ID G3P7Q1_GASAC Unreviewed; 1072 AA.
AC G3P7Q1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Dishevelled associated activator of morphogenesis 1b {ECO:0000313|Ensembl:ENSGACP00000013625.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000013625.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000013625.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000013625.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; G3P7Q1; -.
DR Ensembl; ENSGACT00000013650.1; ENSGACP00000013625.1; ENSGACG00000010299.1.
DR GeneTree; ENSGT00940000156452; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000010299; Expressed in liver and 10 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT DOMAIN 48..423
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 527..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1028
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 441..524
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 532..601
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; 122409 MW; EB6A129DBC90506A CRC64;
MAPRKRGGGG GNRGGLSYIF CCFNGNDHPE ITYRLREDFA LQAMEPALPM PGYDELDGMF
SELVDELDLS EKHREAMFAL PAEKKWQIYC SKKKEQEENK SATSWPEYYI DQLNSMAART
TLLALEKEDE EERNKTIESL KTALRTQPMR FVTRFIDLDG LTCILNFLKS MDYETTESQI
HTSLIGCIKA LMNNSQGRAH VLSHSESINI IAQSLATENI KTKVAVLEIM GAVCLVPGGH
KKILEAMMHY QRFACERTRF QTLINDLDRS TGRYRDEVNL KTAIMSFINA VLSQGAGETS
LEFRIHLRYE FLMLGIQPVI DKLRSHENST LDRHLDYFEM LRNEDELALS KRFESVHIDT
KSANQVFDLI RKKINHTDAH PHFMSVLHHC LLMPHKRSGN TVQYWLLLDR IVQQMVLQND
KGHDPDVTPL ENFNVKNVVR MLVNENEVKQ WKEQAEKMRK EHHELQQRFE KKERECDAKT
QEKEDMMQTL NKMKEKLEKE STEHKNVKQQ VAELTGQLHE LSTRRAAVVP GGPPVGPGPP
GGPLPPPPVP AFGGMCPPPP PPPGGMMPPP PPPPPPPGGP PPPPGCPPIG GIPPPPGAPL
GPSLKRKNIP QPSNALKSFN WAKLSENKLE GTVWMEVDDA KVFKILDLED IEKTFSAYQR
QQKEAEDDAL TSKKVKELSV IDGRRAQNCN ILLSRLKLSN EEMKRAILTM DEQEDLPKDM
LEQLLKFVPE KSDVDLLEEH KHELDRMAKA DRFFYEMSRI NHYQQRLQSL YFKKKFAERI
AEIKPKVEAL SRASKEILHS RNLKQLLEVV LAFGNFMNKG QRGNAYGFKV SSLNKIADTK
SSIDKNITLL HYLITILEKK YPKVLMFQDD LQSLSDAAKV NMTELEKDIG NMRSGLKGVE
SELEYQKKRP QEPGDKFVSV VSQFITVASF SFSDVEDSLV EAKELFLKAV KHFGEDAGKM
QPDEFFGIFD QFLQSFAEAQ QENENMRKRK EEEERRAKME AQLKEQREKE RKARKAKANG
EDDGGEFDDL VSALRSGEVF DKDLSKMKRN RKRINSQTTD ASRERPVTKL NF
//