ID DIAP1_MOUSE Reviewed; 1255 AA.
AC O08808;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 24-JAN-2024, entry version 203.
DE RecName: Full=Protein diaphanous homolog 1;
DE AltName: Full=Diaphanous-related formin-1;
DE Short=DRF1;
DE AltName: Full=p140mDIA;
DE Short=mDIA1 {ECO:0000303|PubMed:23558171};
GN Name=Diaph1; Synonyms=Diap1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RHOA, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9214622; DOI=10.1093/emboj/16.11.3044;
RA Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G., Kakizuka A.,
RA Saito Y., Nakao K., Jockusch B.M., Narumiya S.;
RT "p140mDia, a mammalian homolog of Drosophila diaphanous, is a target
RT protein for Rho small GTPase and is a ligand for profilin.";
RL EMBO J. 16:3044-3056(1997).
RN [2]
RP INTERACTION WITH BAIAP2.
RX PubMed=10814512; DOI=10.1006/bbrc.2000.2671;
RA Fujiwara T., Mammoto A., Kim Y., Takai Y.;
RT "Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-
RT containing IRSp53/BAIAP2.";
RL Biochem. Biophys. Res. Commun. 271:626-629(2000).
RN [3]
RP FUNCTION.
RX PubMed=10678165; DOI=10.1016/s1097-2765(00)80399-8;
RA Tominaga T., Sahai E., Chardin P., McCormick F., Courtneidge S.A.,
RA Alberts A.S.;
RT "Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase
RT signaling.";
RL Mol. Cell 5:13-25(2000).
RN [4]
RP FUNCTION, AND INTERACTION WITH APC AND MAPRE1.
RX PubMed=15311282; DOI=10.1038/ncb1160;
RA Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S., Chen M.,
RA Wallar B.J., Alberts A.S., Gundersen G.G.;
RT "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and
RT promote cell migration.";
RL Nat. Cell Biol. 6:820-830(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH ACTIN.
RX PubMed=15044801; DOI=10.1126/science.1093923;
RA Higashida C., Miyoshi T., Fujita A., Oceguera-Yanez F., Monypenny J.,
RA Andou Y., Narumiya S., Watanabe N.;
RT "Actin polymerization-driven molecular movement of mDia1 in living cells.";
RL Science 303:2007-2010(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH NCDN.
RX PubMed=18572016; DOI=10.1016/j.bbrc.2008.06.042;
RA Schwaibold E.M., Brandt D.T.;
RT "Identification of Neurochondrin as a new interaction partner of the FH3
RT domain of the Diaphanous-related formin Dia1.";
RL Biochem. Biophys. Res. Commun. 373:366-372(2008).
RN [9]
RP INTERACTION WITH SCAI.
RX PubMed=19350017; DOI=10.1038/ncb1862;
RA Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P.,
RA Grosse R.;
RT "SCAI acts as a suppressor of cancer cell invasion through the
RT transcriptional control of beta1-integrin.";
RL Nat. Cell Biol. 11:557-568(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23558171; DOI=10.1126/science.1235038;
RA Baarlink C., Wang H., Grosse R.;
RT "Nuclear actin network assembly by formins regulates the SRF coactivator
RT MAL.";
RL Science 340:864-867(2013).
RN [12]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=24781755; DOI=10.1038/ejhg.2014.82;
RA Ercan-Sencicek A.G., Jambi S., Franjic D., Nishimura S., Li M.,
RA El-Fishawy P., Morgan T.M., Sanders S.J., Bilguvar K., Suri M.,
RA Johnson M.H., Gupta A.R., Yuksel Z., Mane S., Grigorenko E., Picciotto M.,
RA Alberts A.S., Gunel M., Sestan N., State M.W.;
RT "Homozygous loss of DIAPH1 is a novel cause of microcephaly in humans.";
RL Eur. J. Hum. Genet. 23:165-172(2015).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=27808407; DOI=10.1111/cge.12915;
RA Neuhaus C., Lang-Roth R., Zimmermann U., Heller R., Eisenberger T.,
RA Weikert M., Markus S., Knipper M., Bolz H.J.;
RT "Extension of the clinical and molecular phenotype of DIAPH1-associated
RT autosomal dominant hearing loss (DFNA1).";
RL Clin. Genet. 91:892-901(2017).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 826-1163, OLIGOMERIZATION, AND
RP INTERACTION WITH ACTIN.
