DAPLE_XENLA
ID DAPLE_XENLA Reviewed; 2058 AA.
AC P85120;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Protein Daple {ECO:0000303|PubMed:30948426};
DE Short=xDaple {ECO:0000303|PubMed:30948426};
DE AltName: Full=Coiled-coil domain-containing protein 88C;
DE AltName: Full=Dvl-associating protein with a high frequency of leucine residues-like;
DE Short=xDal;
GN Name=ccdc88c; Synonyms=dal;
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}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DVL2, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:16026968};
RX PubMed=16026968; DOI=10.1016/j.mod.2005.05.003;
RA Kobayashi H., Michiue T., Yukita A., Danno H., Sakurai K., Fukui A.,
RA Kikuchi A., Asashima M.;
RT "Novel Daple-like protein positively regulates both the Wnt/beta-catenin
RT pathway and the Wnt/JNK pathway in Xenopus.";
RL Mech. Dev. 122:1138-1153(2005).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, GBA MOTIFS, AND MUTAGENESIS OF PHE-1662;
RP PHE-1689 AND 2055-TYR--VAL-2058.
RX PubMed=30948426; DOI=10.1083/jcb.201811174;
RA Marivin A., Morozova V., Walawalkar I., Leyme A., Kretov D.A.,
RA Cifuentes D., Dominguez I., Garcia-Marcos M.;
RT "GPCR-independent activation of G proteins promotes apical cell
RT constriction in vivo.";
RL J. Cell Biol. 218:1743-1763(2019).
CC -!- FUNCTION: Positive regulator of Wnt signaling, acting synergistically
CC with dvl2/dsh (PubMed:16026968). Functions upstream of ctnnb1/beta-
CC catenin in the canonical Wnt pathway, and also activates jnk in the
CC Wnt/planar cell polarity (PCP) pathway (PubMed:16026968). Acts as a
CC non-receptor guanine nucleotide exchange factor which binds to and
CC activates guanine nucleotide-binding protein G(i) alpha subunits
CC (PubMed:30948426). This promotes apical cell constriction and
CC subsequent bending of the neural plate during neurulation via arhgef18
CC (PubMed:30948426). {ECO:0000269|PubMed:16026968,
CC ECO:0000269|PubMed:30948426}.
CC -!- SUBUNIT: Interacts with dvl2/dsh via the PDZ-binding motif.
CC {ECO:0000269|PubMed:16026968}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9P219}. Cell
CC junction {ECO:0000269|PubMed:30948426}. Note=Enriched at apical cell
CC junctions. {ECO:0000269|PubMed:30948426}.
CC -!- TISSUE SPECIFICITY: Expressed weakly in gastrulae, with slightly
CC stronger expression in the dorsal region. In neurulae, expressed in the
CC neural plate with strong expression in the presumptive mesencephalic
CC region. At the tailbud stage, expressed in somatic cells and in part of
CC the tail. Also strongly expressed in regions of the head including eye
CC vesicles, otic vesicles, olfactory placode and the pharyngeal cavity.
CC {ECO:0000269|PubMed:16026968}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all developmental stages, with a
CC gradual increase in expression from the 2-day tadpole stage onward.
CC {ECO:0000269|PubMed:16026968}.
CC -!- DOMAIN: The GBA (G-alpha binding and activating) motif mediates binding
CC to the alpha subunits of guanine nucleotide-binding proteins (G
CC proteins) (PubMed:30948426). Both motifs are required for binding and
CC activation of alpha subunits (PubMed:30948426).
CC {ECO:0000269|PubMed:30948426}.
CC -!- DOMAIN: The PDZ domain is required for localization to apical
CC junctions. {ECO:0000269|PubMed:30948426}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown does not affect embryo
CC morphology up to gastrulation but causes a delay in the closure of the
CC neural tube (PubMed:30948426). After the neural tube closes, embryos
CC display mild axis curvature and head defects at later stages and
CC malformations are also evident in the embryonic brain which forms a
CC closed structure but displays an enlargement of the ventricles
CC (PubMed:30948426). Embryos show impaired apical constriction of
CC neuroepithelial cells during neurulation (PubMed:30948426).
