PDX1_PANTR
ID PDX1_PANTR Reviewed; 283 AA.
AC A2T756;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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; DQ977375; ABM92011.1; -; Genomic_DNA.
DR RefSeq; NP_001074947.1; NM_001081478.1.
DR AlphaFoldDB; A2T756; -.
DR BMRB; A2T756; -.
DR SMR; A2T756; -.
DR STRING; 9598.ENSPTRP00000009769; -.
DR PaxDb; A2T756; -.
DR Ensembl; ENSPTRT00000010560; ENSPTRP00000009769; ENSPTRG00000005736.
DR GeneID; 452507; -.
DR KEGG; ptr:452507; -.
DR CTD; 3651; -.
DR VGNC; VGNC:5093; PDX1.
DR eggNOG; KOG0489; Eukaryota.
DR GeneTree; ENSGT00940000162542; -.
DR HOGENOM; CLU_087401_0_0_1; -.
DR InParanoid; A2T756; -.
DR OMA; HTWKGQW; -.
DR OrthoDB; 1102286at2759; -.
DR TreeFam; TF326223; -.
DR Proteomes; UP000002277; Chromosome 13.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
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:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0031017; P:exocrine pancreas development; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; IEA:Ensembl.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IEA:Ensembl.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1904692; P:positive regulation of type B pancreatic cell proliferation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0097050; P:type B pancreatic cell apoptotic process; IEA:Ensembl.
DR GO; GO:0003309; P:type B pancreatic cell differentiation; IBA:GO_Central.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IEA:Ensembl.
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_0000285454"
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 34..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..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; 30731 MW; 92CCEC7204CDF689 CRC64;
MNGEEQYYAA TQLYKDSCAF QRGPAPEFSA GPPACLYMGR QPPPPPPHPF PGALGALEQG
SPPDISPYEV PPLADDPAVA HLHHHLPAQL ALPHPPAGPF PEGAEPGVLE EPNRVQLPFP
WMKSTKAHAW KGQWAGGAYA AEPEENKRTR TAYTRAQLLE LEKEFLFNKY ISRPRRVELA
VMLNLTERHI KIWFQNRRMK WKKEEDKKRG GGTAVGGGGV AEPEQDCAVT SGEELLALPP
PPPPGGAVPP AAPVAAREGR LPPGLSASPQ PSSVAPRRPQ EPR