RX PubMed=14992721; DOI=10.1016/s1097-2765(04)00059-0;
RA Shimada A., Nyitrai M., Vetter I.R., Kuehlmann D., Bugyi B., Narumiya S.,
RA Geeves M.A., Wittinghofer A.;
RT "The core FH2 domain of diaphanous-related formins is an elongated actin
RT binding protein that inhibits polymerization.";
RL Mol. Cell 13:511-522(2004).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 135-451 AND 1145-1200, DOMAIN DAD,
RP AND AUTOINHIBITION.
RX PubMed=16292343; DOI=10.1038/sj.emboj.7600879;
RA Lammers M., Rose R., Scrima A., Wittinghofer A.;
RT "The regulation of mDia1 by autoinhibition and its release by Rho*GTP.";
RL EMBO J. 24:4176-4187(2005).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-451 IN COMPLEX WITH RHOC, AND
RP HOMODIMERIZATION.
RX PubMed=15864301; DOI=10.1038/nature03604;
RA Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R.,
RA Wittinghofer A.;
RT "Structural and mechanistic insights into the interaction between Rho and
RT mammalian Dia.";
RL Nature 435:513-518(2005).
CC -!- FUNCTION: Actin nucleation and elongation factor required for the
CC assembly of F-actin structures, such as actin cables and stress fibers
CC (PubMed:10678165, PubMed:15044801, PubMed:18572016, PubMed:23558171).
CC Binds to the barbed end of the actin filament and slows down actin
CC polymerization and depolymerization (PubMed:10678165, PubMed:15044801,
CC PubMed:18572016). Required for cytokinesis, and transcriptional
CC activation of the serum response factor (PubMed:10678165,
CC PubMed:15044801, PubMed:18572016). DFR proteins couple Rho and Src
CC tyrosine kinase during signaling and the regulation of actin dynamics
CC (PubMed:10678165, PubMed:15044801, PubMed:18572016). Functions as a
CC scaffold protein for MAPRE1 and APC to stabilize microtubules and
CC promote cell migration (PubMed:15311282). Has neurite outgrowth
CC promoting activity (PubMed:10678165, PubMed:15044801, PubMed:18572016).
CC Acts in a Rho-dependent manner to recruit PFY1 to the membrane
CC (PubMed:9214622). The MEMO1-RHOA-DIAPH1 signaling pathway plays an
CC important role in ERBB2-dependent stabilization of microtubules at the
CC cell cortex (By similarity). It controls the localization of APC and
CC CLASP2 to the cell membrane, via the regulation of GSK3B activity (By
CC similarity). In turn, membrane-bound APC allows the localization of the
CC MACF1 to the cell membrane, which is required for microtubule capture
CC and stabilization (By similarity). Plays a role in the regulation of
CC cell morphology and cytoskeletal organization (By similarity). Required
CC in the control of cell shape (By similarity). Also acts as an actin
CC nucleation and elongation factor in the nucleus by promoting nuclear
CC actin polymerization inside the nucleus to drive serum-dependent SRF-
CC MRTFA activity (PubMed:23558171). {ECO:0000250|UniProtKB:O60610,
CC ECO:0000269|PubMed:10678165, ECO:0000269|PubMed:15044801,
CC ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:18572016,
CC ECO:0000269|PubMed:23558171, ECO:0000269|PubMed:9214622}.
CC -!- SUBUNIT: Homodimer (PubMed:14992721, PubMed:15864301). Interacts with
CC the GTP-bound form of RHOA (PubMed:9214622). Interacts with RHOC, PFY1,
CC MAPRE1, BAIAP2 and APC (PubMed:10814512, PubMed:15311282,
CC PubMed:15864301). Interacts with APC; acts as a scaffold protein for
CC MAPRE1 and APC to stabilize microtubules and promote cell migration
CC (PubMed:15311282). Interacts with SCAI (PubMed:19350017). Interacts
CC with DCAF7, via FH2 domain (By similarity). Interacts with NCDN
CC (PubMed:18572016). Interacts with OSBPL10, OSBPL2, VIM, TUBB and DYN1
CC (By similarity). {ECO:0000250|UniProtKB:O60610,
CC ECO:0000269|PubMed:10814512, ECO:0000269|PubMed:14992721,
CC ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:15864301,
CC ECO:0000269|PubMed:18572016, ECO:0000269|PubMed:19350017,
CC ECO:0000269|PubMed:9214622}.
