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O08808

- DIAP1_MOUSE

UniProt

O08808 - DIAP1_MOUSE

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Protein
Protein diaphanous homolog 1
Gene
Diaph1, Diap1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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. 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.4 Publications

GO - Molecular functioni

  1. Rho GTPase binding Source: MGI
  2. actin binding Source: MGI
  3. identical protein binding Source: IntAct
  4. ion channel binding Source: BHF-UCL
  5. profilin binding Source: MGI
  6. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. actin cytoskeleton organization Source: MGI
  2. actin filament polymerization Source: MGI
  3. cellular response to histamine Source: Ensembl
  4. cytoskeleton organization Source: UniProtKB
  5. neuron projection development Source: UniProtKB
  6. positive regulation of cell migration Source: Ensembl
  7. protein localization to microtubule Source: Ensembl
  8. regulation of cell shape Source: UniProtKB
  9. regulation of microtubule-based process Source: UniProtKB
  10. regulation of release of sequestered calcium ion into cytosol Source: Ensembl
  11. sensory perception of sound Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Hearing

Keywords - Ligandi

Actin-binding

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
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1194490. Diap1.

Subcellular locationi

Cell membrane. Cell projectionruffle membrane. Cytoplasmcytoskeleton
Note: Membrane ruffles, especially at the tip of ruffles, of motile cells.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. mitotic spindle Source: Ensembl
  3. neuron projection Source: UniProtKB
  4. ruffle membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12551255Protein diaphanous homolog 1
PRO_0000194894Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei22 – 221Phosphoserine By similarity
Cross-linki477 – 477Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei1040 – 10401N6-acetyllysine By similarity
Modified residuei1086 – 10861N6-acetyllysine By similarity
Modified residuei1104 – 11041Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO08808.
PaxDbiO08808.
PRIDEiO08808.

PTM databases

PhosphoSiteiO08808.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiO08808.
BgeeiO08808.
CleanExiMM_DIAP1.
GenevestigatoriO08808.

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.8 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.

Protein-protein interaction databases

BioGridi199221. 6 interactions.
DIPiDIP-29028N.
IntActiO08808. 13 interactions.
MINTiMINT-4093098.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi85 – 939
Helixi98 – 1058
Helixi109 – 12214
Helixi136 – 1438
Turni144 – 1463
Helixi149 – 16517
Helixi168 – 19023
Turni194 – 1963
Helixi201 – 21515
Helixi219 – 2279
Beta strandi228 – 2303
Helixi231 – 2377
Helixi244 – 25815
Beta strandi261 – 2633
Helixi266 – 28116
Helixi287 – 2926
Helixi299 – 31315
Helixi319 – 33113
Helixi334 – 3418
Helixi347 – 37731
Helixi381 – 39212
Beta strandi393 – 3953
Helixi397 – 40812
Turni415 – 4173
Helixi418 – 43316
Helixi436 – 4383
Beta strandi447 – 4515
Turni453 – 4553
Helixi464 – 4696
Turni470 – 4723
Beta strandi748 – 7503
Turni772 – 7754
Beta strandi777 – 7804
Helixi781 – 7833
Helixi786 – 7894
Helixi794 – 8018
Beta strandi833 – 8353
Helixi837 – 85014
Helixi854 – 86310
Turni866 – 8683
Helixi871 – 88010
Helixi884 – 8918
Helixi894 – 8996
Helixi902 – 91110
Helixi916 – 93419
Helixi937 – 95115
Helixi954 – 9585
Turni971 – 9733
Beta strandi974 – 9763
Beta strandi980 – 9823
Helixi984 – 9863
Helixi987 – 9926
Helixi1002 – 101211
Helixi1015 – 10195
Helixi1020 – 10234
Helixi1027 – 10326
Helixi1035 – 105723
Beta strandi1063 – 10664
Helixi1069 – 110436
Turni1109 – 11113
Helixi1114 – 115946
Helixi1181 – 119111

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO08808.
SMRiO08808. Positions 83-457, 745-1198.

Miscellaneous databases

EvolutionaryTraceiO08808.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 440366GBD/FH3
Add
BLAST
Domaini586 – 747162FH1
Add
BLAST
Domaini752 – 1154403FH2
Add
BLAST
Domaini1177 – 120529DAD
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili460 – 562103 Reviewed prediction
Add
BLAST
Coiled coili1027 – 1179153 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1196 – 11994Arg/Lys-rich (basic)

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

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG149898.
GeneTreeiENSGT00730000110702.
HOGENOMiHOG000293231.
HOVERGENiHBG051357.
KOiK05740.
OrthoDBiEOG7G1V5D.
PhylomeDBiO08808.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. Diaphanous_autoregulatory.
IPR010465. Drf_DAD.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027653. Formin_Diaph1.
IPR009408. Formin_homology_1.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view]
PANTHERiPTHR23213:SF17. PTHR23213:SF17. 1 hit.
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]
SMARTiSM00498. 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

