Entry euk:DIAP3_HUMAN

ID   DIAP3_HUMAN             Reviewed;        1193 AA.
AC   Q9NSV4; A2A3B8; A2A3B9; A2A3C0; Q18P99; Q18PA0; Q18PA1; Q2KPB6;
AC   Q3ZK23; Q5JTP8; Q5T2S7; Q5XKF6; Q6MZF0; Q6NUP0; Q86VS4; Q8NAV4;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 4.
DT   10-MAY-2017, entry version 162.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   fibers.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.,
RA   Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA   Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA   Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA   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.,
RA   Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA   Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA   Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA   Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA   Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA   Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA   Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA   King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA   Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA   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.,
RA   Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA   Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA   Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA   Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA   Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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
RT   project: 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Urban E., 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
RT   cell 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.,
RA   Arnett J., 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
RT   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
RP   BY 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation 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.,
RA   Buerckstuemmer T., 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;
RP   SER-175; SER-1093 AND SER-1179, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE 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: Binds to GTP-bound form of Rho and to profilin. Acts in
CC       a Rho-dependent manner to recruit profilin to the membrane, where
CC       it promotes actin polymerization. It is required for cytokinesis,
CC       stress fiber formation, and transcriptional activation of the
CC       serum response factor. DFR proteins couple Rho and Src tyrosine
CC       kinase during signaling and the regulation of actin dynamics (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:18755006, ECO:0000269|PubMed:19457867}.
CC       Note=During mitosis, co-localizes with the actin-rich cleavage
CC       furrow and with the microtubule-rich central spindle during
CC       cytokinesis.
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
CC       cells; levels decrease as cells enter in G0/G1 phase due to
CC       proteasomal degradation (at protein level).
CC       {ECO:0000269|PubMed:19457867}.
CC   -!- DOMAIN: The DAD domain regulates activation via by an
CC       autoinhibitory interaction with the GBD/FH3 domain. This
CC       autoinhibition is released upon competitive binding of an
CC       activated GTPase. The release of DAD allows the FH2 domain to then
CC       nucleate and elongate nonbranched actin filaments (By similarity).
CC       {ECO:0000250}.
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
CC       nerve itself and auditory pathways of the brainstem.
CC       {ECO:0000269|PubMed:20624953}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry. A disease-
CC       causing mutation in the conserved 5'-UTR leads to increased
CC       protein expression (PubMed:20624953).
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; Positions=1147; 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; CAI39756.2; -; Genomic_DNA.
DR   EMBL; AL356502; CAI39756.2; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAI39756.2; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAI39756.2; JOINED; Genomic_DNA.
DR   EMBL; AL354829; CAI39757.2; -; Genomic_DNA.
DR   EMBL; AL356502; CAI39757.2; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAI39757.2; JOINED; Genomic_DNA.
DR   EMBL; AL354829; CAM14265.1; -; Genomic_DNA.
DR   EMBL; AL356502; CAM14265.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM14265.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM14265.1; JOINED; Genomic_DNA.
DR   EMBL; AL354829; CAM14266.1; -; Genomic_DNA.
DR   EMBL; AL356502; CAM14266.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM14266.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM14266.1; JOINED; Genomic_DNA.
DR   EMBL; AL354829; CAM14267.1; -; Genomic_DNA.
DR   EMBL; AL356502; CAM14267.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM14267.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM14267.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAI14102.2; -; Genomic_DNA.
DR   EMBL; AL354829; CAI14102.2; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAI14102.2; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAI14102.2; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM19398.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM19398.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM19398.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM19399.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM19399.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM19399.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM19399.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM19400.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM19400.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM19400.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM19400.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM19401.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM19401.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM19401.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM19401.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM15403.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM15403.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM15403.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM15403.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM15404.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM15404.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM15404.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM15404.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM15405.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM15405.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM15405.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM15405.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM15406.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM15406.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM15406.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM15406.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAI14158.2; -; Genomic_DNA.
DR   EMBL; AL354829; CAI14158.2; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAI14158.2; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAI14158.2; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM19738.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM19738.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM19738.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM19739.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM19739.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM19739.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM19739.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM19740.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM19740.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM19740.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM19740.1; JOINED; Genomic_DNA.
DR   EMBL; AL390878; CAM19741.1; -; Genomic_DNA.
DR   EMBL; AL354829; CAM19741.1; JOINED; Genomic_DNA.
DR   EMBL; AL356502; CAM19741.1; JOINED; Genomic_DNA.
DR   EMBL; AL359266; CAM19741.1; JOINED; 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   UniGene; Hs.283127; -.
DR   ProteinModelPortal; Q9NSV4; -.
DR   SMR; Q9NSV4; -.
DR   BioGrid; 123559; 31.
DR   IntAct; Q9NSV4; 11.
DR   MINT; MINT-1195088; -.
DR   STRING; 9606.ENSP00000383178; -.
DR   iPTMnet; Q9NSV4; -.
DR   PhosphoSitePlus; Q9NSV4; -.
DR   BioMuta; DIAPH3; -.
DR   DMDM; 158520000; -.
DR   EPD; Q9NSV4; -.
DR   PaxDb; Q9NSV4; -.
DR   PeptideAtlas; Q9NSV4; -.
DR   PRIDE; Q9NSV4; -.
