DIAP3_HUMAN
ID DIAP3_HUMAN Reviewed; 1193 AA.
AC Q9NSV4; A2A3B8; A2A3B9; A2A3C0; Q18P99; Q18PA0; Q18PA1; Q2KPB6; Q3ZK23;
AC Q5JTP8; Q5T2S7; Q5XKF6; Q6MZF0; Q6NUP0; Q86VS4; Q8NAV4;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 4.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Protein diaphanous homolog 3;
DE AltName: Full=Diaphanous-related formin-3;
DE Short=DRF3;
DE AltName: Full=MDia2;
GN Name=DIAPH3; Synonyms=DIAP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Mao M., Ward T., Schimmack G., Linsley P.S.;
RT "Homo sapiens diaphanous homolog 3 (DIAPH3) mRNA.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
RA Khoury J., Freeman M.R.;
RT "Identification and analysis of DIAPH3 as an EGF-dependent lipid raft
RT complex in LNCaP prostate cancer cells.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6).
RA Yasuda S., Narumiya S.;
RT "Control of mitotic spindle orientation by mDia-mediated actin fibers.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-669 (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-699 (ISOFORM 3).
RC TISSUE=Mesangial cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18755006; DOI=10.1111/j.1365-2818.2008.02063.x;
RA Block J., Stradal T.E., Hanisch J., Geffers R., Kostler S.A., Urban E.,
RA Small J.V., Rottner K., Faix J.;
RT "Filopodia formation induced by active mDia2/Drf3.";
RL J. Microsc. 231:506-517(2008).
RN [9]
RP SUBCELLULAR LOCATION, UBIQUITINATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19457867; DOI=10.1074/jbc.m109.000885;
RA DeWard A.D., Alberts A.S.;
RT "Ubiquitin-mediated degradation of the formin mDia2 upon completion of cell
RT division.";
RL J. Biol. Chem. 284:20061-20069(2009).
RN [10]
RP INVOLVEMENT IN AUNA1.
RX PubMed=20624953; DOI=10.1073/pnas.1003027107;
RA Schoen C.J., Emery S.B., Thorne M.C., Ammana H.R., Sliwerska E., Arnett J.,
RA Hortsch M., Hannan F., Burmeister M., Lesperance M.M.;
RT "Increased activity of Diaphanous homolog 3 (DIAPH3)/diaphanous causes
RT hearing defects in humans with auditory neuropathy and in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13396-13401(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; THR-68; SER-77; SER-175;
RP SER-1093 AND SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Actin nucleation and elongation factor required for the
CC assembly of F-actin structures, such as actin cables and stress fibers.
CC Required for cytokinesis, stress fiber formation and transcriptional
CC activation of the serum response factor. Binds to GTP-bound form of Rho
CC and to profilin: acts in a Rho-dependent manner to recruit profilin to
CC the membrane, where it promotes actin polymerization. DFR proteins
CC couple Rho and Src tyrosine kinase during signaling and the regulation
CC of actin dynamics. Also acts as an actin nucleation and elongation
CC factor in the nucleus by promoting nuclear actin polymerization inside
CC the nucleus to drive serum-dependent SRF-MRTFA activity.
CC {ECO:0000250|UniProtKB:Q9Z207}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18755006,
CC ECO:0000269|PubMed:19457867}. Nucleus {ECO:0000250|UniProtKB:Q9Z207}.
CC Note=During mitosis, co-localizes with the actin-rich cleavage furrow
CC and with the microtubule-rich central spindle during cytokinesis
CC (PubMed:18755006, PubMed:19457867). Shuttles between the cytoplasm and
CC the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9Z207,
CC ECO:0000269|PubMed:18755006, ECO:0000269|PubMed:19457867}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=3;
CC IsoId=Q9NSV4-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9NSV4-1; Sequence=VSP_015958, VSP_027777, VSP_027778;
CC Name=2;
CC IsoId=Q9NSV4-2; Sequence=VSP_015958, VSP_001574, VSP_001575;
CC Name=4;
CC IsoId=Q9NSV4-4; Sequence=VSP_027774;
CC Name=5;
CC IsoId=Q9NSV4-5; Sequence=VSP_027774, VSP_027776;
CC Name=6;
CC IsoId=Q9NSV4-6; Sequence=VSP_027774, VSP_027775;
CC Name=7;
CC IsoId=Q9NSV4-7; Sequence=VSP_027777, VSP_027778;
CC -!- DEVELOPMENTAL STAGE: Increased expression in S phase and mitotic cells;
CC levels decrease as cells enter in G0/G1 phase due to proteasomal
CC degradation (at protein level). {ECO:0000269|PubMed:19457867}.
