PIT1_RAT
ID PIT1_RAT Reviewed; 291 AA.
AC P10037; Q63431;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Pituitary-specific positive transcription factor 1;
DE Short=PIT-1;
DE AltName: Full=Growth hormone factor 1;
DE Short=GHF-1;
GN Name=Pou1f1; Synonyms=Ghf-1, Pit-1, Pit1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RX PubMed=2902927; DOI=10.1016/0092-8674(88)90037-2;
RA Bodner M., Castrillo J.-L., Theill L.E., Deerinck T., Ellisman M.,
RA Karin M.;
RT "The pituitary-specific transcription factor GHF-1 is a homeobox-containing
RT protein.";
RL Cell 55:505-518(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RX PubMed=2902928; DOI=10.1016/0092-8674(88)90038-4;
RA Ingraham H.A., Chen R., Mangalam H.J., Elsholtz H.P., Flynn S.E., Lin C.R.,
RA Simmons D.M., Swanson L., Rosenfeld M.G.;
RT "A tissue-specific transcription factor containing a homeodomain specifies
RT a pituitary phenotype.";
RL Cell 55:519-529(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RX PubMed=1600947; DOI=10.1002/j.1460-2075.1992.tb05285.x;
RA Theill L.E., Hattori K., Lazzaro D., Castrillo J.-L., Karin M.;
RT "Differential splicing of the GHF1 primary transcript gives rise to two
RT functionally distinct homeodomain proteins.";
RL EMBO J. 11:2261-2269(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM A).
RX PubMed=1569967; DOI=10.1210/mend.6.2.1569967;
RA Konzak K.E., Moore D.D.;
RT "Functional isoforms of Pit-1 generated by alternative messenger RNA
RT splicing.";
RL Mol. Endocrinol. 6:241-247(1992).
RN [5]
RP ALTERNATIVE SPLICING.
RX PubMed=1561093; DOI=10.1093/nar/20.6.1355;
RA Morris A.E., Kloss B., McChesney R.E., Bancroft C., Chasin L.A.;
RT "An alternatively spliced Pit-1 isoform altered in its ability to trans-
RT activate.";
RL Nucleic Acids Res. 20:1355-1361(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 130-273.
RC STRAIN=Sprague-Dawley; TISSUE=Pituitary;
RX PubMed=9009203; DOI=10.1101/gad.11.2.198;
RA Jacobson E.M., Li P., Leon-Del-Rio A., Rosenfeld M.G., Aggarwal A.K.;
RT "Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected
RT arrangement and flexibility.";
RL Genes Dev. 11:198-212(1997).
CC -!- FUNCTION: Transcription factor involved in the specification of the
CC lactotrope, somatotrope, and thyrotrope phenotypes in the developing
CC anterior pituitary. Activates growth hormone and prolactin genes.
CC Specifically binds to the consensus sequence 5'-TAAAT-3'.
CC {ECO:0000250|UniProtKB:P28069}.
CC -!- SUBUNIT: Interacts with PITX1. Interacts with LHX3. Interacts with
CC ELK1. {ECO:0000250|UniProtKB:P28069}.
CC -!- INTERACTION:
CC P10037; Q99697-3: PITX2; Xeno; NbExp=2; IntAct=EBI-9825525, EBI-1175243;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28069}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=PIT-1B, GHF-1;
CC IsoId=P10037-1; Sequence=Displayed;
CC Name=A; Synonyms=PIT-1A, GHF-2;
CC IsoId=P10037-2; Sequence=VSP_002316;
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:P28069}.
CC -!- MISCELLANEOUS: [Isoform A]: Altered in its ability to trans-activate
CC compared to isoform B. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41851.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA41853.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X65364; CAA46440.1; -; Genomic_DNA.
DR EMBL; X65365; CAA46440.1; JOINED; Genomic_DNA.
DR EMBL; X65367; CAA46440.1; JOINED; Genomic_DNA.
DR EMBL; X65368; CAA46440.1; JOINED; Genomic_DNA.
DR EMBL; L01506; AAA41850.1; -; mRNA.
