Diaph3

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

actin binding Source: InterPro
cadherin binding Source: MGI
Rho GTPase binding Source: InterPro

Complete GO annotation...

GO - Biological processⁱ

actin cytoskeleton organization Source: InterPro
spermatogenesis Source: Ensembl

Complete GO annotation...

Enzyme and pathway databases

Reactomeⁱ	R-MMU-5663220. RHO GTPases Activate Formins.

Reactomeⁱ

R-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
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 14

Organism-specific databases

MGIⁱ	MGI:1927222. Diaph3.

Subcellular locationⁱ

Cytoplasm › cytosol 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

cytosol Source: UniProtKB-SubCell
nucleus Source: Ensembl

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	118	K → R: No loss of ubiquitination; when associated with R-119, R-493 and R-494. 1 Publication	1
Mutagenesisⁱ	119	K → R: No loss of ubiquitination; when associated with R-118, R-493 and R-494. 1 Publication	1
Mutagenesisⁱ	493	K → R: No loss of ubiquitination; when associated with R-118, R-119 and R-494. 1 Publication	1
Mutagenesisⁱ	494	K → R: No loss of ubiquitination; when associated with R-118, R-119 and R-493. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000194898	1 – 1171	Protein diaphanous homolog 3Add BLAST		1171

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	47	PhosphothreonineBy similarity	1
Modified residueⁱ	56	PhosphoserineBy similarity	1
Modified residueⁱ	154	PhosphoserineBy similarity	1
Modified residueⁱ	604	PhosphoserineBy similarity	1
Modified residueⁱ	1072	PhosphoserineBy similarity	1
Modified residueⁱ	1157	PhosphoserineBy similarity	1

Post-translational modificationⁱ

Ubiquitinated.1 Publication

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q9Z207.
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9Z207.
PaxDbⁱ	Q9Z207.
PRIDEⁱ	Q9Z207.

PTM databases

iPTMnetⁱ	Q9Z207.
PhosphoSitePlusⁱ	Q9Z207.

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

Bgeeⁱ	ENSMUSG00000022021.
CleanExⁱ	MM_DIAP3.
ExpressionAtlasⁱ	Q9Z207. baseline and differential.
Genevisibleⁱ	Q9Z207. MM.

Interactionⁱ

GO - Molecular functionⁱ

actin binding Source: InterPro
cadherin binding Source: MGI
Rho GTPase binding Source: InterPro

Complete GO annotation...

Protein-protein interaction databases

BioGridⁱ	207965. 3 interactors.
Database of interacting proteins More...DIPⁱ	DIP-29533N.
IntActⁱ	Q9Z207. 4 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-207721.
STRINGⁱ	10090.ENSMUSP00000129420.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q9Z207.
SMRⁱ	Q9Z207.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	93 – 455	GBD/FH3PROSITE-ProRule annotationAdd BLAST	363
Domainⁱ	540 – 610	FH1Add BLAST	71
Domainⁱ	615 – 1013	FH2PROSITE-ProRule annotationAdd BLAST	399
Domainⁱ	1036 – 1066	DADPROSITE-ProRule annotationAdd BLAST	31

Coiled coil

Feature key	Position(s)	DescriptionActions	Length
Coiled coilⁱ	373 – 403	Sequence analysisAdd BLAST	31
Coiled coilⁱ	478 – 533	Sequence analysisAdd BLAST	56
Coiled coilⁱ	887 – 918	Sequence analysisAdd BLAST	32
Coiled coilⁱ	988 – 1038	Sequence analysisAdd BLAST	51

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	1055 – 1058	Arg/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

Belongs to the formin homology family. Diaphanous subfamily.Curated

Keywords - Domainⁱ

Coiled coil, Repeat

Phylogenomic databases

eggNOGⁱ	KOG1924. Eukaryota. ENOG410Y29H. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000118986.
HOVERGENⁱ	HBG051357.
InParanoidⁱ	Q9Z207.
KEGG Orthology (KO) More...KOⁱ	K05745.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0JR0.
PhylomeDBⁱ	Q9Z207.

