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PAX8_XENLA
ID   PAX8_XENLA              Reviewed;         465 AA.
AC   Q9PUK5; Q9YH94;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Paired box protein Pax-8;
DE            Short=XPax-8;
GN   Name=pax8 {ECO:0000250|UniProtKB:Q06710};
GN   Synonyms=pax-8 {ECO:0000312|EMBL:AAD52681.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAD52681.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo {ECO:0000269|PubMed:10491256};
RX   PubMed=10491256; DOI=10.1006/dbio.1999.9414;
RA   Carroll T.J., Vize P.D.;
RT   "Synergism between Pax-8 and lim-1 in embryonic kidney development.";
RL   Dev. Biol. 214:46-59(1999).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:CAA09231.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 222-465 (ISOFORMS 1 AND 2), ALTERNATIVE
RP   SPLICING, TISSUE SPECIFICITY, AND INDUCTION.
RC   TISSUE=Kidney {ECO:0000312|EMBL:CAA09231.1};
RX   PubMed=10322629;
RX   DOI=10.1002/(sici)1520-6408(1999)24:3/4<208::aid-dvg4>3.0.co;2-j;
RA   Heller N., Braendli A.W.;
RT   "Xenopus Pax-2/5/8 orthologues: novel insights into Pax gene evolution and
RT   identification of Pax-8 as the earliest marker for otic and pronephric cell
RT   lineages.";
RL   Dev. Genet. 24:208-219(1999).
RN   [3] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=15223346; DOI=10.1016/j.ydbio.2004.04.013;
RA   Schlosser G., Ahrens K.;
RT   "Molecular anatomy of placode development in Xenopus laevis.";
RL   Dev. Biol. 271:439-466(2004).
RN   [4] {ECO:0000305}
RP   INDUCTION.
RX   PubMed=16979153; DOI=10.1016/j.ydbio.2006.06.047;
RA   Cartry J., Nichane M., Ribes V., Colas A., Riou J.-F., Pieler T., Dolle P.,
RA   Bellefroid E.J., Umbhauer M.;
RT   "Retinoic acid signalling is required for specification of pronephric cell
RT   fate.";
RL   Dev. Biol. 299:35-51(2006).
CC   -!- FUNCTION: Probable transcription factor. Involved in kidney
CC       development, acting synergistically with lhx1/lim-1 to establish the
CC       pronephric primordium in late gastrulae/early neurulae.
CC       {ECO:0000269|PubMed:10491256}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06710,
CC       ECO:0000255|PROSITE-ProRule:PRU00381}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:10322629, ECO:0000269|PubMed:10491256};
CC         IsoId=Q9PUK5-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:10322629};
CC         IsoId=Q9PUK5-2; Sequence=VSP_052378;
CC   -!- TISSUE SPECIFICITY: Expression starts at late gastrula stages in cells
CC       fated to become the primordia of the otic system and the pronephric
CC       kidney. Expression is maintained in these two structures through late
CC       tailbud stages. Does not appear to be expressed in the thyroid gland.
CC       {ECO:0000269|PubMed:10322629, ECO:0000269|PubMed:10491256,
CC       ECO:0000269|PubMed:15223346}.
CC   -!- INDUCTION: By retinoic acid in combination with activin.
CC       {ECO:0000269|PubMed:10322629, ECO:0000269|PubMed:16979153}.
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DR   EMBL; AF179301; AAD52681.1; -; mRNA.
DR   EMBL; AJ010504; CAA09231.1; -; mRNA.
DR   RefSeq; NP_001081941.1; NM_001088472.1. [Q9PUK5-1]
DR   AlphaFoldDB; Q9PUK5; -.
DR   SMR; Q9PUK5; -.
DR   GeneID; 398132; -.
DR   KEGG; xla:398132; -.
DR   CTD; 398132; -.
DR   Xenbase; XB-GENE-865008; pax8.L.
DR   OrthoDB; 592933at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IEP:UniProtKB.
DR   GO; GO:1900218; P:negative regulation of apoptotic process involved in metanephric nephron tubule development; ISS:UniProtKB.
DR   GO; GO:1900212; P:negative regulation of mesenchymal cell apoptotic process involved in metanephros development; ISS:UniProtKB.
DR   GO; GO:2000611; P:positive regulation of thyroid hormone generation; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0039003; P:pronephric field specification; IGI:UniProtKB.
DR   GO; GO:0039020; P:pronephric nephron tubule development; IGI:UniProtKB.
DR   GO; GO:0048793; P:pronephros development; ISS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0035565; P:regulation of pronephros size; IGI:UniProtKB.
DR   GO; GO:0007367; P:segment polarity determination; IEA:UniProtKB-KW.
DR   GO; GO:0001655; P:urogenital system development; ISS:UniProtKB.
DR   CDD; cd00131; PAX; 1.
DR   Gene3D; 1.10.10.10; -; 2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR043182; PAIRED_DNA-bd_dom.
DR   InterPro; IPR001523; Paired_dom.
DR   InterPro; IPR022130; Pax2_C.
DR   InterPro; IPR043565; PAX_fam.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR45636; PTHR45636; 1.
DR   Pfam; PF00292; PAX; 1.
DR   Pfam; PF12403; Pax2_C; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Developmental protein; DNA-binding; Nucleus;
KW   Paired box; Reference proteome; Segmentation polarity protein;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..465
FT                   /note="Paired box protein Pax-8"
FT                   /id="PRO_0000284703"
FT   DNA_BIND        26..152
FT                   /note="Paired"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   REGION          29..85
FT                   /note="PAI subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   REGION          104..152
FT                   /note="RED subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   REGION          206..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         316..377
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10322629"
FT                   /id="VSP_052378"
FT   CONFLICT        285
FT                   /note="I -> N (in Ref. 2; CAA09231)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        351
FT                   /note="N -> S (in Ref. 2; CAA09231)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        449
FT                   /note="G -> A (in Ref. 2; CAA09231)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   465 AA;  49573 MW;  5374FF0E307A2D0A CRC64;
     MPNSSIRSEL TTERGFSGPA SNFNIGHGGL NQLGGAFVNG RPLPEVVRQR IVDLAHQGVR
     PCDISRQLRV SHGCVSKILG RYYETGSIRP GVIGGSKPKV ATPKVVEKIG DYKRQNPTMF
     AWEIRDRLLT DGVCDNDTVP SVSSINRIIR TKVQQLFNLP MESCVKSLSP GQTLIPSSTV
     TPPESPHSDS LGSTYSISGL LGITQPSADG KRKLDDSDQE SCRLSIDSQG SVGISRKQLR
     TEAYGHHPLD ALECHFQRQH FPESYSSSTH SKTEQALYTL PLLNISLDDG KSSLTSTNTT
     IGRNLSTHQG YSALSEFTAF SIKQEASDSS SASSTPSSLC SPTFLDLQPI NSGCSAPSFS
     AFSHPSVYGQ FTSHVASGRD VVGATLPGYP PHIPSGQGNY ASSAIAGMVA AGGDYSANAY
     SHGAYAAYGD SWRFPSSSLL GSPYYYSSGT RTAPPPTTAG AYDLM
 
 
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