Protein diaphanous homolog 3 - Mus musculus (Mouse)

Contribute

Send feedback

Read comments (?) or add your own

Q9Z207 (DIAP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein diaphanous homolog 3

Alternative name(s):
Diaphanous-related formin-3
Short name=DRF3
p134mDIA2
Short name=mDIA2

Gene names

Name:	Diaph3
Synonyms:	Diap3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1171 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.3
Subcellular location	Cytoplasm › cytosol By similarity. Note: During mitosis, co-localizes with the actin-rich cleavage furrow and with the microtubule-rich central spindle during cytokinesis By similarity.
Developmental stage	Increased expression in S phase and mitotic cells; levels decrease as cells enter in G0/G1 phase due to proteasomal degradation (at protein level). Ref.4
Domain	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.
Sequence similarities	Belongs to the formin homology family. Diaphanous subfamily. Contains 1 DAD (diaphanous autoregulatory) domain. Contains 1 FH1 (formin homology 1) domain. Contains 1 FH2 (formin homology 2) domain. Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Coiled coil Repeat
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1171

1171

Protein diaphanous homolog 3

PRO_0000194898

Regions

Domain

93 – 455

363

GBD/FH3

Domain

540 – 610

FH1

Domain

615 – 1013

399

FH2

Domain

1036 – 1066

DAD

Coiled coil

373 – 403

Potential

Coiled coil

478 – 533

Potential

Coiled coil

887 – 918

Potential

Coiled coil

988 – 1038

Potential

Compositional bias

1055 – 1058

Arg/Lys-rich (basic)

Amino acid modifications

Modified residue

604

Phosphoserine By similarity

Cross-link

118

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis

118

K → R: No loss of ubiquitination; when associated with R-119, R-493 and R-494. Ref.4

Mutagenesis

119

K → R: No loss of ubiquitination; when associated with R-118, R-493 and R-494. Ref.4

Mutagenesis

493

K → R: No loss of ubiquitination; when associated with R-118, R-119 and R-494. Ref.4

Mutagenesis

494

K → R: No loss of ubiquitination; when associated with R-118, R-119 and R-493. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Z207 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 95347A854CABC7CF
Show »

FASTA

1,171

133,686

        10         20         30         40         50         60 
MERHRARALG RDSKSSRRKG LQSAPPAGPY EPGEKRPKLH LNIRTLTDDM LDKFASIRIP 

        70         80         90        100        110        120 
GSKKERPPLP HLKTVSGISD SSSLSSETME NNPKALPESE VLKLFEKMME DMNLNEDKKA 

       130        140        150        160        170        180 
PLREKDFGIK KEMVMQYINT ASKTGSLRSS RQISPQEFLH ELKMGYTDER LFTYLESLRV 

       190        200        210        220        230        240 
SLTSHPVSWV QSFGHEGLGL LLDILEKLIN GQIQEKVVKK TQHKVIQCLR ALMNTQYGLE 

       250        260        270        280        290        300 
RIMSDKRSLS LLAKAMDPRQ PAMMADVVKL LSAVCIVGEE SILEEVLEAL TSAGEERKID 

       310        320        330        340        350        360 
RFFSIVEGLR HNSVNLQVAC MQLINALVTS PDDLDFRLHL RNEFMRCGLK EILPNLKGIK 

       370        380        390        400        410        420 
NDGLDIQLKV FDEHKEEDLS EFFHRLEDIR AELDEASDVY SMLWDTVKET RAEGHFLSIL 

       430        440        450        460        470        480 
QHLLLIRNDR FIREQYFKLI DECVSQIVLH RDGTDPDFTY RKRLDLDLSQ FVDVCIDQAK 

       490        500        510        520        530        540 
LDEWEEKASE HCKKFEKECT DHQETQAQLQ KREAKINELQ AELQAFKSQF GALPPGTKIP 

       550        560        570        580        590        600 
LQPSVEGEAG PSALPPAPPA LSGGVPPPPP PPPPPPPPLP GMPMPFGGPV PPPPPLGFLG 

       610        620        630        640        650        660 
GQSSIPLNLP FGLKPKKEFK PEISMRRLNW LKIGPNEMSE NCFWIKVNEN KYENRDLLCK 

       670        680        690        700        710        720 
LENTFCCQEK EKRNTNDFDE KKVIKKRMKE LKFLDPKIAQ NLSIFLSSFR VPYEKIRTMI 