Family and domain databases

Gene3Dⁱ	1.25.10.10. 1 hit.
InterProⁱ	View protein in InterPro IPR011989. ARM-like. IPR016024. 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.
PANTHERⁱ	PTHR23213:SF299. PTHR23213:SF299. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF06345. Drf_DAD. 1 hit. PF06367. Drf_FH3. 1 hit. PF06371. Drf_GBD. 1 hit. PF02181. FH2. 1 hit.
SMARTⁱ	View protein in SMART SM01139. Drf_FH3. 1 hit. SM01140. Drf_GBD. 1 hit. SM00498. FH2. 1 hit.
SUPFAMⁱ	SSF48371. SSF48371. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51231. DAD. 1 hit. PS51444. FH2. 1 hit. PS51232. GBD_FH3. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q9Z207-1 [UniParc]FASTA Add 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.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS36990.1.
PIRⁱ	T17454.
NCBI Reference Sequences More...RefSeqⁱ	NP_062644.1. NM_019670.1.
UniGeneⁱ	Mm.440585.

Genome annotation databases

Ensemblⁱ	ENSMUST00000168889; ENSMUSP00000129420; ENSMUSG00000022021.
GeneIDⁱ	56419.
KEGGⁱ	mmu:56419.
UCSC genome browser More...UCSCⁱ	uc007uub.1. mouse.

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.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF094519 mRNA. Translation: AAC71771.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS36990.1.
PIRⁱ	T17454.
NCBI Reference Sequences More...RefSeqⁱ	NP_062644.1. NM_019670.1.
UniGeneⁱ	Mm.440585.

3D structure databases

ProteinModelPortalⁱ	Q9Z207.
SMRⁱ	Q9Z207.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	207965. 3 interactors.
Database of interacting proteins More...DIPⁱ	DIP-29533N.
IntActⁱ	Q9Z207. 4 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-207721.
STRINGⁱ	10090.ENSMUSP00000129420.

PTM databases

iPTMnetⁱ	Q9Z207.
PhosphoSitePlusⁱ	Q9Z207.

Proteomic databases

EPDⁱ	Q9Z207.
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9Z207.
PaxDbⁱ	Q9Z207.
PRIDEⁱ	Q9Z207.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000168889; ENSMUSP00000129420; ENSMUSG00000022021.
GeneIDⁱ	56419.
KEGGⁱ	mmu:56419.
UCSC genome browser More...UCSCⁱ	uc007uub.1. mouse.

Organism-specific databases

CTDⁱ	81624.
MGIⁱ	MGI:1927222. Diaph3.

Phylogenomic databases

eggNOGⁱ	KOG1924. Eukaryota. ENOG410Y29H. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000118986.
HOVERGENⁱ	HBG051357.
InParanoidⁱ	Q9Z207.
KEGG Orthology (KO) More...KOⁱ	K05745.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0JR0.
PhylomeDBⁱ	Q9Z207.

Enzyme and pathway databases

Reactomeⁱ	R-MMU-5663220. RHO GTPases Activate Formins.

Reactomeⁱ

R-MMU-5663220. RHO GTPases Activate Formins.

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:Q9Z207.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000022021.
CleanExⁱ	MM_DIAP3.
ExpressionAtlasⁱ	Q9Z207. baseline and differential.
Genevisibleⁱ	Q9Z207. MM.

Family and domain databases

Gene3Dⁱ	1.25.10.10. 1 hit.
InterProⁱ	View protein in InterPro IPR011989. ARM-like. IPR016024. 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.
PANTHERⁱ	PTHR23213:SF299. PTHR23213:SF299. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF06345. Drf_DAD. 1 hit. PF06367. Drf_FH3. 1 hit. PF06371. Drf_GBD. 1 hit. PF02181. FH2. 1 hit.
SMARTⁱ	View protein in SMART SM01139. Drf_FH3. 1 hit. SM01140. Drf_GBD. 1 hit. SM00498. FH2. 1 hit.
SUPFAMⁱ	SSF48371. SSF48371. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51231. DAD. 1 hit. PS51444. FH2. 1 hit. PS51232. GBD_FH3. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DIAP3_MOUSE
Accessionⁱ	Q9Z207Primary (citable) accession number: Q9Z207
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
	Last sequence update:	May 1, 1999
	Last modified:	May 10, 2017
	This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9Z207 (DIAP3_MOUSE)

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Protein diaphanous homolog 3

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Coiled coil

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