CC {ECO:0000269|PubMed:30948426}.
CC -!- SIMILARITY: Belongs to the CCDC88 family. {ECO:0000305}.
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DR AlphaFoldDB; P85120; -.
DR SMR; P85120; -.
DR MaxQB; P85120; -.
DR PRIDE; P85120; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; IMP:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR GO; GO:0003383; P:apical constriction; IMP:UniProtKB.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IEA:InterPro.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:UniProtKB.
DR GO; GO:0001841; P:neural tube formation; IMP:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:UniProtKB.
DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR027719; Daple.
DR InterPro; IPR043936; HOOK_N.
DR PANTHER; PTHR18947:SF31; PTHR18947:SF31; 1.
DR Pfam; PF19047; HOOK_N; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Cell junction; Coiled coil; Cytoplasm; Guanine-nucleotide releasing factor;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..2058
FT /note="Protein Daple"
FT /id="PRO_0000284727"
FT DOMAIN 11..131
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1406..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1617..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1696..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1831..1857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..1959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1988..2051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 195..221
FT /evidence="ECO:0000255"
FT COILED 247..428
FT /evidence="ECO:0000255"
FT COILED 455..1016
FT /evidence="ECO:0000255"
FT COILED 1043..1082
FT /evidence="ECO:0000255"
FT COILED 1108..1388
FT /evidence="ECO:0000255"
FT MOTIF 1653..1675
FT /note="GBA 1"
FT /evidence="ECO:0000269|PubMed:30948426"
FT MOTIF 1676..1697
FT /note="GBA 2"
FT /evidence="ECO:0000269|PubMed:30948426"
FT MOTIF 2055..2058
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1419..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1696..1721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1994..2019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1662
FT /note="F->A: Partial reduction in activation of rat Gnai3.
FT Abolishes Gnai3 binding and activation, abolishes promotion
FT of apical cell constriction and fails to rescue morpholino-
FT induced neural plate bending defects but does not affect
FT enrichment at apical cell junctions; when associated with
FT A-1689."
FT /evidence="ECO:0000269|PubMed:30948426"
FT MUTAGEN 1689
FT /note="F->A: Partial reduction in activation of rat Gnai3.
FT Abolishes Gnai3 binding and activation, abolishes promotion
FT of apical cell constriction and fails to rescue morpholino-
FT induced neural plate bending defects but does not affect
FT enrichment at apical cell junctions; when associated with
FT A-1662."
FT /evidence="ECO:0000269|PubMed:30948426"
FT MUTAGEN 2055..2058
FT /note="Missing: Failure to localize to apical cell
FT junctions and to induce apical cell constriction. Failure
FT to rescue morpholino-induced neural plate bending defects."
FT /evidence="ECO:0000269|PubMed:30948426"
SQ SEQUENCE 2058 AA; 236339 MW; C3DA456113A0AD80 CRC64;
MDTTISQQMD HFLESPLVTW VKTFGPCGNE NESKLAMYME LVDGVFLNKI MVQIDPRPSN
QRVNKHVNND VNRRVQNLTI LVRHIKAYYQ EVLQQLIVMN LPNVLLISKD PLTDKSMEEL
KKILLLMLGC AVQCERKEEY IERIKQLDIE TQAGIVSHIQ EVTHNQENVF DLQWLELSDM
APEELDSLSR NMALHLKRLI DERDECKEVI VDLTQERDYL QFQNHPSPVK SSSPDTSANM
VSHLSSEDKK HLAVELAESK AKLRRIRQEL EEKSELLLDT KHEVERLNLE LQKIKQENFQ
LASEARTART YRDEIDSLKE RASKVDRLEN ELARCKEKLH DVDFYKARMD ELREDNMILI
ETKSMLEEQL AAARTRTDKL HELEKENLQL KSKIHDLELD RYSDKNRIEE LLEENMVLEI
AQKQSMNESA QLGWELDQLS KSTDLSDARK SFVFELNETT SSKILKLEKE NQSLQNIIQD
LREASLTLEE GNLKGQEWEK ENQQLSKKIE NLNQQIERER QSSLDLESLS EDLLKEKDQL
SQALENIKSQ KERQIKELEQ ENKHLIQTLE AVRQRSQVST EARVKDIEME NRILHETIKD
TSSKMNELEY EKKQLQKAFD QSKEQVEKLD KMEKEVHRLE KQNEILTKKV TSIKIVEEKM
QGLEKENEVL EGENIVLKKS LDTLQNVTIK LEVLESENKQ LDEENLELRR AVEAMRFSCA
KSTQIERENN ELQKEKEELQ KNVELLKALG KKSERLEVSY QGLNDENWRL QQMLDTGNKK
INDLEKELHD TEKENKDLQR TLEEMKICNK RLERMEEENK AKEQEMVQLE KDNKILQKES
KRLWQQVELK DAILDDNTVK LADLEKENRA LEKEISKLRD LSTKTRDLER ENKDLLQQMT
VDKRTLATLR EDLVLEKLKT QQMSSELDKL SLELEKIGLN KESMLQDENS NAEKKYKLLE
NKIESTLKTT LAVKENKIVA LEMKIEETSS LNQQLQNELN SIKKDIIASK ENLRGAAHNS
YTQLSSKQDC NSQINGQRET TVELLKFKDR TIELERNNAA LQAEKKLFRE QLQHLESHNL
NLSSQMGTLQ KQVTFLQEHN TALQTQTANL QVENATATSQ VASLKSQISQ FQNQLSARES
ENEILQQQKE HLRVTHESLL QDHEQLGSLY ERQSAEYEGM ISQHSSLKSQ YKSLEQAHRS
LEESYSTLIK HKKELEDLDA VLKKEQDVLQ QERRKNFVAM EENQKLKTDL ERLNFLHGEL
QTEYSSLHKH TKEVKTSLNN AQMELNRWQA RFDELKEQHQ TMDISLTKLD NHCELLTRLK
SNLEEENHHL LSQIQMLSQQ NQMLLEQSME TKEQYHEEQK QYIDKLHDLR RQKEKLEEKI
MDQYKFYDPT PKKKSHWSGA KAIAKLIKPK KEPSRESVKS PTDVQSKTMD NAEMAASPSS
MRPLRLQQES LDNSSLGSDE KGSPKVLASK VLVEVAQRQH RMSYHGSSSE QTDGPEHLSR
SRRMESGSRA FSTSTIHLTA PAHNAKVPHL SRPKGYNSDD NQSDQLHEAE SNAGSSRVPW
TSSLEVSRSA SNSSSPLTLK GRPESVSSED MIPTKDIATL SRESNLYHPN AVMLGATKNR
ESPVNRNSLH LYDYPEKKNS SRTPTRPRPG SPGSEMVTLE EFLQESSRQS PPSRRHSLND
SELITLHQFL FEAETLHPSS QSPSPTLHLK DPSQTAVPKS LPSAENCEWR KRADRASRRA
ASLYIPRDMV TNRDDMLGDL FKKTEDPPDI RSPMSELIFK DAAQMPTSYV SPTVKVTGNT
TKPGQYVKPH PRQLDAPLNV TSSLLHQANV YSATSSSQSP EPQALSPHGA MGSRGNSLSR
AFSLASADLL KENGPEVVMQ EKSDVETPVG KDFGRYMIRS STPLGSQSSL REKPQSARMQ
HMLRGDDRQY RSLDSRRLSL ALPKEETTPP QPAPSASSLQ QHYTLGHGAI RGKPKLLSRS
GEVALVSPVR PISSIPELET TQGLASAGPG KSRSTSPDCS PAPVCEEEPN KSETLKSTPA
SPDPSADPQT VWYEYGCV
