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Protein

Protein diaphanous homolog 1

Gene

Diaph1

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

Functioni

Acts in a Rho-dependent manner to recruit PFY1 to the membrane. Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration. Has neurite outgrowth promoting activity (PubMed:10678165, PubMed:15044801, PubMed:18572016, PubMed:9214622). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (By similarity).By similarity4 Publications

GO - Molecular functioni

  • actin binding Source: MGI
  • ion channel binding Source: BHF-UCL
  • poly(A) RNA binding Source: MGI
  • profilin binding Source: MGI
  • Rho GTPase binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hearing

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-6785631. ERBB2 Regulates Cell Motility.
R-MMU-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein diaphanous homolog 1
Alternative name(s):
Diaphanous-related formin-1
Short name:
DRF1
p140mDIA
Short name:
mDIA1
Gene namesi
Name:Diaph1
Synonyms:Diap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1194490. Diaph1.

Subcellular locationi

GO - Cellular componenti

  • brush border Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • microtubule organizing center Source: UniProtKB-SubCell
  • mitotic spindle Source: MGI
  • neuron projection Source: UniProtKB
  • ruffle membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

Knockout mice show normal organization of the cerebral cortex with no significant differences in cortical white matter or callosal thickness. Histological analysis of coronal brain sections at early and postnatal stages shows unilateral ventricular enlargement.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001948941 – 1255Protein diaphanous homolog 1Add BLAST1255

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei22PhosphoserineBy similarity1
Modified residuei751PhosphothreonineBy similarity1
Modified residuei1040N6-acetyllysineBy similarity1
Modified residuei1086N6-acetyllysineBy similarity1
Modified residuei1104PhosphotyrosineCombined sources1
Modified residuei1237PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation at Thr-751 is stimulated by cAMP and regulates stability, complex formation and mitochondrial movement (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO08808.
MaxQBiO08808.
PaxDbiO08808.
PRIDEiO08808.

PTM databases

iPTMnetiO08808.
PhosphoSitePlusiO08808.

Expressioni

Tissue specificityi

Ubiquitous.

Developmental stagei

Expressed in the ventricular and subventricular zone progenitor cells of the dorsal and ventral forebrain and the brainstem, at embryonic days E12.5, E14.5, and E17.5. At later embryonic age, it is observed in neurons of the cortex and hippocampus. During postnatal development, expression is detected in the cerebral cortex, basal ganglia, hippocampus, thalamus, and external granular layer of the cerebellum.1 Publication

Gene expression databases

BgeeiENSMUSG00000024456.
CleanExiMM_DIAP1.
ExpressionAtlasiO08808. baseline and differential.
GenevisibleiO08808. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with the GTP-bound form of RHOA. Interacts with RHOC, PFY1, MAPRE1, BAIAP2 and APC. Interacts with SCAI. Interacts with DCAF7, via FH2 domain (By similarity). Interacts with NCDN. Interacts with RHOA, OSBPL10, OSBPL2, VIM, TUBB and DYN1 (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-1026445,EBI-1026445
Baiap2Q8BKX13EBI-1026445,EBI-771498
IQGAP1P469408EBI-1026445,EBI-297509From a different organism.
RHOAP615863EBI-1026445,EBI-446668From a different organism.

GO - Molecular functioni

  • actin binding Source: MGI
  • ion channel binding Source: BHF-UCL
  • profilin binding Source: MGI
  • Rho GTPase binding Source: MGI

Protein-protein interaction databases

BioGridi199221. 6 interactors.
DIPiDIP-29028N.
IntActiO08808. 15 interactors.
MINTiMINT-4093098.
STRINGi10090.ENSMUSP00000111297.

