pou2f2 {ECO:0000313|RefSeq:XP_012888156.1};
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_012888156.1};
RN [1] {ECO:0000313|RefSeq:XP_012888156.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012888156.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024760}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2
CC subfamily. {ECO:0000256|ARBA:ARBA00008879}.
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DR RefSeq; XP_012888156.1; XM_013032702.1.
DR AlphaFoldDB; A0A1S3GH74; -.
DR GeneID; 105998093; -.
DR CTD; 5452; -.
DR OrthoDB; 4250502at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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 PANTHER; PTHR11636; POU DOMAIN; 1.
DR PANTHER; PTHR11636:SF46; POU DOMAIN, CLASS 2, TRANSCRIPTION FACTOR 2; 1.
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; Homeodomain-like; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 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 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU361194};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 153..227
FT /note="POU-specific"
FT /evidence="ECO:0000259|PROSITE:PS51179"
FT DOMAIN 253..313
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 255..314
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 57621 MW; 8D521D510ECBA76D CRC64;
MTQLFPSPGG AGSMVHSSMG APEIRMSKPL EAEKEGLDSP SEHTDTERNG PDTNHQNPQN
KASPFAVSPI GPSTKDIQQL LQLQQLVLVP GHHLQPPAQF LLPQAQQSQP GLLPTPNLFQ
LPQQTQGALL TSQPRAGLPT QPPKCLEPPS HPEEPSDLEE LEQFARTFKQ RRIKLGFTQG
DVGLAMGKLY GNDFSQTTIS RFEALNLSFK NMCKLKPLLE KWLNDAETMS VDSSLPSPNQ
LSSPSMGFDG LPGRRRKKRT SIETNVRFAL EKSFLANQKP TSEEILLIAE QLHMEKEVIR
VWFCNRRQKE KRINPCSAAP MLPSPGKPTS YSPHLVTPQG GAGTLPLSQA SSSLSTTVTT
LSSAVGTLHP SRTAGGGGGG GGAAPPLNSI PSVTPPPPAT TTNSTNPSPQ GGHSAIGLSG
LSPSTGSTMV GLSSGLGPAL MSNNPLATIQ ALASGGTLPL TSLDGSGNLV LGAASTAPGS
PGLVTSPLFL NHAGLPLLSA PPGVGLVSAA AAAVAASISS KSPGLSSSSS SSSSSSTCSE
AAAQTPGGPG GPEAGSKPE
//