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HNF1B_XENLA
ID   HNF1B_XENLA             Reviewed;         561 AA.
AC   Q91910;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Hepatocyte nuclear factor 1-beta;
DE            Short=HNF-1B;
DE   AltName: Full=LFB3;
DE   AltName: Full=XlFB3;
GN   Name=hnf1b; Synonyms=lfb3, tcf2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=7524626; DOI=10.1016/0925-4773(94)90092-2;
RA   Demartis A., Maffei M., Vignali R., Barsacchi G., de Simone V.;
RT   "Cloning and developmental expression of LFB3/HNF1 beta transcription
RT   factor in Xenopus laevis.";
RL   Mech. Dev. 47:19-28(1994).
CC   -!- FUNCTION: Transcription factor that binds to the inverted palindrome
CC       5'-GTTAATNATTAAC-3'. {ECO:0000250|UniProtKB:P35680}.
CC   -!- SUBUNIT: Binds DNA as a dimer. Can form homodimer or heterodimer with
CC       HNF1-alpha-A or -B. {ECO:0000250|UniProtKB:P35680}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC   -!- TISSUE SPECIFICITY: Expressed at high level in kidney, liver and
CC       intestine. At lower level in lung and testis. Not found in heart,
CC       spleen and muscle.
CC   -!- DEVELOPMENTAL STAGE: Transcription starts at stage 10.5 (mid-gastrula).
CC   -!- SIMILARITY: Belongs to the HNF1 homeobox family. {ECO:0000305}.
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DR   EMBL; X76052; CAA53637.1; -; mRNA.
DR   PIR; I51704; I51704.
DR   AlphaFoldDB; Q91910; -.
DR   SMR; Q91910; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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; IEA:InterPro.
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; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS51936; POU_4; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Homeobox; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..561
FT                   /note="Hepatocyte nuclear factor 1-beta"
FT                   /id="PRO_0000049125"
FT   DOMAIN          1..32
FT                   /note="HNF-p1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01286"
FT   DOMAIN          92..187
FT                   /note="POU-specific atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01285"
FT   DNA_BIND        230..310
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          49..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           228..236
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        321..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  62344 MW;  927FBF7FA4CC51D5 CRC64;
     MVSKLSPLQQ ELLNALLNSG VTKEDLIQAL DDMIPSPSFG VKLENLHMSP EHESDNKPVF
     HTLTNGHHHK GKLSGDEGSE DGDDFDTPPI LKELQSLNTE EAAEQRAEVD RMLSEDPWRA
     AKMIKGYMQQ HNIPQREVVD ITGLNQSHLS QHLNKGTPMK TQKRAALYTW YVRKQREIVI
     QFNQTVQGSG NITGKSSQDQ LLFLFPEFNQ QNPVPGQPDD SCSEPANKKM RRNRFKWGPA
     SQHILYQAYE RQKNPSKEER EALVEECNRA ECIQRGVSPS KAHGLGSNLV TEVRVYNWFA
     NRRKEEAFRQ KLAMDAYSTG PSHPHNLNSL LSHGSPHHTQ PSTSPPSKLQ GMRYNQQGNN
     EVTSSSTISH HGNNAMVHSQ SVLQQVSPVG LDHSHSMLSP DGKLISVSGG GLPPVSTLTN
     IHNLSQSVHH NHQQSQNLIM APISGVMAIT QNLNTSQAQS VPVINSVAGS LAALQSVQFS
     QQLHSPHHQQ IMQQSSGHMA QQPFMATVTQ LQNSHMYAHK HEPPQYSHTS RFPSAMVVTD
     TSSISTLSNM SSSKQCPLQA W
 
 
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