CC -!- INTERACTION:
CC O08808; Q8BKX1: Baiap2; NbExp=3; IntAct=EBI-1026445, EBI-771498;
CC O08808; O08808: Diaph1; NbExp=9; IntAct=EBI-1026445, EBI-1026445;
CC O08808; P46940: IQGAP1; Xeno; NbExp=8; IntAct=EBI-1026445, EBI-297509;
CC O08808; P61586: RHOA; Xeno; NbExp=3; IntAct=EBI-1026445, EBI-446668;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9214622}. Cell
CC projection, ruffle membrane {ECO:0000269|PubMed:9214622}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:9214622}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:O60610}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:O60610}. Cytoplasm
CC {ECO:0000269|PubMed:23558171}. Nucleus {ECO:0000269|PubMed:23558171}.
CC Note=Membrane ruffles, especially at the tip of ruffles, of motile
CC cells. {ECO:0000269|PubMed:9214622}.
CC -!- TISSUE SPECIFICITY: Widely expressed. In the organ of Corti, it is
CC expressed at the outer and inner hair cell layers. Expression at the
CC inner hair cell layer is restricted to inner pillar cells. Detected in
CC cochlear spiral ganglion neurons (PubMed:27808407).
CC {ECO:0000269|PubMed:27808407}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the ventricular and subventricular
CC zone progenitor cells of the dorsal and ventral forebrain and the
CC brainstem, at 12.5 dpc, 14.5 dpc, and 17.5 dpc. At later embryonic age,
CC it is observed in neurons of the cortex and hippocampus. During
CC postnatal development, expression is detected in the cerebral cortex,
CC basal ganglia, hippocampus, thalamus, and external granular layer of
CC the cerebellum. {ECO:0000269|PubMed:24781755}.
CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC interaction with the GBD/FH3 domain. This autoinhibition is released
CC upon competitive binding of an activated GTPase. The release of DAD
CC allows the FH2 domain to then nucleate and elongate nonbranched actin
CC filaments. {ECO:0000269|PubMed:16292343}.
CC -!- PTM: Phosphorylation at Thr-751 is stimulated by cAMP and regulates
CC stability, complex formation and mitochondrial movement (By
CC similarity). {ECO:0000250|UniProtKB:O60610}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice show normal organization of the
CC cerebral cortex with no significant differences in cortical white
CC matter or callosal thickness (PubMed:24781755). Histological analysis
CC of coronal brain sections at early and postnatal stages shows
CC unilateral ventricular enlargement (PubMed:24781755).
CC {ECO:0000269|PubMed:24781755}.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000305}.
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DR EMBL; U96963; AAC53280.1; -; mRNA.
DR CCDS; CCDS57121.1; -.
DR PIR; T31065; T31065.
DR RefSeq; NP_031884.1; NM_007858.4.
DR PDB; 1V9D; X-ray; 2.60 A; A/B/C/D=826-1163.
DR PDB; 1Z2C; X-ray; 3.00 A; B/D=69-451.
DR PDB; 2BAP; X-ray; 3.30 A; A/B=135-451, C/D=1145-1200.
DR PDB; 2BNX; X-ray; 2.40 A; A/B=131-516.
DR PDB; 2F31; X-ray; 2.10 A; A=135-367, B=1177-1196.
DR PDB; 2V8F; X-ray; 1.10 A; C=635-655.
DR PDB; 3EG5; X-ray; 2.70 A; B/D=69-451.
DR PDB; 3O4X; X-ray; 3.20 A; A/B/C/D=131-458, E/F/G/H=736-1200.
DR PDB; 3OBV; X-ray; 2.75 A; A/B/C/D=131-457, E/F/G/H=753-1209.
DR PDB; 4UWX; X-ray; 1.65 A; A/B=135-369.
DR PDBsum; 1V9D; -.
DR PDBsum; 1Z2C; -.
DR PDBsum; 2BAP; -.
DR PDBsum; 2BNX; -.
DR PDBsum; 2F31; -.
DR PDBsum; 2V8F; -.
DR PDBsum; 3EG5; -.
DR PDBsum; 3O4X; -.
DR PDBsum; 3OBV; -.
