ID A0A3B3C8N3_ORYME Unreviewed; 1196 AA.
AC A0A3B3C8N3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Diaphanous related formin 3 {ECO:0000313|Ensembl:ENSOMEP00000014286.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000014286.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000014286.1}
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; A0A3B3C8N3; -.
DR Ensembl; ENSOMET00000022141.1; ENSOMEP00000014286.1; ENSOMEG00000015857.1.
DR GeneTree; ENSGT00940000157767; -.
DR Proteomes; UP000261560; Unplaced.
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; 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}.
FT DOMAIN 84..446
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 596..1005
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1028..1058
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 989..1026
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1196 AA; 136254 MW; FBD14CBC1E9C36FC CRC64;
MDSYSQRFET STVGREGKPQ KKKGHHASYY DDGERKPKFL DRFASIRIPG SKKERPPLTL
SKSNTSDWST TSSTTLHHFE EVSSKITSEK EILAMFEKMM EDMNLNEDKK APLREKDLNT
KREMVIQYIF AASKTGNLRN SHQISPQEFL CELKSGVMDE RLFACLDSLR VSLTSNPVSW
VQSFGHEGLG LLLDILERLL FKKLQEKIDK KNQHKVVQCL KAFMNNKYGL DRILGEERSL
GLLARAIDPT HSAMMTDVVK LLSAICIVGE ENTLEKILEA ITTAGEWRSI ERFSPIVQGL
RDRSVQLQVA CMQLINALVT SPDELDFRLH IRNEFMRCGL KEILPQLATI RNEALDIQLK
VFEEHKEEDM MEFSHRLEDI RSELDDAGDV FGIVQSMVKD TNAEPYFLSI LQHLALIRND
YLVRPQYFKI IEECISQIVL HRSGTDPDFS YRKRLDVDFS HLLEVCTDKA RIDEFEQRAS
ELAQKFDEEF LRRQEAQAEL GKCEEKIAEL QTELQAFRTQ GGQPSSSSTT PVAGSSVPGP
PPPPPPPPPP PPSGCPPAPP PPGPPPPLGI PPPPPLVFGG AFGSPTPDTL PYGLRPKKEF
KLETSMKRLN WSKIRPQEMS EGCFWVRADE NQYSKPELLN RVAVTFGSQR TDCEESVPTE
EQIKKEEEDM EDKKSIKKRI KELKVLDPKI AQNLSIFLGS FRMPYEEIRR MIVEVDEEQL
TEPMIQNLVK HLPEQDQLNA LAKYKNEYSS LSEPEQFGVV MSTVKRLRPR LSHILFRLQF
EEQINNLRPD ILAVNAACEE VRRSCSFGRL LELVLLLGNY MNAGSRNAQS YGFDLSSLCK
LKDTKSADQK TTLLHFLAQI CEEEFPDVIK FVDDLEHVDR ASRVSAENVE KSLRQMERQL
LQLERDLETF SSPDDQSDMF FVKMASFSKG AREQYSKLVI MHSKMETSYQ NILEYFAVDP
KKTSVEELFT DLSNFRSMFT QALKENFRQR ELEEKQRRAR VAKEKAEREK LERQQKKRRL
LEVNAENDET GVMDCLLEAL QSGAAFRDRR KRAPRPRENK QQTISPSSFR QVLRPVNYEN
NKPPIQRSCS RPNVNASLAA AAKASSAKES RNESEGHPSA ARSQASSSLE SGRRNRNPPG
HSYGLERERV VEREVLKGSK KEVEAEALQP SSSAVSSINA NGEPDVEALL AKLRAL
//