       730        740        750        760        770        780 
LEVDETQLSE SMIQNLIKHL PDEEQLKSLS QFRSDYNSLC EPEQFAVVMS NVKRLRPRLS 

       790        800        810        820        830        840 
AILFKLQFEE QVNNIKPDIM AVSTACEEIK KSKGFSKLLE LVLLMGNYMN AGSRNAQTFG 

       850        860        870        880        890        900 
FDLSSLCKLK DTKSADQKTT LLHFLVDVCE EKHADILHFV DDLAHLDKAS RVSVEMLEKN 

       910        920        930        940        950        960 
VKQMGRQLQQ LEKNLETFPP PEDLHDKFVI KMSSFVISAN EQYEKLSTLL GSMTQLYQSI 

       970        980        990       1000       1010       1020 
MGYYAVDMKK VSVEEFFNDL NNFRTSFMLA LKENIKKREA AEKEKRARIA KERAEKERLE 

      1030       1040       1050       1060       1070       1080 
RQQEKKRLLE MKTEGDETGV MDSLLEALQS GAAFRDRRKR TPKLKDIRQS LSPMSQRPVL 

      1090       1100       1110       1120       1130       1140 
KVCNHENQKM QLTEGSRPHH SINCNSTRTP VAKELNYNLD THASTGRIKA VEKEACNAES 

      1150       1160       1170 
NKKKEMELLG SVAKSESVPE VEALLARLRA L

« Hide

References

[1]	"Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7." Alberts A.S., Bouquin N., Johnston L.H., Treisman R. J. Biol. Chem. 273:8616-8622(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Tominaga T., Sahai E., Treisman R.H., Alberts A.S. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase signaling." Tominaga T., Sahai E., Chardin P., McCormick F., Courtneidge S.A., Alberts A.S. Mol. Cell 5:13-25(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"Ubiquitin-mediated degradation of the formin mDia2 upon completion of cell division." DeWard A.D., Alberts A.S. J. Biol. Chem. 284:20061-20069(2009) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF LYS-118; LYS-119; LYS-493 AND LYS-494.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF094519 mRNA. Translation: AAC71771.1.
IPI	IPI00230476.
PIR	T17454.
RefSeq	NP_062644.1. NM_019670.1.
UniGene	Mm.440585.
3D structure databases
ProteinModelPortal	Q9Z207.
SMR	Q9Z207. Positions 101-490, 609-1057.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29533N.
MINT	MINT-207721.
STRING	10090.ENSMUSP00000022599.
PTM databases
PhosphoSite	Q9Z207.
Proteomic databases
PaxDb	Q9Z207.
PRIDE	Q9Z207.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000168889; ENSMUSP00000129420; ENSMUSG00000022021.
GeneID	56419.
KEGG	mmu:56419.
UCSC	uc007uub.1. mouse.
Organism-specific databases
CTD	56419.
MGI	MGI:1927222. Diap3.
Phylogenomic databases
eggNOG	NOG149898.
GeneTree	ENSGT00700000104080.
HOVERGEN	HBG051357.
InParanoid	Q9Z207.
KO	K05745.
OrthoDB	EOG461437.
Gene expression databases
ArrayExpress	Q9Z207.
Bgee	Q9Z207.
CleanEx	MM_DIAP3.
Genevestigator	Q9Z207.
GermOnline	ENSMUSG00000022021. Mus musculus.
Family and domain databases
InterPro	IPR003104. Actin-bd_FH2/DRF_autoreg. IPR016024. ARM-type_fold. IPR014767. Diaphanous_autoregulatory. IPR010465. Drf_DAD. IPR010472. Drf_FH3. IPR010473. Drf_GTPase-bd. IPR015425. FH2_actin-bd. IPR014768. GTPase-bd/formin_homology_3. [Graphical view]
Pfam	PF06345. Drf_DAD. 1 hit. PF06367. Drf_FH3. 1 hit. PF06371. Drf_GBD. 1 hit. PF02181. FH2. 1 hit. [Graphical view]
SMART	SM00498. FH2. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF101447. FH2_actin_bd. 1 hit.
PROSITE	PS51231. DAD. 1 hit. PS51444. FH2. 1 hit. PS51232. GBD_FH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	312564.
SOURCE	Search...

Entry information

Entry name

DIAP3_MOUSE

Accession

Primary (citable) accession number: Q9Z207

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents