DAPLE_DANRE
ID DAPLE_DANRE Reviewed; 2023 AA.
AC A0A2R8QCI3; F1QG38; Q6DG47;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Protein Daple {ECO:0000303|PubMed:30948426};
DE AltName: Full=Coiled-coil domain-containing protein 88C {ECO:0000312|ZFIN:ZDB-GENE-100419-3};
GN Name=ccdc88c {ECO:0000312|ZFIN:ZDB-GENE-100419-3};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000312|EMBL:AAH76506.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1643-2023.
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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 (By similarity). Functions upstream of ctnnb1/beta-catenin in
CC the canonical Wnt pathway, and also activates jnk in the Wnt/planar
CC cell polarity (PCP) pathway (By similarity). Acts as a non-receptor
CC guanine nucleotide exchange factor which binds to and activates guanine
CC nucleotide-binding protein G(i) alpha (Gi-alpha) subunits
CC (PubMed:30948426). This promotes apical cell constriction and
CC subsequent bending of the neural plate during neurulation via arhgef18
CC (By similarity). {ECO:0000250|UniProtKB:P85120,
CC ECO:0000269|PubMed:30948426}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9P219}. Cell
CC junction {ECO:0000250|UniProtKB:Q9P219}. Note=Enriched at apical cell
CC junctions. {ECO:0000250|UniProtKB:Q9P219}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A2R8QCI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A2R8QCI3-2; Sequence=VSP_060436;
CC -!- DEVELOPMENTAL STAGE: Undetectable at the gastrula stage at 7.5 hours
CC post-fertilization (hpf) but readily observable during neurulation at
CC 16 and 22 hpf where expression is restricted to the neural rod at 16
CC hpf and the neural tube at 22 and 28 hpf.
CC {ECO:0000269|PubMed:30948426}.
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). {ECO:0000250|UniProtKB:Q9P219}.
CC -!- DOMAIN: The PDZ domain is required for localization to apical
CC junctions. {ECO:0000250|UniProtKB:Q9P219}.
CC -!- DISRUPTION PHENOTYPE: Impaired hinge point formation in the forebrain
CC and midbrain cavities at 22 hours post-fertilization (hpf) in 95% of
CC embryos (PubMed:30948426). Moderate curvature of the dorsal axis in 35%
CC of embryos at 28 hpf which disappears at later stages
CC (PubMed:30948426). Mild abnormalities in midbrain and forebrain
CC ventricular cavities at 56 hpf (PubMed:30948426).
CC {ECO:0000269|PubMed:30948426}.
CC -!- SIMILARITY: Belongs to the CCDC88 family. {ECO:0000305}.
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DR EMBL; BX530029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC076506; AAH76506.1; -; mRNA.
DR RefSeq; XP_001921927.1; XM_001921892.5. [A0A2R8QCI3-2]
DR AlphaFoldDB; A0A2R8QCI3; -.
DR SMR; A0A2R8QCI3; -.
DR STRING; 7955.ENSDARP00000062009; -.
DR Ensembl; ENSDART00000062010; ENSDARP00000062009; ENSDARG00000053713. [A0A2R8QCI3-2]
DR Ensembl; ENSDART00000187996; ENSDARP00000149375; ENSDARG00000053713. [A0A2R8QCI3-1]
DR GeneID; 553231; -.
DR KEGG; dre:553231; -.
DR CTD; 440193; -.
DR ZFIN; ZDB-GENE-100419-3; ccdc88c.
DR eggNOG; KOG4643; Eukaryota.
DR GeneTree; ENSGT00940000154785; -.
DR HOGENOM; CLU_001421_1_0_1; -.
DR OMA; EAESWQR; -.
DR OrthoDB; 59187at2759; -.
DR TreeFam; TF320231; -.
DR PRO; PR:A0A2R8QCI3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000053713; Expressed in mature ovarian follicle and 27 other tissues.