Structurei

Secondary structure

11255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi85 – 93Combined sources9
Helixi98 – 105Combined sources8
Helixi109 – 122Combined sources14
Helixi135 – 143Combined sources9
Turni144 – 146Combined sources3
Helixi149 – 165Combined sources17
Helixi168 – 191Combined sources24
Turni194 – 196Combined sources3
Helixi201 – 215Combined sources15
Helixi219 – 226Combined sources8
Beta strandi228 – 230Combined sources3
Helixi231 – 237Combined sources7
Helixi244 – 258Combined sources15
Beta strandi261 – 264Combined sources4
Helixi266 – 281Combined sources16
Helixi287 – 292Combined sources6
Helixi299 – 313Combined sources15
Helixi319 – 332Combined sources14
Helixi334 – 342Combined sources9
Helixi347 – 367Combined sources21
Helixi381 – 392Combined sources12
Beta strandi393 – 395Combined sources3
Helixi397 – 408Combined sources12
Turni415 – 417Combined sources3
Helixi418 – 433Combined sources16
Helixi436 – 438Combined sources3
Beta strandi447 – 451Combined sources5
Turni453 – 455Combined sources3
Helixi457 – 461Combined sources5
Helixi464 – 469Combined sources6
Turni470 – 472Combined sources3
Beta strandi748 – 750Combined sources3
Turni772 – 775Combined sources4
Beta strandi777 – 780Combined sources4
Helixi781 – 783Combined sources3
Helixi786 – 789Combined sources4
Helixi794 – 801Combined sources8
Beta strandi833 – 835Combined sources3
Helixi837 – 850Combined sources14
Helixi854 – 863Combined sources10
Turni866 – 868Combined sources3
Helixi871 – 880Combined sources10
Helixi884 – 891Combined sources8
Helixi894 – 899Combined sources6
Helixi902 – 911Combined sources10
Helixi916 – 934Combined sources19
Helixi937 – 951Combined sources15
Helixi954 – 958Combined sources5
Helixi961 – 968Combined sources8
Beta strandi972 – 974Combined sources3
Turni975 – 978Combined sources4
Beta strandi980 – 982Combined sources3
Helixi984 – 986Combined sources3
Helixi987 – 992Combined sources6
Helixi1002 – 1012Combined sources11
Helixi1015 – 1019Combined sources5
Helixi1020 – 1023Combined sources4
Helixi1027 – 1032Combined sources6
Helixi1035 – 1057Combined sources23
Beta strandi1063 – 1066Combined sources4
Helixi1069 – 1104Combined sources36
Turni1109 – 1111Combined sources3
Helixi1114 – 1159Combined sources46
Helixi1181 – 1191Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V9DX-ray2.60A/B/C/D826-1163[»]
1Z2CX-ray3.00B/D69-451[»]
2BAPX-ray3.30A/B135-451[»]
C/D1145-1200[»]
2BNXX-ray2.40A/B131-516[»]
2F31X-ray2.10A135-367[»]
B1177-1196[»]
2V8FX-ray1.10C635-655[»]
3EG5X-ray2.70B/D69-451[»]
3O4XX-ray3.20A/B/C/D131-458[»]
E/F/G/H736-1200[»]
3OBVX-ray2.75A/B/C/D131-457[»]
E/F/G/H753-1209[»]
4UWXX-ray1.65A/B135-369[»]
ProteinModelPortaliO08808.
SMRiO08808.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08808.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini75 – 440GBD/FH3PROSITE-ProRule annotationAdd BLAST366
Domaini586 – 747FH1Add BLAST162
Domaini752 – 1154FH2PROSITE-ProRule annotationAdd BLAST403
Domaini1177 – 1205DADPROSITE-ProRule annotationAdd BLAST29

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili460 – 562Sequence analysisAdd BLAST103
Coiled coili1027 – 1179Sequence analysisAdd BLAST153

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1196 – 1199Arg/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.1 Publication

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.
HOGENOMiHOG000293231.
HOVERGENiHBG051357.
InParanoidiO08808.
KOiK05740.
PhylomeDBiO08808.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. DAD_dom.
IPR010465. Drf_DAD.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027653. Formin_Diaph1.
IPR009408. Formin_homology_1.
IPR014768. GBD/FH3_dom.
IPR010473. GTPase-bd.
[Graphical view]
PANTHERiPTHR23213:SF17. PTHR23213:SF17. 4 hits.
PfamiPF06345. Drf_DAD. 1 hit.
PF06346. Drf_FH1. 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.

O08808-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPSGGGLGP GRGTRDKKKG RSPDELPATG GDGGKHKKFL ERFTSMRIKK
60 70 80 90 100
EKEKPNSAHR NSSASYGDDP TAQSLQDISD EQVLVLFEQM LVDMNLNEEK
110 120 130 140 150
QQPLREKDIV IKREMVSQYL HTSKAGMNQK ESSRSAMMYI QELRSGLRDM
160 170 180 190 200
HLLSCLESLR VSLNNNPVSW VQTFGAEGLA SLLDILKRLH DEKEETSGNY
210 220 230 240 250
DSRNQHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD PAVPNMMIDA
260 270 280 290 300
AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTSIA
310 320 330 340 350
LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQE LREIENEDMK
360 370 380 390 400
VQLCVFDEQG DEDFFDLKGR LDDIRMEMDD FGEVFQIILN TVKDSKAEPH
410 420 430 440 450
FLSILQHLLL VRNDYEARPQ YYKLIEECVS QIVLHKNGTD PDFKCRHLQI
460 470 480 490 500
DIERLVDQMI DKTKVEKSEA KATELEKKLD SELTARHELQ VEMKKMENDF
510 520 530 540 550
EQKLQDLQGE KDALDSEKQQ ITAQKQDLEA EVSKLTGEVA KLSKELEDAK
560 570 580 590 600
NEMASLSAVV VAPSVSSSAA VPPAPPLPGD SGTVIPPPPP PPPLPGGVVP
610 620 630 640 650
PSPPLPPGTC IPPPPPLPGG ACIPPPPQLP GSAAIPPPPP LPGVASIPPP
660 670 680 690 700
PPLPGATAIP PPPPLPGATA IPPPPPLPGG TGIPPPPPPL PGSVGVPPPP
710 720 730 740 750
PLPGGPGLPP PPPPFPGAPG IPPPPPGMGV PPPPPFGFGV PAAPVLPFGL
760 770 780 790 800
TPKKVYKPEV QLRRPNWSKF VAEDLSQDCF WTKVKEDRFE NNELFAKLTL
810 820 830 840 850
AFSAQTKTSK AKKDQEGGEE KKSVQKKKVK ELKVLDSKTA QNLSIFLGSF
860 870 880 890 900
RMPYQEIKNV ILEVNEAVLT ESMIQNLIKQ MPEPEQLKML SELKEEYDDL
910 920 930 940 950
AESEQFGVVM GTVPRLRPRL NAILFKLQFS EQVENIKPEI VSVTAACEEL
960 970 980 990 1000
RKSENFSSLL ELTLLVGNYM NAGSRNAGAF GFNISFLCKL RDTKSADQKM
1010 1020 1030 1040 1050
TLLHFLAELC ENDHPEVLKF PDELAHVEKA SRVSAENLQK SLDQMKKQIA
1060 1070 1080 1090 1100
DVERDVQNFP AATDEKDKFV EKMTSFVKDA QEQYNKLRMM HSNMETLYKE
1110 1120 1130 1140 1150
LGDYFVFDPK KLSVEEFFMD LHNFRNMFLQ AVKENQKRRE TEEKMRRAKL
1160 1170 1180 1190 1200
AKEKAEKERL EKQQKREQLI DMNAEGDETG VMDSLLEALQ SGAAFRRKRG
1210 1220 1230 1240 1250
PRQVNRKAGC AVTSLLASEL TKDDAMAPGP VKVPKKSEGV PTILEEAKEL