DR PDBsum; 4UWX; -.
DR AlphaFoldDB; O08808; -.
DR SMR; O08808; -.
DR BioGRID; 199221; 19.
DR CORUM; O08808; -.
DR DIP; DIP-29028N; -.
DR IntAct; O08808; 16.
DR STRING; 10090.ENSMUSP00000025337; -.
DR iPTMnet; O08808; -.
DR PhosphoSitePlus; O08808; -.
DR EPD; O08808; -.
DR jPOST; O08808; -.
DR MaxQB; O08808; -.
DR PaxDb; 10090-ENSMUSP00000025337; -.
DR ProteomicsDB; 279658; -.
DR Pumba; O08808; -.
DR Antibodypedia; 7674; 421 antibodies from 41 providers.
DR DNASU; 13367; -.
DR Ensembl; ENSMUST00000115634.8; ENSMUSP00000111297.2; ENSMUSG00000024456.17.
DR GeneID; 13367; -.
DR KEGG; mmu:13367; -.
DR UCSC; uc033hgk.1; mouse.
DR AGR; MGI:1194490; -.
DR CTD; 1729; -.
DR MGI; MGI:1194490; Diaph1.
DR VEuPathDB; HostDB:ENSMUSG00000024456; -.
DR eggNOG; KOG1924; Eukaryota.
DR GeneTree; ENSGT00940000159910; -.
DR InParanoid; O08808; -.
DR OrthoDB; 1118745at2759; -.
DR PhylomeDB; O08808; -.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 13367; 6 hits in 47 CRISPR screens.
DR ChiTaRS; Diaph1; mouse.
DR EvolutionaryTrace; O08808; -.
DR PRO; PR:O08808; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; O08808; Protein.
DR Bgee; ENSMUSG00000024456; Expressed in granulocyte and 259 other cell types or tissues.
DR ExpressionAtlas; O08808; baseline and differential.
DR Genevisible; O08808; MM.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0032587; C:ruffle membrane; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005522; F:profilin binding; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0045010; P:actin nucleation; IDA:MGI.
DR GO; GO:0016199; P:axon midline choice point recognition; IGI:MGI.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0071420; P:cellular response to histamine; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IGI:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0071965; P:multicellular organismal locomotion; IGI:MGI.
DR GO; GO:0070571; P:negative regulation of neuron projection regeneration; IGI:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
DR GO; GO:0106028; P:neuron projection retraction; IGI:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IGI:MGI.
DR GO; GO:0035372; P:protein localization to microtubule; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISO:MGI.
DR GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
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; PF06346; Drf_FH1; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Hearing; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1255
FT /note="Protein diaphanous homolog 1"
FT /id="PRO_0000194894"
FT DOMAIN 75..440
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 586..747
FT /note="FH1"
FT DOMAIN 752..1154
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1177..1205
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..562
FT /evidence="ECO:0000255"
FT COILED 1027..1179
FT /evidence="ECO:0000255"
FT COMPBIAS 12..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
FT MOD_RES 751
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
FT MOD_RES 1040
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
FT MOD_RES 1086
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
FT MOD_RES 1104
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60610"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:3EG5"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:3EG5"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:3EG5"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:4UWX"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 168..191
FT /evidence="ECO:0007829|PDB:4UWX"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:2BNX"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:4UWX"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 244..258
FT /evidence="ECO:0007829|PDB:4UWX"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 266..281
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 299..313
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 319..332
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 347..367
