DAPLE_MOUSE
ID DAPLE_MOUSE Reviewed; 2009 AA.
AC Q6VGS5; Q3UVI2;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein Daple;
DE AltName: Full=Coiled-coil domain-containing protein 88C;
DE AltName: Full=Dvl-associating protein with a high frequency of leucine residues;
GN Name=Ccdc88c; Synonyms=Daple;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAR08446.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DVL1,
RP HOMOOLIGOMERIZATION, AND MUTAGENESIS OF GLY-2007 AND VAL-2009.
RC TISSUE=Brain {ECO:0000269|PubMed:14750955};
RX PubMed=14750955; DOI=10.1111/j.1365-2443.2003.00692.x;
RA Oshita A., Kishida S., Kobayashi H., Michiue T., Asahara T., Asashima M.,
RA Kikuchi A.;
RT "Identification and characterization of a novel Dvl-binding protein that
RT suppresses Wnt signalling pathway.";
RL Genes Cells 8:1005-1017(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE23287.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-966 (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23287.1};
RC TISSUE=Urinary bladder {ECO:0000312|EMBL:BAE23287.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUBCELLULAR LOCATION.
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: Required for activation of guanine nucleotide-binding
CC proteins (G-proteins) during non-canonical Wnt signaling. Binds to
CC ligand-activated Wnt receptor FZD7, displacing DVL1 from the FZD7
CC receptor and leading to inhibition of canonical Wnt signaling. Acts as
CC a non-receptor guanine nucleotide exchange factor by also binding to
CC guanine nucleotide-binding protein G(i) alpha (Gi-alpha) subunits,
CC leading to their activation. Binding to Gi-alpha subunits displaces the
CC beta and gamma subunits from the heterotrimeric G-protein complex,
CC triggering non-canonical Wnt responses such as activation of RAC1 and
CC PI3K-AKT signaling. Promotes apical constriction of cells via ARHGEF18.
CC {ECO:0000250|UniProtKB:Q9P219}.
CC -!- SUBUNIT: Homooligomer (PubMed:14750955). Interacts with DVL1 (via PDZ
CC domain); dissociates following initiation of non-canonical Wnt
CC signaling (PubMed:14750955). Interacts (via C-terminus) with ligand-
CC activated Wnt receptor FZD7; competes with DVL1 for binding to FZD7 and
CC displaces DVL1 from ligand-activated FZD7 (By similarity). Interacts
CC (via GBA motif) with guanine nucleotide-binding protein G(i) alpha
CC subunits GNAI1, GNAI2 and GNAI3 (inactive GDP-bound form); interacts
CC with higher affinity with GNAI1 and GNAI3 than with GNAI2 and
CC interaction leads to G(i) alpha subunit activation (By similarity).
CC Does not interact with GNAO1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9P219, ECO:0000269|PubMed:14750955}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:14750955};
CC IsoId=Q6VGS5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q6VGS5-2; Sequence=VSP_052377;
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 -!- SIMILARITY: Belongs to the CCDC88 family. {ECO:0000305}.
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DR EMBL; AY339881; AAR08446.1; -; mRNA.
DR EMBL; AK137260; BAE23287.1; -; mRNA.
DR CCDS; CCDS26110.1; -. [Q6VGS5-1]
DR RefSeq; NP_080957.2; NM_026681.4. [Q6VGS5-1]
DR AlphaFoldDB; Q6VGS5; -.
DR SMR; Q6VGS5; -.
DR BioGRID; 212810; 8.
DR IntAct; Q6VGS5; 3.
DR MINT; Q6VGS5; -.
DR STRING; 10090.ENSMUSP00000082177; -.
DR iPTMnet; Q6VGS5; -.
DR PhosphoSitePlus; Q6VGS5; -.
DR EPD; Q6VGS5; -.
DR MaxQB; Q6VGS5; -.
DR PaxDb; Q6VGS5; -.
DR PeptideAtlas; Q6VGS5; -.