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:0000250|UniProtKB:Q9Z207}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:19457867}.
CC -!- DISEASE: Auditory neuropathy, autosomal dominant, 1 (AUNA1)
CC [MIM:609129]: A form of sensorineural hearing loss with absent or
CC severely abnormal auditory brainstem response, in the presence of
CC normal cochlear outer hair cell function and normal otoacoustic
CC emissions. Auditory neuropathies result from a lesion in the area
CC including the inner hair cells, connections between the inner hair
CC cells and the cochlear branch of the auditory nerve, the auditory nerve
CC itself and auditory pathways of the brainstem.
CC {ECO:0000269|PubMed:20624953}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. A disease-causing
CC mutation in the conserved 5'-UTR leads to increased protein expression.
CC {ECO:0000269|PubMed:20624953}.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW73254.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY750055; AAW73254.1; ALT_FRAME; mRNA.
DR EMBL; AY818645; AAW78862.1; -; mRNA.
DR EMBL; AB244756; BAE96350.1; -; mRNA.
DR EMBL; AB244757; BAE96351.1; -; mRNA.
DR EMBL; AB244758; BAE96352.1; -; mRNA.
DR EMBL; AL137718; CAB70890.1; -; mRNA.
DR EMBL; BX649186; CAE46204.1; -; mRNA.
DR EMBL; AL354829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034952; AAH34952.1; -; mRNA.
DR EMBL; BC048963; AAH48963.1; -; mRNA.
DR EMBL; BC068504; AAH68504.1; -; mRNA.
DR EMBL; AK092024; BAC03793.1; -; mRNA.
DR CCDS; CCDS41898.1; -. [Q9NSV4-3]
DR CCDS; CCDS58294.1; -. [Q9NSV4-6]
DR CCDS; CCDS58295.1; -. [Q9NSV4-5]
DR CCDS; CCDS58296.1; -. [Q9NSV4-4]
DR CCDS; CCDS58297.1; -. [Q9NSV4-7]
DR CCDS; CCDS73579.1; -. [Q9NSV4-2]
DR CCDS; CCDS73580.1; -. [Q9NSV4-1]
DR RefSeq; NP_001035982.1; NM_001042517.1. [Q9NSV4-3]
DR RefSeq; NP_001245295.1; NM_001258366.1. [Q9NSV4-4]
DR RefSeq; NP_001245296.1; NM_001258367.1. [Q9NSV4-5]
DR RefSeq; NP_001245297.1; NM_001258368.1. [Q9NSV4-6]
DR RefSeq; NP_001245298.1; NM_001258369.1. [Q9NSV4-7]
DR RefSeq; NP_001245299.1; NM_001258370.1. [Q9NSV4-2]
DR RefSeq; NP_112194.2; NM_030932.3. [Q9NSV4-1]
DR PDB; 5UWP; X-ray; 2.05 A; D=1179-1193.
DR PDB; 6X2Y; X-ray; 2.30 A; D=1183-1193.
DR PDBsum; 5UWP; -.
DR PDBsum; 6X2Y; -.
DR AlphaFoldDB; Q9NSV4; -.
DR SMR; Q9NSV4; -.
DR BioGRID; 123559; 99.
DR IntAct; Q9NSV4; 27.
DR MINT; Q9NSV4; -.
DR STRING; 9606.ENSP00000383178; -.
DR GlyGen; Q9NSV4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NSV4; -.
DR PhosphoSitePlus; Q9NSV4; -.
DR BioMuta; DIAPH3; -.
DR DMDM; 158520000; -.
DR EPD; Q9NSV4; -.
DR jPOST; Q9NSV4; -.
DR MassIVE; Q9NSV4; -.
DR MaxQB; Q9NSV4; -.
DR PaxDb; Q9NSV4; -.
DR PeptideAtlas; Q9NSV4; -.
DR PRIDE; Q9NSV4; -.
