ID I3J5A4_ORENI Unreviewed; 917 AA.
AC I3J5A4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Diaphanous-related formin 3 {ECO:0000313|Ensembl:ENSONIP00000004044.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000004044.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000004044.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000256|ARBA:ARBA00008214}.
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DR AlphaFoldDB; I3J5A4; -.
DR Ensembl; ENSONIT00000004045.2; ENSONIP00000004044.2; ENSONIG00000003222.2.
DR eggNOG; KOG1924; Eukaryota.
DR GeneTree; ENSGT00940000157767; -.
DR TreeFam; TF315383; -.
DR Proteomes; UP000005207; Linkage group 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:UP000005207}.
FT DOMAIN 94..457
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 622..917
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 504..531
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 104179 MW; C90C0B0D097700F7 CRC64;
MESYSQRFES TTGRDSKSQK KKGSTSSYTD DGDRKPKFHL PFRNITDDVL DRFASIRIPG
SKKERPPLTQ SKHNANDWSS SSSSTSHHFE ELSSKINSEK EILALFEKMM EDMNLNEDKK
TPLREKDLNT KKEMVIQYIS TASKTVRKQV ISGSLRNSHQ ISPQEFLSEL KSGVMDERLF
SCLDSLRVSL TSNPVSWVQN FGHEGLGLLL DILERLLFKK HQEKIDKKNQ HKVIQCLKAF
MNNKYGLDRI LGEEKSLALL ARAIDPNQSA MMTDVVKLLS AICIVGEENT LEKVLEAITT
AGEWRGIERF SPIVQGLRDR SVQLQVACMQ LINALVTSPD ELDFRLHIRN EFMRCGLKEI
LPQLLVIRNE ALDIQLKVFE EHKEEDMMEF SHRLEDIRSE LEYPCLYDKK DSSAEPYFIS
ILQHLVLIRN DHLIRPQYFK IIEECVSQIV LHRSGTDPDF SYRKRLDVDF SHLLEVCVDK
SRIDEYEQRA SELAQKFDEE FLSRQEAQAQ LVKCEEKIAE LQAELQAFRS QFGAVPVGPA
SANAGQALSS STIPSGVPSP APASLGPVPP PPPPPPPLPG CPAPPPPPGM PPPFGAPPPP
PLGFGGGLGS PTHHTLPYGL RPKKEFKPET SMKRLNWSKI RPQEMSEGCF WVRVDEDQYA
KPDLLNRVAL TFGSQRTEDD TEDKKSIKKR IKELKVLDPK IAQNLSIFLG SFRIPYQEIR
RMIVEVDEEQ LSEPMIQNLV KHLPEQEQLN ALATYKNEYS NLSEPEQFGV VMSSVKRLRP
RLSHILFRLQ FEEHVNNLRP DILAVNAACD EVRKSRSFGR LLELVLLLGN YMNAGSRNAQ
SYGFDLSSLC KLKDTKSADQ KTTLLHFLAQ VCEEEFPDVV KFLDDLEHVD RASRGNILKH
LDKRIMMAQS VHASKHA
//
