HNF1B_PIG
ID HNF1B_PIG Reviewed; 559 AA.
AC Q03365;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Hepatocyte nuclear factor 1-beta;
DE Short=HNF-1-beta;
DE Short=HNF-1B;
DE AltName: Full=FPC-binding protein;
DE Short=FPCB;
DE AltName: Full=Transcription factor 2;
DE Short=TCF-2;
GN Name=HNF1B; Synonyms=TCF2;
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], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=8388098; DOI=10.1093/nar/21.8.1845;
RA Menoud P.-A., Matthies R., Hofsteenge J., Nagamine Y.;
RT "Purification and cDNA cloning of a transcription factor which functionally
RT cooperates within a cAMP regulatory unit in the porcine uPA gene.";
RL Nucleic Acids Res. 21:1845-1852(1993).
CC -!- FUNCTION: Transcription factor that binds to the inverted palindrome
CC 5'-GTTAATNATTAAC-3' (PubMed:8388098). Binds to the FPC element in the
CC cAMP regulatory unit of the PLAU gene (PubMed:8388098). Transcriptional
CC activity is increased by coactivator PCBD1 (By similarity).
CC {ECO:0000250|UniProtKB:P35680, ECO:0000269|PubMed:8388098}.
CC -!- SUBUNIT: Binds DNA as a dimer. Can form homodimer or heterodimer with
CC HNF1-alpha (By similarity). Interacts (via HNF-p1 domain) with PCBD1;
CC the interaction increases its transactivation activity (By similarity).
CC {ECO:0000250|UniProtKB:P35680}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the HNF1 homeobox family. {ECO:0000305}.
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DR EMBL; X69675; CAA49356.1; -; mRNA.
DR PIR; S33724; S33724.
DR RefSeq; NP_999121.1; NM_213956.1.
DR AlphaFoldDB; Q03365; -.
DR BMRB; Q03365; -.
DR SMR; Q03365; -.
DR STRING; 9823.ENSSSCP00000028034; -.
DR PaxDb; Q03365; -.
DR GeneID; 397002; -.
DR KEGG; ssc:397002; -.
DR CTD; 6928; -.
DR eggNOG; ENOG502QRPW; Eukaryota.
DR InParanoid; Q03365; -.
DR OrthoDB; 409935at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0031018; P:endocrine pancreas development; ISS:UniProtKB.
DR GO; GO:0048806; P:genitalia development; ISS:UniProtKB.
DR GO; GO:0030073; P:insulin secretion; IEA:InterPro.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0001889; P:liver development; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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; IPR039066; HNF-1.
DR InterPro; IPR006899; HNF-1_N.
DR InterPro; IPR044869; HNF-1_POU.
DR InterPro; IPR023219; HNF1_dimer_N_dom_sf.
DR InterPro; IPR006897; HNF1b_C.
DR InterPro; IPR044866; HNF_P1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR PANTHER; PTHR11568; PTHR11568; 1.
DR Pfam; PF04814; HNF-1_N; 1.
DR Pfam; PF04812; HNF-1B_C; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF100957; SSF100957; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS51937; HNF_P1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS51936; POU_4; 1.
PE 1: Evidence at protein level;
KW Activator; Direct protein sequencing; DNA-binding; Homeobox; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..559
FT /note="Hepatocyte nuclear factor 1-beta"
FT /id="PRO_0000049123"
FT DOMAIN 1..32
FT /note="HNF-p1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01286"
FT DOMAIN 93..188
FT /note="POU-specific atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01285"
FT DNA_BIND 231..312
FT /note="Homeobox; HNF1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..31
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT REGION 328..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27889"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27889"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27889"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27889"
SQ SEQUENCE 559 AA; 61528 MW; 0CF648543ADE2815 CRC64;
MVSKLTSLQQ ELLSALLSSG VTKEVLVQAL EELLPSPSFG VKLETLPLSP GSGTEPDTKP
VFHTLTNGHA KGRLSGDEGS EDGDDYDTPP ILKELQALNT EEAADDGAEV DRMLSEDPWR
AAKMIKGYMQ QHNIPQREVV DVTGLNQSHL SQHLNKGTPM KTQKRAALYT WYVRKQREIL
RQFNQTVQSS GNLTDKSSQD QLLFLFPEFS QQSQGPGQSD DACSEPTNKK MRRNRFKWGP
ASQQILYQAY DRQKNPSKEE REALVEECNR AECLQRGVSP SKAHGLGSNL VTEVRVYNWF
ANRRKEEEAF RQKLAMDAYS SNQTHSLNTL LSHSSPHHQP STSPPNKLPG VRYNQQGNNE
VTSSSTISHH GNSAMVTSQS VLQQVSPASL DPGHNLLSPD GKMQISVSGG GLPPVSTLTN
IHSLSHHNPQ QSQNLIMTPL SGVMAIAQSL NSSQAQSVPV INSVAGSLAA LQPVQFSQQL
HSPHQQPLMQ QSPGSHMAQQ PFMAAVTQLQ NSHMYTHKQE PPQYSHTSRF PPAMVVTDTS
SISTLTNMSS SKQCPLQAW