DR ProteomicsDB; 82583; -. [Q9NSV4-3]
DR ProteomicsDB; 82584; -. [Q9NSV4-1]
DR ProteomicsDB; 82585; -. [Q9NSV4-2]
DR ProteomicsDB; 82586; -. [Q9NSV4-4]
DR ProteomicsDB; 82587; -. [Q9NSV4-5]
DR ProteomicsDB; 82588; -. [Q9NSV4-6]
DR ProteomicsDB; 82589; -. [Q9NSV4-7]
DR Antibodypedia; 24286; 270 antibodies from 30 providers.
DR DNASU; 81624; -.
DR Ensembl; ENST00000267215.8; ENSP00000267215.4; ENSG00000139734.19. [Q9NSV4-7]
DR Ensembl; ENST00000377908.6; ENSP00000367141.2; ENSG00000139734.19. [Q9NSV4-4]
DR Ensembl; ENST00000400319.5; ENSP00000383173.1; ENSG00000139734.19. [Q9NSV4-6]
DR Ensembl; ENST00000400320.5; ENSP00000383174.1; ENSG00000139734.19. [Q9NSV4-5]
DR Ensembl; ENST00000400324.9; ENSP00000383178.3; ENSG00000139734.19. [Q9NSV4-3]
DR Ensembl; ENST00000465066.5; ENSP00000478137.1; ENSG00000139734.19. [Q9NSV4-1]
DR Ensembl; ENST00000498416.2; ENSP00000479091.1; ENSG00000139734.19. [Q9NSV4-2]
DR GeneID; 81624; -.
DR KEGG; hsa:81624; -.
DR MANE-Select; ENST00000400324.9; ENSP00000383178.3; NM_001042517.2; NP_001035982.1.
DR UCSC; uc001vht.6; human. [Q9NSV4-3]
DR CTD; 81624; -.
DR DisGeNET; 81624; -.
DR GeneCards; DIAPH3; -.
DR HGNC; HGNC:15480; DIAPH3.
DR HPA; ENSG00000139734; Tissue enhanced (bone marrow, testis).
DR MalaCards; DIAPH3; -.
DR MIM; 609129; phenotype.
DR MIM; 614567; gene.
DR neXtProt; NX_Q9NSV4; -.
DR OpenTargets; ENSG00000139734; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR PharmGKB; PA27335; -.
DR VEuPathDB; HostDB:ENSG00000139734; -.
DR eggNOG; KOG1924; Eukaryota.
DR GeneTree; ENSGT00940000157767; -.
DR HOGENOM; CLU_002356_0_0_1; -.
DR InParanoid; Q9NSV4; -.
DR OMA; WEVKNPM; -.
DR PhylomeDB; Q9NSV4; -.
DR TreeFam; TF315383; -.
DR PathwayCommons; Q9NSV4; -.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q9NSV4; -.
DR BioGRID-ORCS; 81624; 57 hits in 1087 CRISPR screens.
DR ChiTaRS; DIAPH3; human.
DR GenomeRNAi; 81624; -.
DR Pharos; Q9NSV4; Tbio.
DR PRO; PR:Q9NSV4; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9NSV4; protein.
DR Bgee; ENSG00000139734; Expressed in sperm and 129 other tissues.
