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Protein

Protein diaphanous homolog 3

Gene

Diaph3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds to GTP-bound form of Rho and to profilin. Acts in a Rho-dependent manner to recruit profilin to the membrane, where it promotes actin polymerization. It is required for cytokinesis, stress fiber formation, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-5663220. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein diaphanous homolog 3
Alternative name(s):
Diaphanous-related formin-3
Short name:
DRF3
p134mDIA2
Short name:
mDIA2
Gene namesi
Name:Diaph3
Synonyms:Diap3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1927222. Diaph3.

Subcellular locationi

  • Cytoplasmcytosol By similarity

  • Note: During mitosis, colocalizes with the actin-rich cleavage furrow and with the microtubule-rich central spindle during cytokinesis.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi118K → R: No loss of ubiquitination; when associated with R-119, R-493 and R-494. 1 Publication1
Mutagenesisi119K → R: No loss of ubiquitination; when associated with R-118, R-493 and R-494. 1 Publication1
Mutagenesisi493K → R: No loss of ubiquitination; when associated with R-118, R-119 and R-494. 1 Publication1
Mutagenesisi494K → R: No loss of ubiquitination; when associated with R-118, R-119 and R-493. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001948981 – 1171Protein diaphanous homolog 3Add BLAST1171

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei47PhosphothreonineBy similarity1
Modified residuei56PhosphoserineBy similarity1
Modified residuei154PhosphoserineBy similarity1
Modified residuei604PhosphoserineBy similarity1
Modified residuei1072PhosphoserineBy similarity1
Modified residuei1157PhosphoserineBy similarity1

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Z207.
MaxQBiQ9Z207.
PaxDbiQ9Z207.
PRIDEiQ9Z207.

PTM databases

iPTMnetiQ9Z207.
PhosphoSitePlusiQ9Z207.

Expressioni

Developmental stagei

Increased expression in S phase and mitotic cells; levels decrease as cells enter in G0/G1 phase due to proteasomal degradation (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000022021.
CleanExiMM_DIAP3.
ExpressionAtlasiQ9Z207. baseline and differential.
GenevisibleiQ9Z207. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207965. 3 interactors.
DIPiDIP-29533N.
IntActiQ9Z207. 4 interactors.
MINTiMINT-207721.
STRINGi10090.ENSMUSP00000129420.

Structurei

3D structure databases

ProteinModelPortaliQ9Z207.
SMRiQ9Z207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini93 – 455GBD/FH3PROSITE-ProRule annotationAdd BLAST363
Domaini540 – 610FH1Add BLAST71
Domaini615 – 1013FH2PROSITE-ProRule annotationAdd BLAST399
Domaini1036 – 1066DADPROSITE-ProRule annotationAdd BLAST31

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili373 – 403Sequence analysisAdd BLAST31
Coiled coili478 – 533Sequence analysisAdd BLAST56
Coiled coili887 – 918Sequence analysisAdd BLAST32
Coiled coili988 – 1038Sequence analysisAdd BLAST51

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1055 – 1058Arg/Lys-rich (basic)4

