ID   DAA1A_XENLA             Reviewed;        1081 AA.
AC   B0DOB5;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Disheveled-associated activator of morphogenesis 1-A;
GN   Name=daam1-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], AND FUNCTION.
RX   PubMed=26644512; DOI=10.1083/jcb.201502043;
RA   Yasunaga T., Hoff S., Schell C., Helmstaedter M., Kretz O., Kuechlin S.,
RA   Yakulov T.A., Engel C., Mueller B., Bensch R., Ronneberger O., Huber T.B.,
RA   Lienkamp S.S., Walz G.;
RT   "The polarity protein Inturned links NPHP4 to Daam1 to control the
RT   subapical actin network in multiciliated cells.";
RL   J. Cell Biol. 211:963-973(2015).
RN   [2]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=11779461; DOI=10.1016/s0092-8674(01)00614-6;
RA   Habas R., Kato Y., He X.;
RT   "Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and
RT   requires a novel Formin homology protein Daam1.";
RL   Cell 107:843-854(2001).
CC   -!- FUNCTION: Binds to disheveled (dsh) and Rho, and mediates Wnt-induced
CC       dsh-Rho complex formation during gastrulation (PubMed:11779461). May
CC       play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF,
CC       thereby enhancing Rho-GTP formation. Can direct nucleation and
CC       elongation of new actin filaments. Involved in building functional
CC       cilia (By similarity). Involved in building functional cilia. Involved
CC       in the organization of the subapical actin network in multiciliated
CC       epithelial cells (PubMed:26644512). {ECO:0000250|UniProtKB:Q9Y4D1,
CC       ECO:0000269|PubMed:11779461, ECO:0000269|PubMed:26644512}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4D1}.
CC       Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000250|UniProtKB:Q9Y4D1}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis.
CC       {ECO:0000269|PubMed:11779461}.
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DR   AlphaFoldDB; B0DOB5; -.
DR   SMR; B0DOB5; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.2220; -; 1.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; DAD_dom.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM01139; Drf_FH3; 1.
DR   SMART; SM01140; Drf_GBD; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW   Reference proteome; Wnt signaling pathway.
FT   CHAIN           1..1081
FT                   /note="Disheveled-associated activator of morphogenesis 1-
FT                   A"
FT                   /id="PRO_0000437576"
FT   DOMAIN          45..418
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT   DOMAIN          603..1012
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   DOMAIN          1030..1061
FT                   /note="DAD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT   REGION          455..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..705
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4D1"
FT   REGION          1013..1038
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1060..1081
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..590
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1081 AA;  124182 MW;  B7BE8C4BE4E0A232 CRC64;
     MAPRKRNSRG VSFIFCCFRS SEHPEITYRL RNDSNFALQS MEPALPVPPV EELDAMFAEL
     VDELDLSEKH REAMFALSAE KKWQIYCSKK KDHEEGATSW PEFYIDQLNS MAARRTLFAM
     DKEDEEERNK TIESLKTALR TKPMRFVTRF IDLDGLTCIL NFLKSMDYEI AESQIHTSLI
     GCIKALMNNS QGRAHVLAHT ESINVIAQSL ATENIKTKVA VLEIMGAVCL VPGGHKKVLE
     AMLHYQRYAS ERTRFQTLIN DLDRSTGRYR DEVSLKTAIM SFINAVLSQG AGVESLDFRL
     HLRYEFLMLG IQPVIDKLRE HENSTLDRHL DFFEMLRNED ELEFAKRFDL VHIDTKSATQ
     MFELIRKRLT HTESYPHFTS ILHHCLQMPY KRSGNTVHYW LLLDRIVQQI VIQNEKGQDP
     DTSPLENFNV KNVVRMLVNE NEVKQWKEQA EKMRKEHNEL QQKLEKKERE CDAKTQEKEE
     MMQTLNKMKE KLEKETTEYK NVKQQVAELT AQIQELNSRT VCAPGPGGPP PPPGAPGGPM
     SMPSGNFMPP PPPPPPPFPG GMAPPPPPPP PPPPPPGGPP PPPGLPLLGA APPGAPLGLS
     MKKKNIPQPK NPLKSFNWSK LPDNKLEGTL WIDLDDAKVL KILDLEDIER TFSAYQRQQD
     FFVNNGIKQK EMDCTDDTLS SKMKVKELSV VDGRRAQNCN ILLSRLKLTN EEIKRAILTM
     DEQEDLPKDM LEQLLKFVPE KSDIDLLEEH KHELDRMAKA DRFLFEMSRI NHYQQRLQSL
     YFKKKFAERV AEVKPKVEAI RDASKEVLQS KNLKQLLEVV LAFGNYMNKG QRGNAYGFKI
     SSLNKIADTK SSIDKNITLL HYLITVVEKK YPKIVNLHEE LQTISVAAKV NMTELEKEIS
     ALRNGLKSVE NELEYQKTQP TLPGDKFVSV VSQFITVAGF SFCDVEDLLS EAKELFVKSA
     KRFGEETNKI QPDEFFGIFD QFLQAFLEAK QENENIRKRK EEEERRIRME AQLKEQRERE
     RKARKAKENG EEEGEFDDLV SALRSGEVFD KDLSKLKRNR KRIVSQTTES SRERPVTKLN
     Y