ID A0A3P9B7K1_9CICH Unreviewed; 886 AA.
AC A0A3P9B7K1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Protein diaphanous homolog 3 {ECO:0000313|Ensembl:ENSMZEP00005005861.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005005861.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005005861.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005005861.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000256|ARBA:ARBA00008214}.
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DR AlphaFoldDB; A0A3P9B7K1; -.
DR Ensembl; ENSMZET00005006115.1; ENSMZEP00005005861.1; ENSMZEG00005003495.1.
DR GeneTree; ENSGT00940000157767; -.
DR Proteomes; UP000265160; LG1.
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; 6.10.30.30; -; 1.
DR Gene3D; 1.10.20.40; Formin, diaphanous GTPase-binding domain; 1.
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; IPR044933; DIA_GBD_sf.
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; PTHR45691; PROTEIN DIAPHANOUS; 1.
DR PANTHER; PTHR45691:SF9; PROTEIN DIAPHANOUS HOMOLOG 3; 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; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..886
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017926695"
FT DOMAIN 59..413
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 557..886
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 26..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 830..857
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 477..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 100799 MW; AE46C8FAE4F2885F CRC64;
YFFLFLIVLS FFLQLDRFAS IRIPGSKKER PPLTQSKHNA NDWSSSSSST SHHFEELSSK
INSEKEILAL FEKMMEDMNL NEDKKTPLRE KDLNTKKEMV IQYISTASKT GNLRSSHQIS
PQEFLSELKS GVMDERLFSC LDSLRVSLTS NPVSWVQNFG HEGLGLLLDI LERLLFKKHQ
EKIDKKNQHK VIQCLKAFMN NKYGLDRILG EEKSLALLAR AIDPNQSAMM TDVVKLLSAI
CIVGEENILE KVLEAITTAG EWRGIERFSP IVQGLRDRSV QLQVACMQLI NALVTSPDEL
DFRLHIRNEF MRCGLKEILP VIIRNEALDI QLKVFEEHKE EDMMEFSHRL EDIKSDIFSI
VQSMVKDSSA EPYFLSILQH LVLIRNDHLI RPQYFKIIEE CVSQIVLHRS GTDPDFSYRK
RLDVDFSHLL EVCVDKSRID EYEQQASELA QKASNDKRKQ KYSMLTFKLC SVPVGPANAG
QASSSSTIPS GVPIPAPASL GPVPPPPPPP PPLPGCPAPP PPPGMPPPFG APPPPPLGFG
GGLGSPTHHT LPYGLRPKKE FKPETSMKRL NWSKIRPQEM SEGCFWVRVD EDQYAKPDLL
IFLSLSAKKE EEDTEDKKSI KKRIKELKVL DPKIAQNLSI FLGSFRIPYQ EIRRMIVEVD
EEQLSEPMIQ NLVKHLPEQE QLNALATYKN EYSNLSEPEQ FGVVMSSVKR LRPRLSHILF
RLQFEEHVNN LRPDILAVNA ACDEVRKSRS FGRLLELVLL LGNYMNAGSR NAQSYGFDLS
SLCKLKDTKS ADQKTTLLHF LAQVCEDEFP DVVKFLDDLE HVDRASRVSA ENLEKSLRQM
ERQLLQLERD LETFSSSDDP NDMFLTKMAI SFTRVCIGSS LWAIMQ
//