DR PRIDE; Q6VGS5; -.
DR ProteomicsDB; 279825; -. [Q6VGS5-1]
DR ProteomicsDB; 279826; -. [Q6VGS5-2]
DR Antibodypedia; 105; 15 antibodies from 10 providers.
DR Ensembl; ENSMUST00000068411; ENSMUSP00000068629; ENSMUSG00000021182. [Q6VGS5-1]
DR Ensembl; ENSMUST00000085096; ENSMUSP00000082177; ENSMUSG00000021182. [Q6VGS5-2]
DR GeneID; 68339; -.
DR KEGG; mmu:68339; -.
DR UCSC; uc007ote.1; mouse. [Q6VGS5-1]
DR CTD; 440193; -.
DR MGI; MGI:1915589; Ccdc88c.
DR VEuPathDB; HostDB:ENSMUSG00000021182; -.
DR eggNOG; KOG4643; Eukaryota.
DR GeneTree; ENSGT00940000154785; -.
DR HOGENOM; CLU_001421_1_1_1; -.
DR InParanoid; Q6VGS5; -.
DR OMA; YRDELEC; -.
DR OrthoDB; 59187at2759; -.
DR PhylomeDB; Q6VGS5; -.
DR TreeFam; TF320231; -.
DR BioGRID-ORCS; 68339; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ccdc88c; mouse.
DR PRO; PR:Q6VGS5; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q6VGS5; protein.
DR Bgee; ENSMUSG00000021182; Expressed in granulocyte and 213 other tissues.
DR ExpressionAtlas; Q6VGS5; 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:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
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:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:UniProtKB.
DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; ISS:UniProtKB.
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 Alternative splicing; Cell junction; Coiled coil; Cytoplasm;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..2009
FT /note="Protein Daple"
FT /id="PRO_0000284726"
FT DOMAIN 11..131
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 221..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1757..1787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1808..2009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2007..2009
FT /note="DVL1-binding"
FT /evidence="ECO:0000269|PubMed:14750955"
FT COILED 247..425
FT /evidence="ECO:0000255"
FT COILED 456..1008
FT /evidence="ECO:0000255"
FT COILED 1190..1384
FT /evidence="ECO:0000255"
FT MOTIF 1652..1683
FT /note="GBA"
FT /evidence="ECO:0000250|UniProtKB:Q9P219"
FT MOTIF 2006..2009
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 221..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1552..1582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1631..1660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1761..1787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1890..1915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..1995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P219"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P219"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P219"
FT MOD_RES 1435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P219"
FT MOD_RES 1592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P219"
FT MOD_RES 1798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P219"
FT VAR_SEQ 509
FT /note="K -> KAGSLHLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052377"
FT MUTAGEN 2007
FT /note="G->A: Abolishes binding to DVL1."
FT /evidence="ECO:0000269|PubMed:14750955"
FT MUTAGEN 2009
FT /note="V->A: Abolishes binding to DVL1."