VGRAS
Length:1,255
Mass (Da):139,343
Last modified:July 1, 1997 - v1
Checksum:i09404164873CA7C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96963 mRNA. Translation: AAC53280.1.
CCDSiCCDS57121.1.
PIRiT31065.
RefSeqiNP_031884.1. NM_007858.4.
UniGeneiMm.195916.

Genome annotation databases

EnsembliENSMUST00000115634; ENSMUSP00000111297; ENSMUSG00000024456.
GeneIDi13367.
KEGGimmu:13367.
UCSCiuc033hgk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96963 mRNA. Translation: AAC53280.1.
CCDSiCCDS57121.1.
PIRiT31065.
RefSeqiNP_031884.1. NM_007858.4.
UniGeneiMm.195916.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V9DX-ray2.60A/B/C/D826-1163[»]
1Z2CX-ray3.00B/D69-451[»]
2BAPX-ray3.30A/B135-451[»]
C/D1145-1200[»]
2BNXX-ray2.40A/B131-516[»]
2F31X-ray2.10A135-367[»]
B1177-1196[»]
2V8FX-ray1.10C635-655[»]
3EG5X-ray2.70B/D69-451[»]
3O4XX-ray3.20A/B/C/D131-458[»]
E/F/G/H736-1200[»]
3OBVX-ray2.75A/B/C/D131-457[»]
E/F/G/H753-1209[»]
4UWXX-ray1.65A/B135-369[»]
ProteinModelPortaliO08808.
SMRiO08808.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199221. 6 interactors.
DIPiDIP-29028N.
IntActiO08808. 15 interactors.
MINTiMINT-4093098.
STRINGi10090.ENSMUSP00000111297.

PTM databases

iPTMnetiO08808.
PhosphoSitePlusiO08808.

Proteomic databases

EPDiO08808.
MaxQBiO08808.
PaxDbiO08808.
PRIDEiO08808.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000115634; ENSMUSP00000111297; ENSMUSG00000024456.
GeneIDi13367.
KEGGimmu:13367.
UCSCiuc033hgk.1. mouse.

Organism-specific databases

CTDi1729.
MGIiMGI:1194490. Diaph1.

Phylogenomic databases

eggNOGiKOG1924. Eukaryota.
ENOG410Y29H. LUCA.
GeneTreeiENSGT00760000118986.
HOGENOMiHOG000293231.
HOVERGENiHBG051357.
InParanoidiO08808.
KOiK05740.
PhylomeDBiO08808.

Enzyme and pathway databases

ReactomeiR-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-6785631. ERBB2 Regulates Cell Motility.
R-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiO08808.
PROiO08808.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024456.
CleanExiMM_DIAP1.
ExpressionAtlasiO08808. baseline and differential.
GenevisibleiO08808. MM.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. DAD_dom.
IPR010465. Drf_DAD.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027653. Formin_Diaph1.
IPR009408. Formin_homology_1.
IPR014768. GBD/FH3_dom.
IPR010473. GTPase-bd.
[Graphical view]
PANTHERiPTHR23213:SF17. PTHR23213:SF17. 4 hits.
PfamiPF06345. Drf_DAD. 1 hit.
PF06346. Drf_FH1. 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 nameiDIAP1_MOUSE
AccessioniPrimary (citable) accession number: O08808
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 1, 1997
Last modified: November 30, 2016
This is version 159 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.