DR   Ensembl; ENST00000267215; ENSP00000267215; ENSG00000139734. [Q9NSV4-7]
DR   Ensembl; ENST00000377908; ENSP00000367141; ENSG00000139734. [Q9NSV4-4]
DR   Ensembl; ENST00000400319; ENSP00000383173; ENSG00000139734. [Q9NSV4-6]
DR   Ensembl; ENST00000400320; ENSP00000383174; ENSG00000139734. [Q9NSV4-5]
DR   Ensembl; ENST00000400324; ENSP00000383178; ENSG00000139734. [Q9NSV4-3]
DR   Ensembl; ENST00000465066; ENSP00000478137; ENSG00000139734. [Q9NSV4-1]
DR   Ensembl; ENST00000498416; ENSP00000479091; ENSG00000139734. [Q9NSV4-2]
DR   GeneID; 81624; -.
DR   KEGG; hsa:81624; -.
DR   UCSC; uc001vht.6; human. [Q9NSV4-3]
DR   CTD; 81624; -.
DR   DisGeNET; 81624; -.
DR   GeneCards; DIAPH3; -.
DR   H-InvDB; HIX0037336; -.
DR   HGNC; HGNC:15480; DIAPH3.
DR   HPA; HPA032151; -.
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   eggNOG; KOG1924; Eukaryota.
DR   eggNOG; ENOG410Y29H; LUCA.
DR   GeneTree; ENSGT00760000118986; -.
DR   HOVERGEN; HBG051357; -.
DR   InParanoid; Q9NSV4; -.
DR   KO; K05745; -.
DR   OMA; KQMGRQL; -.
DR   OrthoDB; EOG091G0JR0; -.
DR   PhylomeDB; Q9NSV4; -.
DR   TreeFam; TF315383; -.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   ChiTaRS; DIAPH3; human.
DR   GenomeRNAi; 81624; -.
DR   PRO; PR:Q9NSV4; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   Bgee; ENSG00000139734; -.
DR   CleanEx; HS_DIAPH3; -.
DR   Genevisible; Q9NSV4; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
DR   GO; GO:0017048; F:Rho GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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; IPR010465; Drf_DAD.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR027654; Formin_DIAPH3.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   PANTHER; PTHR23213:SF299; PTHR23213:SF299; 1.
DR   Pfam; PF06345; Drf_DAD; 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   Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW   Deafness; Isopeptide bond; Neuropathy; Non-syndromic deafness;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   Ubl conjugation.
FT   CHAIN         1   1193       Protein diaphanous homolog 3.
FT                                /FTId=PRO_0000194897.
FT   DOMAIN      114    476       GBD/FH3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00579}.
FT   DOMAIN      561    631       FH1.
FT   DOMAIN      636   1034       FH2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00774}.
FT   DOMAIN     1057   1087       DAD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00577}.
FT   COILED      497    554       {ECO:0000255}.
FT   COILED     1013   1056       {ECO:0000255}.
FT   COMPBIAS    561    636       Pro-rich.
FT   MOD_RES      26     26       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES      68     68       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES      77     77       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     175    175       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     624    624       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES    1093   1093       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1179   1179       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ       1    263       Missing (in isoform 1 and isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_015958.
FT   VAR_SEQ      61     71       Missing (in isoform 4, isoform 5 and
FT                                isoform 6). {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_027774.
FT   VAR_SEQ      72    130       Missing (in isoform 6).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_027775.
FT   VAR_SEQ     131    165       Missing (in isoform 5).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_027776.
FT   VAR_SEQ     913    956       VSVETLEKNLRQMGRQLQQLEKELETFPPPEDLHDKFVTKM
FT                                SRF -> GLCLFKKHFMALIFSAKRLKIIPFICMYFPLSHS
FT                                VFIPNISF (in isoform 2).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_001574.
FT   VAR_SEQ     957   1193       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_001575.
FT   VAR_SEQ    1107   1112       ENQKVQ -> GNKPYL (in isoform 7 and
FT                                isoform 1). {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.2}.
FT                                /FTId=VSP_027777.
FT   VAR_SEQ    1113   1193       Missing (in isoform 7 and isoform 1).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.2}.
FT                                /FTId=VSP_027778.
FT   VARIANT     363    363       N -> S (in dbSNP:rs36084898).
FT                                /FTId=VAR_049097.
FT   VARIANT     773    773       F -> L (in dbSNP:rs35579086).
FT                                /FTId=VAR_049098.
FT   VARIANT    1041   1041       E -> G (in dbSNP:rs7491389).
FT                                /FTId=VAR_049099.
FT   CONFLICT     55     55       E -> G (in Ref. 3; BAE96352).
FT                                {ECO:0000305}.
FT   CONFLICT    128    128       K -> R (in Ref. 7; BAC03793).
FT                                {ECO:0000305}.
FT   CONFLICT    274    274       A -> V (in Ref. 6; AAH34952).
FT                                {ECO:0000305}.
FT   CONFLICT    330    330       L -> P (in Ref. 3; BAE96351).
FT                                {ECO:0000305}.
FT   CONFLICT    588    588       P -> L (in Ref. 7; BAC03793).
FT                                {ECO:0000305}.
FT   CONFLICT    613    613       P -> L (in Ref. 3; BAE96351).
FT                                {ECO:0000305}.
FT   CONFLICT    669    669       N -> K (in Ref. 4; CAE46204).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT      1060   1074       ipfam:Drf_DAD [T]
FT   MYHIT       305    489       ipfam:Drf_FH3 [T]
FT   MYHIT       302    488       ismart:Drf_FH3 [T]
FT   MYHIT       114    476       iprf:GBD_FH3 [T]
FT   MYHIT       637   1008       ipfam:FH2 [T]
FT   MYHIT       116    297       ipfam:Drf_GBD [T]
FT   MYHIT       636   1034       iprf:FH2 [T]
FT   MYHIT      1057   1087       iprf:DAD [T]
FT   MYHIT       113    297       ismart:Drf_GBD [T]
FT   MYHIT       636   1077       ismart:FH2 [T]
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
//