FT /evidence="ECO:0000269|PubMed:14750955"
SQ SEQUENCE 2009 AA; 226535 MW; 68AB26B288393BD4 CRC64;
MDVTVSQLVE LFLQSPLVTW VKTFGSFGSG HQDNLTLYMD LVDGIFLNQI MLQIDPRPSN
QRINKHVNND VNLRIQNLSI LVRNIKTYYQ EVLQQLIVMN LPNVLMIGKD PLSGKSMEEI
KKVLLLVLGC AVQCERKEEF IERIKQLDIE TQAGIVAHIQ EVTHNQENVF DLQWLDLPDV
APEELEALSR NMVFHLRRLI DERDECTELI VDLTQERDYL QTQQPPSPGK FSSPDSTPSP
TSSLSSEDKQ HLAVELADTK ARLRRVRQEL EEKTEQLADT RHEVDQLVLE LQKAKQDNIQ
LAADARSARA YRDELDSLRE KANRVERLEM DLVRCKEKLH DVDFYKARME ELREDNIILI
ETKAMLEEQL TASRARSDKV HELEKENLQL KSKLHDLELD RDADKKQIEK LLEEYMVLEM
AQKQSMKESA HLGWELEQLS KNADLSDASR KSFVFELNEC ASSRILKLEK ENQSLQSTIQ
GLRDTSLALE ESSLKYGELE KENQQLSKKI EKLQTQLERE KQSNQDLETL SEELIREKEQ
LQSGMEALKA DRARQIKDLE QEKGHLHQAV WSLRERPQVN STKDVEKENR ALHQAVTEAG
SKLSQLELEK QQLHRDLEEA KEKGEQAEAL EKELHRLEKE NEQLTKEVTS LKAATEKVEA
LEHQSQGLEL ENRSLRKSLD TLQNVSVQLE GLERDKQQLG QENLELRKMV EAMRFTSAKM
AQIETENRQL EREKEELRRD VELLKTLSKK SERLELSYQS VSAENLQLQH SLESSTHKSQ
ALQRELSQLE AERQALRRDL ETLQLTHKQL EGAEEDRKAL EQEVAQLEKD KKLLEKEARR
LWQQVELKDA ILDDSAAKLS AAEKESRALD KELARCRDVG SKLKELEKDN RDLTKQVTMH
TRTLTTLRED LVLEKLKSQQ LSSELDKLSQ ELEKVGLSKD LLLQEDDGHG DGKGKTESAL
KTTLAMKEEK IVFLEAQVEE KESLSRQLQI ELQMIKKEHE QLRQTQEGGD KAQNALKRPP
GKVTSHQEKE AWEPSHKEAT MELLRVKDRA IELERSNAAL QAERQLLKEQ LQHLETQNVS
FSSQILTLQK QSAFLQEHTT TLQTQTAKLQ VENSTLSSQN AALSAQYTVL QSQQAAKEAE
HEGLQQQQEQ LAAVYEALLQ DHKHLGTLYE CQSSEYEALI RQHSCLKTLH RNLELEHKEL
GERHGDLQQR KAELEELEKV LSTEREALER EQKTNAIATS ENQRLRGELD RISFLHQQLK
GEYEELHAHT KELKTSLNNS QLELSRWQVR FDELKEQHQS MDISLTKMDN HCELLSRLKG
NLEEENHHLL SQIQLLSQQN QMLLEQNMES KEQYHEEQKQ YIDKLNALRR HKEKLEEKIM
DQYKFYDPAP KKKNHWIGAK ALVKLIKPKK EGSRERLKST TDSPPWQLEP SDPASPSPSQ
ALRSQTENPD NPPSGPNCVE ERDTHNGPVG KGPGDLKPKR GSPRGGSVDR TDTSTDPAVK
SWPSEPGSRT FSTSATTAAL SSSTPIPKHL GRTKGCNSDD NLCEPSSEPD GPYHRQQASR
PNSLESSRNA SSNSSPLSLK GSSDHLHSRC ESFSSADLIP SRDPATLSRD GNTSGRGLLG
RHEYPPPRNG PVSQETIQKK GAASTHTGVR PHSASPSSEM VTLEEFLEES NRGGSPTHDT
PSCRDDLLSD YFRKAHDPPA LGGQPGPPAR KDGAKMPTSF VAPTIKMSIN TSEGQQLKPG
HYVKPNLRPS EAEALAGMPS RQVQPPQSLS LGRPRQTTMT QNCHMPVSRS ASLSRAFSLA
SADLLRASGP EACRPESPQK PGGHEAAGAR ETSTHSLQGS HILARERTPI VGKADSPSPG
QGTRGRPLDT RRFSLAPPKE ERLAPLQQSA TAPALATGCS SGSNPQIQHF SPTVAPAVRT
KSKVPQHSGE VATVAPVRPG LGTSEGDGGP GHGYSEGLLT KSPGRSSDLP PHVKRGPDDF
SQGSSSKSTP ASPEPGGDPQ TVWYEYGCV
