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PAX3B_XENLA
ID   PAX3B_XENLA             Reviewed;         483 AA.
AC   Q0IH87; Q5UCU0; Q645N5;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Paired box protein Pax-3-B;
DE            Short=xPax3-B;
DE   AltName: Full=Paired-domain transcription factor Pax3-B;
GN   Name=pax3-b;
GN   Synonyms=pax3 {ECO:0000312|EMBL:AAV31938.1},
GN   pax3B {ECO:0000303|PubMed:15843410};
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:AAV31938.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15843410; DOI=10.1242/dev.01823;
RA   Sato T., Sasai N., Sasai Y.;
RT   "Neural crest determination by co-activation of Pax3 and Zic1 genes in
RT   Xenopus ectoderm.";
RL   Development 132:2355-2363(2005).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAU25939.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Wang E.P., Monsoro-Burq A.-H., Harland R.M.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAU25939.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-268 (ISOFORM 1).
RC   TISSUE=Neurula {ECO:0000312|EMBL:AAI23264.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305}
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=9169853; DOI=10.1242/dev.124.10.2075;
RA   Bang A.G., Papalopulu N., Kintner C., Goulding M.D.;
RT   "Expression of Pax-3 is initiated in the early neural plate by
RT   posteriorizing signals produced by the organizer and by posterior non-axial
RT   mesoderm.";
RL   Development 124:2075-2085(1997).
RN   [5] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=10498689; DOI=10.1242/dev.126.20.4547;
RA   Davidson L.A., Keller R.E.;
RT   "Neural tube closure in Xenopus laevis involves medial migration, directed
RT   protrusive activity, cell intercalation and convergent extension.";
RL   Development 126:4547-4556(1999).
RN   [6] {ECO:0000305}
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=10433827; DOI=10.1006/dbio.1999.9319;
RA   Bang A.G., Papalopulu N., Goulding M.D., Kintner C.;
RT   "Expression of Pax-3 in the lateral neural plate is dependent on a Wnt-
RT   mediated signal from posterior nonaxial mesoderm.";
RL   Dev. Biol. 212:366-380(1999).
RN   [7] {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   [8] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15691759; DOI=10.1016/j.devcel.2004.12.017;
RA   Monsoro-Burq A.-H., Wang E.P., Harland R.M.;
RT   "Msx1 and Pax3 cooperate to mediate FGF8 and WNT signals during Xenopus
RT   neural crest induction.";
RL   Dev. Cell 8:167-178(2005).
RN   [9] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17409353; DOI=10.1091/mbc.e06-11-1047;
RA   Hong C.-S., Saint-Jeannet J.-P.;
RT   "The activity of Pax3 and Zic1 regulates three distinct cell fates at the
RT   neural plate border.";
RL   Mol. Biol. Cell 18:2192-2202(2007).
CC   -!- FUNCTION: Probable transcription factor. Promotes both hatching gland
CC       and neural crest cell fates, two of the cell populations that arise
CC       from the neural plate border. Acts downstream of msx1 to induce the
CC       neural crest, cooperating with zic1 and mediating signals from both the
CC       wnt and fgf8 signaling pathways. Induction of hatching gland cell fate
CC       is independent of zic1. {ECO:0000269|PubMed:15691759,
CC       ECO:0000269|PubMed:15843410, ECO:0000269|PubMed:17409353}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P23760,
CC       ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-
CC       ProRule:PRU00381}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q0IH87-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:15843410};
CC         IsoId=Q0IH87-2; Sequence=VSP_053009;
CC   -!- TISSUE SPECIFICITY: Expressed in the dorsolateral ectoderm during early
CC       and mid-gastrula stages. At late-gastrula and neurula stages, expressed
CC       in the lateral neural plate, becoming progressively refined to the
CC       neural folds during convergence and extension. Expression is also
CC       restricted in the A/P axis, extending into the midbrain but excluded
CC       from the forebrain. {ECO:0000269|PubMed:10433827,
CC       ECO:0000269|PubMed:10498689, ECO:0000269|PubMed:15223346,
CC       ECO:0000269|PubMed:15691759, ECO:0000269|PubMed:15843410,
CC       ECO:0000269|PubMed:17409353, ECO:0000269|PubMed:9169853}.
