ID I3J5A5_ORENI Unreviewed; 1109 AA.
AC I3J5A5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Diaphanous-related formin 3 {ECO:0000313|Ensembl:ENSONIP00000004045.2};
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:ENSONIP00000004045.2, 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:ENSONIP00000004045.2}
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; I3J5A5; -.
DR STRING; 8128.ENSONIP00000004045; -.
DR Ensembl; ENSONIT00000004046.2; ENSONIP00000004045.2; ENSONIG00000003222.2.
DR GeneTree; ENSGT00940000157767; -.
DR HOGENOM; CLU_002356_0_0_1; -.
DR InParanoid; I3J5A5; -.
DR OMA; VTKMSIF; -.
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; 1.20.58.630; -; 1.
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; IPR014767; DAD_dom.
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; 2.
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 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..477
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 627..1027
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1050..1080
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
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 555..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 524..551
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 906..933
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 565..610
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1109 AA; 127175 MW; 4B7F6D54DA38AC56 CRC64;
MESYSQRFES TTGRDSKSQK KKGSTSSYTD DGDRKPKFHL PFRNITDDVL DRFASIRIPG
SKKERPPLTQ SKHNANDWSS SSSSTSHHFE ELSSKINSEK EILALFEKMM EDMNLNEDKK
TPLREKDLNT KKEMVIQYIS TASKTGSLRN SHQISPQEFL SELKSGVMDE RLFSCLDSLR
VSLTSNPVRY ANSNLLLSCF NSQEKIDKKN QHKVIQCLKA FMNNKYGLDR ILGEEKSLAL
LARAIDPNQS AMMTDVVKLL SAICIVGEEN TLEKVLEAIT TAGEWRGIER FSPIVQGLRD
RSVQLQVACM QLINALVTSP DELDFRLHIR NEFMRCGLKE ILPQLLVIRN EALDIQLKVF
EEHKEEDMME FSHRLEDIRS ELEYPFKTRI SFISLPSFLR EIALLTLKYK SLTRCTDAGD
VFSIVQSMVK DSSAEPYFIS ILQHLVLIRN DHLIRPQYFK IIEECVSQIV LHRSGTDPDF
SYRKRLDVDF SHLLEVCVDK SRIDEYEQRA SELAQKFDEE FLSRQEAQAQ LVKCEEKIAE
LQAELQAFRS QALSSSTIPS GVPSPAPASL GPVPPPPPPP PPLPGCPAPP PPPGMPPPFG
APPPPPLGFG GGLGSPTHHT LPYGLRPKKE FKPETSMKRL NWSKIRPQEM SEGCFWVRVD
EDQYAKPDLL NRVALTFGSQ RTAKKEEDDT EDKKSIKKRI KELKVLDPKI AQNLSIFLGS
FRIPYQEIRR MIVEVDEEQL SEPMIQNLVK HLPEQEQLNA LATYKNEYSN LSEPEQFGVV
MSSVKRLRPR LSHILFRLQF EEHVNNLRPD ILAVNAACDE VRKSRSFGRL LELVLLLGNY
MNAGSRNAQS YGFDLSSLCK LKDTKSADQK TTLLHFLAQV CEEEFPDVVK FLDDLEHVDR
ASRVSAENLE KSLRQMERQL LQLERDLETF SSSDDPNDMF LTKMAISFTR VFAREQYDKL
VIMHGNMETL YQNLLEYFAI DPKKTSVEEL FTDLSNFRSM FTQALKENFR QRETEEKQRR
ARAAKEKAER EKRERQQKKR RLLEVNAEND ETGVMDSLLE ALQSGAAFRD RRKRAPRPRG
NHHQTISPSS FRQVLRPVNY GKNTRSKNC
//