Domaini

The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).By similarity

Sequence similaritiesi

Contains 1 DAD (diaphanous autoregulatory) domain.PROSITE-ProRule annotation
Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG1924. Eukaryota.
ENOG410Y29H. LUCA.
GeneTreeiENSGT00760000118986.
HOVERGENiHBG051357.
InParanoidiQ9Z207.
KOiK05745.
OrthoDBiEOG091G0JR0.
PhylomeDBiQ9Z207.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. DAD_dom.
IPR010465. Drf_DAD.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027654. Formin_DIAPH3.
IPR014768. GBD/FH3_dom.
IPR010473. GTPase-bd.
[Graphical view]
PANTHERiPTHR23213:SF198. PTHR23213:SF198. 2 hits.
PfamiPF06345. Drf_DAD. 1 hit.
PF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 1 hit.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM01139. Drf_FH3. 1 hit.
SM01140. Drf_GBD. 1 hit.
SM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z207-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERHRARALG RDSKSSRRKG LQSAPPAGPY EPGEKRPKLH LNIRTLTDDM
60 70 80 90 100
LDKFASIRIP GSKKERPPLP HLKTVSGISD SSSLSSETME NNPKALPESE
110 120 130 140 150
VLKLFEKMME DMNLNEDKKA PLREKDFGIK KEMVMQYINT ASKTGSLRSS
160 170 180 190 200
RQISPQEFLH ELKMGYTDER LFTYLESLRV SLTSHPVSWV QSFGHEGLGL
210 220 230 240 250
LLDILEKLIN GQIQEKVVKK TQHKVIQCLR ALMNTQYGLE RIMSDKRSLS
260 270 280 290 300
LLAKAMDPRQ PAMMADVVKL LSAVCIVGEE SILEEVLEAL TSAGEERKID
310 320 330 340 350
RFFSIVEGLR HNSVNLQVAC MQLINALVTS PDDLDFRLHL RNEFMRCGLK
360 370 380 390 400
EILPNLKGIK NDGLDIQLKV FDEHKEEDLS EFFHRLEDIR AELDEASDVY
410 420 430 440 450
SMLWDTVKET RAEGHFLSIL QHLLLIRNDR FIREQYFKLI DECVSQIVLH
460 470 480 490 500
RDGTDPDFTY RKRLDLDLSQ FVDVCIDQAK LDEWEEKASE HCKKFEKECT
510 520 530 540 550
DHQETQAQLQ KREAKINELQ AELQAFKSQF GALPPGTKIP LQPSVEGEAG
560 570 580 590 600
PSALPPAPPA LSGGVPPPPP PPPPPPPPLP GMPMPFGGPV PPPPPLGFLG
610 620 630 640 650
GQSSIPLNLP FGLKPKKEFK PEISMRRLNW LKIGPNEMSE NCFWIKVNEN
660 670 680 690 700
KYENRDLLCK LENTFCCQEK EKRNTNDFDE KKVIKKRMKE LKFLDPKIAQ
710 720 730 740 750
NLSIFLSSFR VPYEKIRTMI LEVDETQLSE SMIQNLIKHL PDEEQLKSLS
760 770 780 790 800
QFRSDYNSLC EPEQFAVVMS NVKRLRPRLS AILFKLQFEE QVNNIKPDIM
810 820 830 840 850
AVSTACEEIK KSKGFSKLLE LVLLMGNYMN AGSRNAQTFG FDLSSLCKLK
860 870 880 890 900
DTKSADQKTT LLHFLVDVCE EKHADILHFV DDLAHLDKAS RVSVEMLEKN
910 920 930 940 950
VKQMGRQLQQ LEKNLETFPP PEDLHDKFVI KMSSFVISAN EQYEKLSTLL
960 970 980 990 1000
GSMTQLYQSI MGYYAVDMKK VSVEEFFNDL NNFRTSFMLA LKENIKKREA
1010 1020 1030 1040 1050
AEKEKRARIA KERAEKERLE RQQEKKRLLE MKTEGDETGV MDSLLEALQS
1060 1070 1080 1090 1100
GAAFRDRRKR TPKLKDIRQS LSPMSQRPVL KVCNHENQKM QLTEGSRPHH
1110 1120 1130 1140 1150
SINCNSTRTP VAKELNYNLD THASTGRIKA VEKEACNAES NKKKEMELLG
1160 1170
SVAKSESVPE VEALLARLRA L
Length:1,171
Mass (Da):133,686
Last modified:May 1, 1999 - v1
Checksum:i95347A854CABC7CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF094519 mRNA. Translation: AAC71771.1.
CCDSiCCDS36990.1.
PIRiT17454.
RefSeqiNP_062644.1. NM_019670.1.
UniGeneiMm.440585.

Genome annotation databases

EnsembliENSMUST00000168889; ENSMUSP00000129420; ENSMUSG00000022021.
GeneIDi56419.
KEGGimmu:56419.
UCSCiuc007uub.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF094519 mRNA. Translation: AAC71771.1.
CCDSiCCDS36990.1.
PIRiT17454.
RefSeqiNP_062644.1. NM_019670.1.
UniGeneiMm.440585.

3D structure databases

ProteinModelPortaliQ9Z207.
SMRiQ9Z207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207965. 3 interactors.
DIPiDIP-29533N.
IntActiQ9Z207. 4 interactors.
MINTiMINT-207721.
STRINGi10090.ENSMUSP00000129420.

PTM databases

iPTMnetiQ9Z207.
PhosphoSitePlusiQ9Z207.

Proteomic databases

EPDiQ9Z207.
MaxQBiQ9Z207.
PaxDbiQ9Z207.
PRIDEiQ9Z207.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000168889; ENSMUSP00000129420; ENSMUSG00000022021.
GeneIDi56419.
KEGGimmu:56419.
UCSCiuc007uub.1. mouse.

Organism-specific databases

CTDi81624.
MGIiMGI:1927222. Diaph3.

Phylogenomic databases

eggNOGiKOG1924. Eukaryota.
ENOG410Y29H. LUCA.
GeneTreeiENSGT00760000118986.
HOVERGENiHBG051357.
InParanoidiQ9Z207.
KOiK05745.
OrthoDBiEOG091G0JR0.
PhylomeDBiQ9Z207.

Enzyme and pathway databases

ReactomeiR-MMU-5663220. RHO GTPases Activate Formins.

Miscellaneous databases

PROiQ9Z207.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022021.
CleanExiMM_DIAP3.
ExpressionAtlasiQ9Z207. baseline and differential.
GenevisibleiQ9Z207. MM.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. DAD_dom.
IPR010465. Drf_DAD.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027654. Formin_DIAPH3.
IPR014768. GBD/FH3_dom.
IPR010473. GTPase-bd.
[Graphical view]
PANTHERiPTHR23213:SF198. PTHR23213:SF198. 2 hits.
PfamiPF06345. Drf_DAD. 1 hit.
PF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 1 hit.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM01139. Drf_FH3. 1 hit.
SM01140. Drf_GBD. 1 hit.
SM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDIAP3_MOUSE
AccessioniPrimary (citable) accession number: Q9Z207
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.