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 381..392
FT /evidence="ECO:0007829|PDB:2BNX"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2BAP"
FT HELIX 397..408
FT /evidence="ECO:0007829|PDB:2BNX"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:2BNX"
FT HELIX 418..433
FT /evidence="ECO:0007829|PDB:2BNX"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:2BNX"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:3OBV"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:2BNX"
FT HELIX 457..461
FT /evidence="ECO:0007829|PDB:2BNX"
FT HELIX 464..469
FT /evidence="ECO:0007829|PDB:2BNX"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:2BNX"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:3O4X"
FT TURN 772..775
FT /evidence="ECO:0007829|PDB:3OBV"
FT STRAND 777..780
FT /evidence="ECO:0007829|PDB:3OBV"
FT HELIX 781..783
FT /evidence="ECO:0007829|PDB:3OBV"
FT HELIX 786..789
FT /evidence="ECO:0007829|PDB:3OBV"
FT HELIX 794..801
FT /evidence="ECO:0007829|PDB:3OBV"
FT STRAND 833..835
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 837..850
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 854..863
FT /evidence="ECO:0007829|PDB:1V9D"
FT TURN 866..868
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 871..880
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 884..891
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 894..899
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 902..911
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 916..934
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 937..951
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 954..958
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 961..968
FT /evidence="ECO:0007829|PDB:1V9D"
FT STRAND 972..974
FT /evidence="ECO:0007829|PDB:1V9D"
FT TURN 975..978
FT /evidence="ECO:0007829|PDB:1V9D"
FT STRAND 980..982
FT /evidence="ECO:0007829|PDB:3O4X"
FT HELIX 984..986
FT /evidence="ECO:0007829|PDB:3OBV"
FT HELIX 987..992
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 1002..1012
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 1015..1019
FT /evidence="ECO:0007829|PDB:3OBV"
FT HELIX 1020..1023
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 1027..1032
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 1035..1057
FT /evidence="ECO:0007829|PDB:1V9D"
FT STRAND 1063..1066
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 1069..1104
FT /evidence="ECO:0007829|PDB:1V9D"
FT TURN 1109..1111
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 1114..1159
FT /evidence="ECO:0007829|PDB:1V9D"
FT HELIX 1181..1191
FT /evidence="ECO:0007829|PDB:2F31"
SQ SEQUENCE 1255 AA; 139343 MW; 09404164873CA7C1 CRC64;
MEPSGGGLGP GRGTRDKKKG RSPDELPATG GDGGKHKKFL ERFTSMRIKK EKEKPNSAHR
NSSASYGDDP TAQSLQDISD EQVLVLFEQM LVDMNLNEEK QQPLREKDIV IKREMVSQYL
HTSKAGMNQK ESSRSAMMYI QELRSGLRDM HLLSCLESLR VSLNNNPVSW VQTFGAEGLA
SLLDILKRLH DEKEETSGNY DSRNQHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD
PAVPNMMIDA AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTSIA
LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQE LREIENEDMK VQLCVFDEQG
DEDFFDLKGR LDDIRMEMDD FGEVFQIILN TVKDSKAEPH FLSILQHLLL VRNDYEARPQ
YYKLIEECVS QIVLHKNGTD PDFKCRHLQI DIERLVDQMI DKTKVEKSEA KATELEKKLD
SELTARHELQ VEMKKMENDF EQKLQDLQGE KDALDSEKQQ ITAQKQDLEA EVSKLTGEVA
KLSKELEDAK NEMASLSAVV VAPSVSSSAA VPPAPPLPGD SGTVIPPPPP PPPLPGGVVP
PSPPLPPGTC IPPPPPLPGG ACIPPPPQLP GSAAIPPPPP LPGVASIPPP PPLPGATAIP
PPPPLPGATA IPPPPPLPGG TGIPPPPPPL PGSVGVPPPP PLPGGPGLPP PPPPFPGAPG
IPPPPPGMGV PPPPPFGFGV PAAPVLPFGL TPKKVYKPEV QLRRPNWSKF VAEDLSQDCF
WTKVKEDRFE NNELFAKLTL AFSAQTKTSK AKKDQEGGEE KKSVQKKKVK ELKVLDSKTA
QNLSIFLGSF RMPYQEIKNV ILEVNEAVLT ESMIQNLIKQ MPEPEQLKML SELKEEYDDL
AESEQFGVVM GTVPRLRPRL NAILFKLQFS EQVENIKPEI VSVTAACEEL RKSENFSSLL
ELTLLVGNYM NAGSRNAGAF GFNISFLCKL RDTKSADQKM TLLHFLAELC ENDHPEVLKF
PDELAHVEKA SRVSAENLQK SLDQMKKQIA DVERDVQNFP AATDEKDKFV EKMTSFVKDA
QEQYNKLRMM HSNMETLYKE LGDYFVFDPK KLSVEEFFMD LHNFRNMFLQ AVKENQKRRE
TEEKMRRAKL AKEKAEKERL EKQQKREQLI DMNAEGDETG VMDSLLEALQ SGAAFRRKRG
PRQVNRKAGC AVTSLLASEL TKDDAMAPGP VKVPKKSEGV PTILEEAKEL VGRAS
//
