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DCT1A_XENLA
ID   DCT1A_XENLA             Reviewed;         818 AA.
AC   Q8JJ48;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Dapper 1-A;
DE   AltName: Full=Dapper1b;
DE            Short=XDpr1b;
DE   AltName: Full=Functional regulator of dsh in ontogenesis;
DE            Short=Frodo;
GN   Name=dact1-a;
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], FUNCTION, INTERACTION WITH DVL2, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 810-GLY--VAL-818.
RC   TISSUE=Gastrula;
RX   PubMed=11941372; DOI=10.1038/ncb784;
RA   Gloy J., Hikasa H., Sokol S.Y.;
RT   "Frodo interacts with Dishevelled to transduce Wnt signals.";
RL   Nat. Cell Biol. 4:351-357(2002).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH TCF7L1-A.
RX   PubMed=15329348; DOI=10.1242/dev.01369;
RA   Hikasa H., Sokol S.Y.;
RT   "The involvement of Frodo in TCF-dependent signaling and neural tissue
RT   development.";
RL   Development 131:4725-4734(2004).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH DBF4.
RX   PubMed=15866161; DOI=10.1016/j.devcel.2005.02.012;
RA   Brott B.K., Sokol S.Y.;
RT   "A vertebrate homolog of the cell cycle regulator Dbf4 is an inhibitor of
RT   Wnt signaling required for heart development.";
RL   Dev. Cell 8:703-715(2005).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH CTNND1.
RX   PubMed=17084360; DOI=10.1016/j.devcel.2006.09.022;
RA   Park J.I., Ji H., Jun S., Gu D., Hikasa H., Li L., Sokol S.Y., McCrea P.D.;
RT   "Frodo links Dishevelled to the p120-catenin/Kaiso pathway: distinct
RT   catenin subfamilies promote Wnt signals.";
RL   Dev. Cell 11:683-695(2006).
CC   -!- FUNCTION: Involved in regulation of intracellular signaling pathways
CC       during development. Specifically thought to play a role in canonical
CC       and/or non-canonical Wnt signaling pathways through interaction with
CC       DSH (Dishevelled) family proteins. Binds to dvl2/dsh and impedes the
CC       degradation of beta-catenin (ctnnb1-A and possibly ctnnb1-B), thereby
CC       enhancing the transcriptional activation of target genes of the Wnt
CC       signaling pathway. Also promotes catenin delta/ctnnd1 stability which
CC       in turn promotes zbtb33/kaiso sequestration and thus is involved in the
CC       regulation of zbtb33/kaiso-mediated transcriptional repression. May
CC       also bind to and directly stimulate the transcriptional activity of
CC       tcf7l1-A. Required for eye development and neural patterning.
CC       {ECO:0000269|PubMed:11941372, ECO:0000269|PubMed:15329348,
CC       ECO:0000269|PubMed:15866161, ECO:0000269|PubMed:17084360}.
CC   -!- SUBUNIT: Interacts with dbf4 and tcf7l1-A. Interacts with dvl2/dsh via
CC       the C-terminus. {ECO:0000269|PubMed:11941372,
CC       ECO:0000269|PubMed:15329348, ECO:0000269|PubMed:15866161,
CC       ECO:0000269|PubMed:17084360}.
CC   -!- INTERACTION:
CC       Q8JJ48; Q8AXM9: ctnnd1; NbExp=6; IntAct=EBI-6259065, EBI-6260685;
CC       Q8JJ48; P70062: tcf7l1-a; NbExp=3; IntAct=EBI-6259065, EBI-6259044;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the animal and dorsal marginal regions
CC       at late blastula and early gastrula stages. Expressed predominantly in
CC       the anterior neural plate at neurulation. Expressed mainly in the
CC       ectodermal placodes, including the eye anlagen and the otic vesicle, at
CC       later stages of development. {ECO:0000269|PubMed:11941372}.
CC   -!- DEVELOPMENTAL STAGE: Expressed bpth maternally and zygotically.
CC       {ECO:0000269|PubMed:11941372}.
CC   -!- DOMAIN: The C-terminal PDZ-binding motif may mediate interaction with
CC       the PDZ domains of DSH (Dishevelled) family proteins.
CC   -!- SIMILARITY: Belongs to the dapper family. {ECO:0000305}.
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DR   EMBL; AF393622; AAM33467.1; -; mRNA.
DR   AlphaFoldDB; Q8JJ48; -.
DR   SMR; Q8JJ48; -.
DR   IntAct; Q8JJ48; 2.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0010470; P:regulation of gastrulation; IDA:UniProtKB.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IDA:UniProtKB.
DR   InterPro; IPR024848; Dact1.
DR   InterPro; IPR024843; Dapper.
DR   PANTHER; PTHR15919; PTHR15919; 1.
DR   PANTHER; PTHR15919:SF12; PTHR15919:SF12; 1.
DR   Pfam; PF15268; Dapper; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Developmental protein; Neurogenesis; Nucleus;
KW   Reference proteome; Wnt signaling pathway.
FT   CHAIN           1..818
FT                   /note="Dapper 1-A"
FT                   /id="PRO_0000191355"
FT   REGION          1..337
FT                   /note="Interaction with tcf7l1-A"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          79..130
FT                   /evidence="ECO:0000255"
FT   MOTIF           815..818
FT                   /note="PDZ-binding"
FT   COMPBIAS        14..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         810..818
FT                   /note="Missing: Abrogates binding to dvl2."
FT                   /evidence="ECO:0000269|PubMed:11941372"
SQ   SEQUENCE   818 AA;  90360 MW;  FBBF0F3B193416A6 CRC64;
     MKPIPSPEPP GQLRLTPRRK DKGEAEWERH RTRERLEATL AGLAELDCLR HRQQLLVQNV
     LSPGTHGQDA APTGDSPRSD EQKLLEENIS LLKKQLNCLR KRDAGLLSQL HELDKQINDL
     KIDSEKTEET DSRPSSGFYE LSDGTSGSLS NSSNSVFSEC LSSCHSSTCF CNPLETSLNL
     TDGQAKSAED FLEWLDYRES QHETGTVRCS FSAPHSNSVE VTADVHPKYQ CDLVSKNGND
     VYRYPSPLHA VAVQSPMFLI SVMGNIKAEE PEEEIGPNDN DDCIVPELDH LKDEDSFLHQ
     SSLCSLPLSS GKKMDGYILS IIHKKAHPVR TNKPRTSVNA DPGKGILRHG SICVKQTVGV
     SQSNAVNLKN SKQTCLHSAG MISVDNSTYP SLKPCSKESL SEQLESKRMP SISTYPSCNV
     NELQSQNNSR NTVKSVCQGL ARGSVAMTSN VQKENVTPNA PANLPNASSS VCNGSPREST
     QNSALLPQEI KVVPPVKRVS LKNTLLSYHE SSSFEERPPL DFKSEGSSSQ SLDEGMLVNA
     HYIPAQQHGV KLHKNTKNVK IVKSSTLKHR ADVQYVLENG SQTLKEKSKV VGKKCRFPED
     LDTNKKVKKS TPRVKKIVHP HFEPAAVGRN PVAVRSGIKS HGHPKDVVLA KPKHKRSDYR
     RWKSSAEISY EEALRRARRR VQREMMGVCA QVPFSHASPY AYIASDSEYS AECESLFHST
     VVDTSEDEQS NYTTNCFGDS ESSLSEVEFV GESTTSSDTD ESGGLIWSQF VHTLPMQATA
     TAELQTTAKA FIKIKASHNL KKKILRFRSG SLKLMTTV
 
 
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