CC   -!- INDUCTION: By wnt-signaling from the posterior mesoderm.
CC       {ECO:0000269|PubMed:10433827, ECO:0000269|PubMed:9169853}.
CC   -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI23264.1; Type=Miscellaneous discrepancy; Note=May contain intron retention.; Evidence={ECO:0000305};
CC       Sequence=AAU25939.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY757359; AAV31938.1; -; mRNA.
DR   EMBL; AY725268; AAU25939.1; ALT_INIT; mRNA.
DR   EMBL; BC123263; AAI23264.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001088994.1; NM_001095525.1.
DR   AlphaFoldDB; Q0IH87; -.
DR   SMR; Q0IH87; -.
DR   DNASU; 496377; -.
DR   GeneID; 496377; -.
DR   KEGG; xla:496377; -.
DR   CTD; 496377; -.
DR   Xenbase; XB-GENE-6252072; pax3.L.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 496377; Expressed in neurula embryo and 6 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:UniProtKB.
DR   GO; GO:0048785; P:hatching gland development; IMP:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0014034; P:neural crest cell fate commitment; IMP:UniProtKB.
DR   GO; GO:0014029; P:neural crest formation; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IGI:UniProtKB.
DR   CDD; cd00086; homeodomain; 1.
DR   CDD; cd00131; PAX; 1.
DR   Gene3D; 1.10.10.10; -; 2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR043182; PAIRED_DNA-bd_dom.
DR   InterPro; IPR001523; Paired_dom.
DR   InterPro; IPR022106; Pax7_C.
DR   InterPro; IPR043565; PAX_fam.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR45636; PTHR45636; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF00292; PAX; 1.
DR   Pfam; PF12360; Pax7; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Developmental protein; Differentiation; DNA-binding;
KW   Homeobox; Neurogenesis; Nucleus; Paired box; Reference proteome;
KW   Transcription; Transcription regulation; Wnt signaling pathway.
FT   CHAIN           1..483
FT                   /note="Paired box protein Pax-3-B"
FT                   /id="PRO_0000366208"
FT   DNA_BIND        34..160
FT                   /note="Paired"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   DNA_BIND        219..278
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          37..93
FT                   /note="PAI subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   REGION          112..160
FT                   /note="RED subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   REGION          164..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         126..149
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15843410, ECO:0000303|Ref.2"
FT                   /id="VSP_053009"
FT   CONFLICT        107
FT                   /note="K -> KQ (in Ref. 2; AAU25939)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        266..268
FT                   /note="WFS -> ARA (in Ref. 3; AAI23264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        338..341
FT                   /note="SVHQ -> VHQS (in Ref. 1; AAV31938)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   483 AA;  53544 MW;  30FA220FDE77D971 CRC64;
     MTSLAGAVPR MMRPCPGQNY PRTGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV
     EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPKVTT PEVEKKIEEF
     KRDNPGMFSW EIRDKLLKDG VCDRNTVPSV SSISRILRSK FGKGDEEDME LDRKEQEESE
     KRAKHSIDGI LRERAPASPE SEEGSDIDSE PDLPLKRKQR RSRTTFTAEQ LEELERAFER
     THYPDIYTRE ELAQRAKLTE ARVQVWFSNR RARWRKQAGA NQLMAFNHLI PGAFPPTAMP
     ALPTYQLSET SYQPTSIPQA VSDPSNTVHR PQPLPPSSVH QSLPSNPDSS SAYCLPSSRH
     GFSSYTDSFV PPSGPSNPMN PAIGNGLSPQ VMGLLTNHGG VPHQPQTDYA LSPLTGGLEP
     PTAVSASCSQ RLEHMKSLDS LSTSQSYCPP TYSTSGYSME PMTGYQYPQY GQSAFHYLKP
     DIA
 
 
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