PDX1_PANPA
ID PDX1_PANPA Reviewed; 283 AA.
AC A1YG85;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Pancreas/duodenum homeobox protein 1;
DE AltName: Full=Homeodomain protein PDX1;
DE AltName: Full=Insulin promoter factor 1;
DE Short=IPF-1;
GN Name=PDX1; Synonyms=IPF1;
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT "Positive selection in transcription factor genes on the human lineage.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Activates insulin and somatostatin gene transcription. Key
CC regulator of islet peptide hormone expression but also responsible for
CC the development of the pancreas, most probably by determining
CC maturation and differentiation of common pancreatic precursor cells in
CC the developing gut. As part of a PDX1:PBX1b:MEIS2b complex in
CC pancreatic acinar cells is involved in the transcriptional activation
CC of the ELA1 enhancer; the complex binds to the enhancer B element and
CC cooperates with the transcription factor 1 complex (PTF1) bound to the
CC enhancer A element. Binds the DNA sequence 5'-CC[CT]TAATGGG-3' (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the basic helix-loop-helix domains of TCF3(E47)
CC and NEUROD1 and with HMG-I(Y). Interacts with SPOP. Part of a
CC PDX1:PBX1b:MEIS2b complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC Cytoplasm, cytosol {ECO:0000250}.
CC -!- DOMAIN: The Antp-type hexapeptide mediates heterodimerization with PBX
CC on a regulatory element of the somatostatin promoter. {ECO:0000250}.
CC -!- DOMAIN: The homeodomain, which contains the nuclear localization
CC signal, not only mediates DNA-binding, but also acts as a protein-
CC protein interaction domain for TCF3(E47), NEUROD1 and HMG-I(Y).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by the SAPK2 pathway at high intracellular glucose
CC concentration. Phosphorylated by HIPK2 on Ser-268 upon glucose
CC accumulation. This phosphorylation mediates subnuclear localization
CC shifting. Phosphorylation by PASK may lead to translocation into the
CC cytosol (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Antp homeobox family. IPF1/XlHbox-8
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ977234; ABM54310.1; -; Genomic_DNA.
DR BMRB; A1YG85; -.
DR STRING; 9597.XP_008969888.1; -.
DR eggNOG; KOG0489; Eukaryota.
DR Proteomes; UP000240080; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017995; Homeobox_antennapedia.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR020479; Homeobox_metazoa.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00025; ANTENNAPEDIA.
DR PRINTS; PR00024; HOMEOBOX.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 3: Inferred from homology;
KW Activator; Cytoplasm; DNA-binding; Homeobox; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..283
FT /note="Pancreas/duodenum homeobox protein 1"
FT /id="PRO_0000285453"
FT DNA_BIND 146..205
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 13..73
FT /note="Transactivation domain"
FT /evidence="ECO:0000250"
FT REGION 30..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 118..123
FT /note="Antp-type hexapeptide"
FT MOTIF 197..203
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 37..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphothreonine; by PASK"
FT /evidence="ECO:0000250|UniProtKB:P52946"
FT MOD_RES 268
FT /note="Phosphoserine; by HIPK2"
FT /evidence="ECO:0000250|UniProtKB:P52945"
SQ SEQUENCE 283 AA; 30771 MW; 848E8691F16C7F89 CRC64;
MNGEEQYYAA TQLYKDSCAF QRGPAPEFSA GPPACLYMGR QPPPPPPHPF PGALGALEQG
SPPDISPYEV PPLADDPAVA HLHHHLPAQL ALPHPPAGPF PEGAEPGVLE EPNRVQLPFP
WMKSTKAHXW KGQWAGGAYA AEPEENKRTR TAYTRAQLLE LEKEFLFNKY ISRPRRVELA
VMLNLTERHI KIWFQNRRMK WKKEEDKKRG GGTAVGGGGV AEPEQDCAVT SGEELLALPP
PPPPGGAVPP AAPVAAREGR LPPGLSASPQ PSSVAPRRPQ EPR
