ID A0A3B4UJC8_SERDU Unreviewed; 1140 AA.
AC A0A3B4UJC8;
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=Protein diaphanous homolog 1-like {ECO:0000313|Ensembl:ENSSDUP00000018689.1};
GN Name=DIAPH1 {ECO:0000313|Ensembl:ENSSDUP00000018689.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000018689.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000018689.1}
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; A0A3B4UJC8; -.
DR Ensembl; ENSSDUT00000019024.1; ENSSDUP00000018689.1; ENSSDUG00000013578.1.
DR GeneTree; ENSGT00940000159910; -.
DR Proteomes; UP000261420; 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; 1.20.1170.10; -; 1.
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:SF4; PROTEIN DIAPHANOUS HOMOLOG 1; 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 57..424
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 681..1083
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1105..1133
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1053..1101
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..680
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 128306 MW; 69FF98D886521345 CRC64;
MSQKSEKGPS QFPRSQGYLE RFTSMRMKKD KEKPGHMPGQ RHSSAASYEL NPQSAMLHDH
SDEYVLELFE QMLVDMNLNE EKQQPLRAKD IMIKREMVSQ YLHTSKAGQN QKESSKSALV
YIQELKSDSR DTQLLGCLES LRVSLNNNPV SWVQNFGDEG LALLLNLLRK LQDEKDEMIG
VKCQHEIIRC LKAFMNNKYG LKSMLESDEG IPLLVRAINP AVPHMMVDAV KLLSAISILQ
HSENLHERVL EAITEEAERR DIERFQPLLA GMNNHNIALK GGCMQLINAL ISQGEELDFR
IHIRSELLRL GLRDLLTVRT IENEELRVQL NVFDEQAEDD SEDLKARLDD IRIEMEYPST
GKNVPLEVFE ILVNTVKDSK AESHFLSLMQ HLLLIRSDYY ARPQYYKLID ECIAQIVLHR
NGADPDFKCR NLSLNIEGLI DNMVDQTKVE TSEAKATELG KKLDTELTAR HELQVELKKL
EGDYEQKLRD LSQEKEQLAS SKQEREKENQ GLQQQLSSLN QQIEKLSKDL EEAKTKVVTV
TVPVPTPGLP PPPPAPPLPG QNVGVPPPPP PPPLPGYAAI PFPQPPPPPP LPGQACIPPP
PPPPPLPGMP GPPPPPPLPG MPGPPPPPPL PGMGPPPPPP PPGLPGIPPP PPGPGMPPPP
PFGMGGWGAP APPPLPYGLK PKKDYKPEVQ LKRANWSKIG PEDLSENSFW TKAKEEQFEN
NELFAKLTLT FSSQTKSESK KEQDGGDDKK QPQKKKVKEL KILDSKASQN LSIFLGSFRL
PYEEIKNAIL EVNEKILTES MAQNLVKQLP APEQLSVLGE MKDEYDDLAE SEQFGVVMSS
VKRLMPRLQA ILFKLQFEEQ LNNIKPDVVS VTAACEELRQ SQTFSKLLQI ILLVGNYMNS
GSRNGKAFGF SLSYLCKLRD TKSADLKQTL LHFLADVCQE QYPEIMSFPD ELIHVEKASR
VSAETIQKNL ELMGRQIKNL EKDLETFPPP QNDKDLFAEK ILHSFVISAH EQYEKLDLMH
KNMEKQYTDL GDCFVFDPKK MSVEEFFGDL NTFKNMFQQA VKENQKRKEA EEKIKRAKLA
REKAEKEKEE KLKRNQLLDI NAEDDETGIM DGLLEALQSG AAFRRKRGPR PAGTHTQAGL
//
