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Database: UniProt
Entry: A0A3P8PT66_ASTCA
LinkDB: A0A3P8PT66_ASTCA
Original site: A0A3P8PT66_ASTCA 
ID   A0A3P8PT66_ASTCA        Unreviewed;      1072 AA.
AC   A0A3P8PT66;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Dishevelled associated activator of morphogenesis 1 {ECO:0000313|Ensembl:ENSACLP00000020271.1};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000020271.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000020271.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000020271.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3P8PT66; -.
DR   Ensembl; ENSACLT00000020740.1; ENSACLP00000020271.1; ENSACLG00000013675.1.
DR   GeneTree; ENSGT00940000156452; -.
DR   Proteomes; UP000265100; Chromosome 15.
DR   Bgee; ENSACLG00000013675; Expressed in anal fin and 8 other cell types or tissues.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 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   PANTHER; PTHR45725:SF16; DISHEVELED-ASSOCIATED ACTIVATOR OF MORPHOGENESIS 1; 1.
DR   PANTHER; PTHR45725; FORMIN HOMOLOGY 2 FAMILY MEMBER; 1.
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; ARM repeat; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}.
FT   DOMAIN          51..426
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          606..1002
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1020..1052
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          531..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          980..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1042..1072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          444..527
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        535..600
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        982..1024
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1059
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1072 AA;  122186 MW;  5C4EC507FF965EFE CRC64;
     MPPRKRGGGS GGGGGRSGFS AIFCCFNNRD HPEITYKLRD DFALQSMEPS LPMPGNDELD
     SMFAELVDEL DLTEKHREAM FALPAEKKWQ IYCSKKKEQE ENKSATSWPE YYIDQLNSMA
     ARKTLLALEK EDEEERNKTI ENLKTALRTQ PMRFVTRFID LDGLTCILNF LKSMDYDTTE
     SQIHTSLIGC IKALMNNSQG RAHVLAHSES INIIAQSLAT ENIKTKVAVL EIMGAVCLVP
     GGHKKILESM LHYQRFACER TRFQTLVNDL DRSTGRYRDE VSLKTAIMSF INAVLSQGAE
     ETSLEFRIHL RYEFLMLGIQ PVIDKLHSHE NATLDRHLDY FEMLRNDDEL AVSKRFESVH
     VDTKSATQVF DLIRKKMSHT DAYPHFMSVL HHCLLMPHKR SGNTVQYWLL LDRIVQQMVL
     QNDKGHDPDV TPLENFNVKN VVRMLVNENE VKQWKEQAEK MRKEHHELQQ KFEKKERECD
     AKTQEKEDMM QTLNKMKEKL EKESNEQKNV KQQVAELTAR LHELSTRQAA VVPGGPPVAP
     GPPGGPVPQP GFAGIAPPPP PPPGGMMPPP PPPPPPPGGP PPPPGLPPIG GIPPPPGAPL
     GSSLKKKNIP QPSNPLKSFN WSKLAENKLE GTVWMEVDDA KVFKVLDLDD IEKTFSAYQR
     QQKEAEDDTL GSKKVKELSV IDGRRAQNCN ILLSRLKLSN DEIKRAILTM DEQEDLPKDM
     LEQLLKFVPE KSDVDLLEEH KHELDRMAKP DRFLYEMSRI NHYQQRLQSL YFKKKFAERI
     AEIKPKVEAL GKASKEVLNS RNLKQLLEVV LAFGNYMNKG QRGNAYGFKV SSLNKIADTK
     SSIDKNITLL HYLITILEKK YPKVLKFQED LQSISEAAKV NMTELEKDIG NLRSGLKSVE
     SELEYQKKGP QEPGDKFVSV VSQFITVASF SFTDVEDSLI EAKELFLRAV KHFGEDASKM
     QPDEFFGIFD QFLQSFTEAQ QENENIRKRK EEEERRAKVE AQLREQREKE RKARKAKANG
     EEDGGEFDDL VSALRSGEVF DKDLSKMKRN RKRINNQNTD SGRERPVTKL NF
//
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