DR EMBL; L01506; AAA41851.1; ALT_INIT; mRNA.
DR EMBL; L01507; AAA41852.1; -; mRNA.
DR EMBL; L01507; AAA41853.1; ALT_INIT; mRNA.
DR EMBL; S97398; AAC60656.1; -; mRNA.
DR EMBL; M23253; AAA41854.1; -; mRNA.
DR EMBL; X12658; CAA31185.1; -; mRNA.
DR EMBL; X63089; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S22705; S22705.
DR RefSeq; XP_006248036.1; XM_006247974.1. [P10037-2]
DR PDB; 1AU7; X-ray; 2.30 A; A/B=128-273.
DR PDBsum; 1AU7; -.
DR AlphaFoldDB; P10037; -.
DR SMR; P10037; -.
DR BioGRID; 247549; 4.
DR CORUM; P10037; -.
DR IntAct; P10037; 1.
DR STRING; 10116.ENSRNOP00000000905; -.
DR iPTMnet; P10037; -.
DR PhosphoSitePlus; P10037; -.
DR Ensembl; ENSRNOT00000000905; ENSRNOP00000000905; ENSRNOG00000000715. [P10037-2]
DR GeneID; 25517; -.
DR UCSC; RGD:3367; rat. [P10037-1]
DR CTD; 5449; -.
DR RGD; 3367; Pou1f1.
DR VEuPathDB; HostDB:ENSRNOG00000000715; -.
DR eggNOG; KOG3802; Eukaryota.
DR GeneTree; ENSGT00940000158913; -.
DR HOGENOM; CLU_882684_0_0_1; -.
DR InParanoid; P10037; -.
DR OMA; ATYGMMT; -.
DR OrthoDB; 797288at2759; -.
DR PhylomeDB; P10037; -.
DR TreeFam; TF316413; -.
DR EvolutionaryTrace; P10037; -.
DR PRO; PR:P10037; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Genevisible; P10037; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0106222; F:lncRNA binding; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0021984; P:adenohypophysis development; IMP:RGD.
DR GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR GO; GO:0001708; P:cell fate specification; ISO:RGD.
DR GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0021983; P:pituitary gland development; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISO:RGD.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0060133; P:somatotropin secreting cell development; ISO:RGD.
DR GO; GO:0060126; P:somatotropin secreting cell differentiation; ISO:RGD.
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; IPR015586; Pit_1.
DR InterPro; IPR013847; POU.
DR InterPro; IPR000327; POU_dom.
DR PANTHER; PTHR11636:SF84; PTHR11636:SF84; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding; Homeobox;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..291
FT /note="Pituitary-specific positive transcription factor 1"
FT /id="PRO_0000100701"
FT DOMAIN 124..198
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 214..273
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT MOTIF 5..13
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P28069"
FT VAR_SEQ 47
FT /note="T -> TVPSILSLIQTPKCLHTYFSMTTMGNT (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_002316"
FT HELIX 129..146
FT /evidence="ECO:0007829|PDB:1AU7"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:1AU7"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:1AU7"
FT HELIX 180..196
FT /evidence="ECO:0007829|PDB:1AU7"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:1AU7"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:1AU7"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:1AU7"
SQ SEQUENCE 291 AA; 32903 MW; 2651876B2F7668A1 CRC64;
MSCQPFTSAD TFIPLNSDAS AALPLRMHHS AAEGLPASNH ATNVMSTATG LHYSVPSCHY
GNQPSTYGVM AGTLTPCLYK FPDHTLSHGF PPLHQPLLAE DPTASEFKQE LRRKSKLVEE
PIDMDSPEIR ELEQFANEFK VRRIKLGYTQ TNVGEALAAV HGSEFSQTTI CRFENLQLSF
KNACKLKAIL SKWLEEAEQV GALYNEKVGA NERKRKRRTT ISIAAKDALE RHFGEHSKPS
SQEIMRMAEE LNLEKEVVRV WFCNRRQREK RVKTSLNQSL FSISKEHLEC R