DR Genevisible; Q9NSV4; HS.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR Gene3D; 1.10.20.40; -; 1.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 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; IPR027654; Formin_DIAPH3.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45691:SF9; PTHR45691:SF9; 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; SSF48371; 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; Alternative splicing; Coiled coil; Cytoplasm; Deafness;
KW Neuropathy; Non-syndromic deafness; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1193
FT /note="Protein diaphanous homolog 3"
FT /id="PRO_0000194897"
FT DOMAIN 114..476
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 561..631
FT /note="FH1"
FT DOMAIN 636..1034
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1057..1087
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 497..554
FT /evidence="ECO:0000255"
FT COILED 1013..1056
FT /evidence="ECO:0000255"
FT MOTIF 36..60
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9Z207"
FT MOTIF 1184..1193
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9Z207"
FT COMPBIAS 573..621
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 68
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..263
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_015958"
FT VAR_SEQ 61..71
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_027774"
FT VAR_SEQ 72..130
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_027775"
FT VAR_SEQ 131..165
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_027776"
FT VAR_SEQ 913..956
FT /note="VSVETLEKNLRQMGRQLQQLEKELETFPPPEDLHDKFVTKMSRF -> GLCL
FT FKKHFMALIFSAKRLKIIPFICMYFPLSHSVFIPNISF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_001574"
FT VAR_SEQ 957..1193
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_001575"
FT VAR_SEQ 1107..1112
FT /note="ENQKVQ -> GNKPYL (in isoform 7 and isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_027777"
FT VAR_SEQ 1113..1193
FT /note="Missing (in isoform 7 and isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_027778"
FT VARIANT 363
FT /note="N -> S (in dbSNP:rs36084898)"
FT /id="VAR_049097"
FT VARIANT 773
FT /note="F -> L (in dbSNP:rs35579086)"
FT /id="VAR_049098"
FT VARIANT 1041
FT /note="E -> G (in dbSNP:rs7491389)"
FT /id="VAR_049099"
FT CONFLICT 55
FT /note="E -> G (in Ref. 3; BAE96352)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="K -> R (in Ref. 7; BAC03793)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> V (in Ref. 6; AAH34952)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="L -> P (in Ref. 3; BAE96351)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="P -> L (in Ref. 7; BAC03793)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="P -> L (in Ref. 3; BAE96351)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="N -> K (in Ref. 4; CAE46204)"
FT /evidence="ECO:0000305"
FT HELIX 1184..1191
FT /evidence="ECO:0007829|PDB:5UWP"
SQ SEQUENCE 1193 AA; 136926 MW; ABCA4E859873F9E7 CRC64;
MERHQPRLHH PAQGSAAGTP YPSSASLRGC RESKMPRRKG PQHPPPPSGP EEPGEKRPKF
HLNIRTLTDD MLDKFASIRI PGSKKERPPL PNLKTAFASS DCSAAPLEMM ENFPKPLSEN
ELLELFEKMM EDMNLNEDKK APLREKDFSI KKEMVMQYIN TASKTGSLKR SRQISPQEFI
HELKMGSADE RLVTCLESLR VSLTSNPVSW VESFGHEGLG LLLDILEKLI SGKIQEKVVK
KNQHKVIQCL KALMNTQYGL ERIMSEERSL SLLAKAVDPR HPNMMTDVVK LLSAVCIVGE
ESILEEVLEA LTSAGEEKKI DRFFCIVEGL RHNSVQLQVA CMQLINALVT SPDDLDFRLH
IRNEFMRCGL KEILPNLKCI KNDGLDIQLK VFDEHKEEDL FELSHRLEDI RAELDEAYDV
YNMVWSTVKE TRAEGYFISI LQHLLLIRND YFIRQQYFKL IDECVSQIVL HRDGMDPDFT
YRKRLDLDLT QFVDICIDQA KLEEFEEKAS ELYKKFEKEF TDHQETQAEL QKKEAKINEL
QAELQAFKSQ FGALPADCNI PLPPSKEGGT GHSALPPPPP LPSGGGVPPP PPPPPPPPLP
GMRMPFSGPV PPPPPLGFLG GQNSPPLPIL PFGLKPKKEF KPEISMRRLN WLKIRPHEMT
ENCFWIKVNE NKYENVDLLC KLENTFCCQQ KERREEEDIE EKKSIKKKIK ELKFLDSKIA
QNLSIFLSSF RVPYEEIRMM ILEVDETRLA ESMIQNLIKH LPDQEQLNSL SQFKSEYSNL
CEPEQFVVVM SNVKRLRPRL SAILFKLQFE EQVNNIKPDI MAVSTACEEI KKSKSFSKLL
ELVLLMGNYM NAGSRNAQTF GFNLSSLCKL KDTKSADQKT TLLHFLVEIC EEKYPDILNF
VDDLEPLDKA SKVSVETLEK NLRQMGRQLQ QLEKELETFP PPEDLHDKFV TKMSRFVISA
KEQYETLSKL HENMEKLYQS IIGYYAIDVK KVSVEDFLTD LNNFRTTFMQ AIKENIKKRE
AEEKEKRVRI AKELAERERL ERQQKKKRLL EMKTEGDETG VMDNLLEALQ SGAAFRDRRK
RTPMPKDVRQ SLSPMSQRPV LKVCNHENQK VQLTEGSRSH YNINCNSTRT PVAKELNYNL
DTHTSTGRIK AAEKKEACNV ESNRKKETEL LGSFSKNESV PEVEALLARL RAL