DR ExpressionAtlas; A0A2R8QCI3; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
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:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003383; P:apical constriction; ISS:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0001841; P:neural tube formation; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA: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 2: Evidence at transcript level;
KW Alternative splicing; Cell junction; Coiled coil; Cytoplasm;
KW Guanine-nucleotide releasing factor; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..2023
FT /note="Protein Daple"
FT /id="PRO_0000448711"
FT DOMAIN 11..131
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1013..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1837..2023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 250..415
FT /evidence="ECO:0000255"
FT COILED 458..1064
FT /evidence="ECO:0000255"
FT COILED 1105..1419
FT /evidence="ECO:0000255"
FT MOTIF 1700..1728
FT /note="GBA"
FT /evidence="ECO:0000250|UniProtKB:Q9P219"
FT MOTIF 2020..2023
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1441..1462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1492
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1591..1605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1665..1703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1965..1984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1986..2013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1065..1090
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060436"
SQ SEQUENCE 2023 AA; 230337 MW; EB1530D0DA868CA2 CRC64;
MDITVSELMS NFMDSPLVVW VKTFGPLGFS SEDKLSMFMD LVDGVFLHKI MTHIDPSPMN
QRVNKQVNND VNLRIQNLNT VIRHIKNYYQ EHLQQLIVMN LPNVLAIAKD PLSGKSMEEM
KRMLLLILGC AVQCDRKEEI IEKIKLLDIE TQAAIVTHIQ EVTHNQENVL DLQWMEVAEI
PAEQLDPLSR TMAFHLRKLI DERDESAELV IELTQERDYL QSQQPSGLLG FPSPERTSLS
PITLLSKEDR QHLAVELADT KAKLRRSRQE LEEKTEQLID AKNEIERLDS DIQKLKQENT
QLLAEARSVR AYRDEVDSLR ERAGKVDRLE TELSRFKEKL NDVHFYKTRI EELREDNLTL
LETKSMLEEQ LTGARGRCDK LHELEKENLQ LRSKLHDIEI DRDSDKKRLE ELLEENMLLE
ISQKQSMNES AHLGWELEQL AKNNEVNEAR KSFVFELNES ASSRLLKLEK ENQCLQSTIQ
ELREASINME EGQLHSLELE KENQSLSKKL ERLQSQLDQE KQTTQDMENL GEELIKEKQR
MEKTLETIQA EKDRQISELE QEKEHLTQAV SSLRKRAQAN SEARVREVET ENRILHQTIS
ETGGKLARLE AEKRQVTKEL ESLRERGERC EELEREVPRL ERVREQLQRE AAALKIGSER
AEALERENAT LEQDNRRLKK LADTAQNATL RLAVLEKDHQ QLEEENLEQR RALETLRPAA
ARLAQLQQEH AELEREHEEM CRTMEELRSQ AKRSERLEKS CGSLSLENQR LQQTLENSST
KMQGLESELR QNEAEMKDLQ RELEGLRQKV TWAETLEKEN RGMEQELSQL EKEKKQLEKE
ARRFRQQLEV KEAALEENCL RLASMEKEGT ALSKELGRVK EAAGRLKELE RENKDLQKQA
TMDKKTLATL REELVNEKLR VQQQCNELEK LSHELEKIGL NREKLLQEEH SCEDNKYKIL
ETKIESALKK TLELREEKIQ SLESRLEESS SLNQQLRTEL TTVKKNLEAL KQRHEEEAAH
SEISQQTLGQ TRSLPDKEKW EMEQREATAE LLKLKDRLID VEKNVRQRHV SIDIHRVIFS
IVICFCDSLQ NAALQTEKYL LKDQLKQIDS QNAQLNAQTL ALQKQAASLQ EHNTSLHKET
AKLQVENSTL SSQSSSLMAQ YGALQAQLQT LESEAESLQK QREEASAARD RVTQDHERLL
GVHERQASEY EQLIAQHAAL KASQRALEQE NRTLENKYMV LLKQKDAMEA LEESLQRDRE
SLGEEIRKNT LILGENRSLR EEVDRVSHMH TQLRQEYDSL QLQTKELKTS LNESQLELNR
WQARYDQLKE QHQGLDISMT KLDNHCELLT RLKGNLEEEN HHLLSQIQML SQQNQTLLER
TMESKELYHE EQKQYIDKLN SLRRQKEKLE EKIMDQYKFY DPTPKKSRQW VGAKAIAKFI
KPKKESSRER PDAPRERIRS APDIPLPEIP TCIDCPESAP PPPPPPLPPR QSRPSLDSMN
SQSVEENHVQ SPTLSSPALN GRVLNESGGS RSRDGYRSIG GGSESMNGYE ELLRWRSREP
GGATCSTPLS RNSHNAPGFT SSSSLRPGRR PKGLVSEEDL RHHSPDAGFG SGVHGNTGHR
PSSAEFSRNT SSSNSPVSSK GSLDCLQGRS ASLSSDDVVG LAHEGSRLSQ SSLLPRSSTL
PCDSPSASRP SQRPASRRPS SPGSEMVTLE EFLQESNALS PPTVQTGSRE DLMTDYFTRS
TRPVPLRDGA KTPTNYVTPT VKTTPPELDA RTPKPGHSVK PSVRLTDTST PPSHSQTLPN
RGAGLRPSAL QQSSPRGSVG GSASLSRTFS LASADLLRSN GPDSYRTEAA SPNQNDVVMR
RPGAVARERP MSARVTGSSP LPGDPGHISV DPRRLSLAQP RDEFSLVSPP PLHSSSMSLQ
AEREYVGSGS SRAGAARSGS AQPRGAPHRG EVAMVTPVRA VPALRLNDLE EEPQEQREAE
SPLLKKADTT NLSYASKEQP TSKPASPDPN NDPQTVWYEY GCV