MEPSGGGLGP GRGTRDKKKG RSPDELPATG GDGGKHKKFL ERFTSMRIKK     50
EKEKPNSAHR NSSASYGDDP TAQSLQDISD EQVLVLFEQM LVDMNLNEEK 100
QQPLREKDIV IKREMVSQYL HTSKAGMNQK ESSRSAMMYI QELRSGLRDM 150
HLLSCLESLR VSLNNNPVSW VQTFGAEGLA SLLDILKRLH DEKEETSGNY 200
DSRNQHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD PAVPNMMIDA 250
AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTSIA 300
LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQE LREIENEDMK 350
VQLCVFDEQG DEDFFDLKGR LDDIRMEMDD FGEVFQIILN TVKDSKAEPH 400
FLSILQHLLL VRNDYEARPQ YYKLIEECVS QIVLHKNGTD PDFKCRHLQI 450
DIERLVDQMI DKTKVEKSEA KATELEKKLD SELTARHELQ VEMKKMENDF 500
EQKLQDLQGE KDALDSEKQQ ITAQKQDLEA EVSKLTGEVA KLSKELEDAK 550
NEMASLSAVV VAPSVSSSAA VPPAPPLPGD SGTVIPPPPP PPPLPGGVVP 600
PSPPLPPGTC IPPPPPLPGG ACIPPPPQLP GSAAIPPPPP LPGVASIPPP 650
PPLPGATAIP PPPPLPGATA IPPPPPLPGG TGIPPPPPPL PGSVGVPPPP 700
PLPGGPGLPP PPPPFPGAPG IPPPPPGMGV PPPPPFGFGV PAAPVLPFGL 750
TPKKVYKPEV QLRRPNWSKF VAEDLSQDCF WTKVKEDRFE NNELFAKLTL 800
AFSAQTKTSK AKKDQEGGEE KKSVQKKKVK ELKVLDSKTA QNLSIFLGSF 850
RMPYQEIKNV ILEVNEAVLT ESMIQNLIKQ MPEPEQLKML SELKEEYDDL 900
AESEQFGVVM GTVPRLRPRL NAILFKLQFS EQVENIKPEI VSVTAACEEL 950
RKSENFSSLL ELTLLVGNYM NAGSRNAGAF GFNISFLCKL RDTKSADQKM 1000
TLLHFLAELC ENDHPEVLKF PDELAHVEKA SRVSAENLQK SLDQMKKQIA 1050
DVERDVQNFP AATDEKDKFV EKMTSFVKDA QEQYNKLRMM HSNMETLYKE 1100
LGDYFVFDPK KLSVEEFFMD LHNFRNMFLQ AVKENQKRRE TEEKMRRAKL 1150
AKEKAEKERL EKQQKREQLI DMNAEGDETG VMDSLLEALQ SGAAFRRKRG 1200
PRQVNRKAGC AVTSLLASEL TKDDAMAPGP VKVPKKSEGV PTILEEAKEL 1250
VGRAS 1255
Length:1,255
Mass (Da):139,343
Last modified:July 1, 1997 - v1
Checksum:i09404164873CA7C1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U96963 mRNA. Translation: AAC53280.1.
CCDSiCCDS57121.1.
PIRiT31065.
RefSeqiNP_031884.1. NM_007858.2.
UniGeneiMm.195916.

Genome annotation databases

EnsembliENSMUST00000115634; ENSMUSP00000111297; ENSMUSG00000024456.
GeneIDi13367.
KEGGimmu:13367.
UCSCiuc008erj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U96963 mRNA. Translation: AAC53280.1 .
CCDSi CCDS57121.1.
PIRi T31065.
RefSeqi NP_031884.1. NM_007858.2.
UniGenei Mm.195916.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1V9D X-ray 2.60 A/B/C/D 826-1163 [» ]
1Z2C X-ray 3.00 B/D 69-451 [» ]
2BAP X-ray 3.30 A/B 135-451 [» ]
C/D 1145-1200 [» ]
2BNX X-ray 2.40 A/B 131-516 [» ]
2F31 X-ray 2.10 A 135-367 [» ]
B 1177-1196 [» ]
2V8F X-ray 1.10 C 635-655 [» ]
3EG5 X-ray 2.70 B/D 69-451 [» ]
3O4X X-ray 3.20 A/B/C/D 131-458 [» ]
E/F/G/H 736-1200 [» ]
3OBV X-ray 2.75 A/B/C/D 131-457 [» ]
E/F/G/H 753-1209 [» ]
ProteinModelPortali O08808.
SMRi O08808. Positions 83-457, 745-1198.
ModBasei Search...

Protein-protein interaction databases

BioGridi 199221. 6 interactions.
DIPi DIP-29028N.
IntActi O08808. 13 interactions.
MINTi MINT-4093098.

PTM databases

PhosphoSitei O08808.

Proteomic databases

MaxQBi O08808.
PaxDbi O08808.
PRIDEi O08808.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000115634 ; ENSMUSP00000111297 ; ENSMUSG00000024456 .
GeneIDi 13367.
KEGGi mmu:13367.
UCSCi uc008erj.1. mouse.

Organism-specific databases

CTDi 13367.
MGIi MGI:1194490. Diap1.

Phylogenomic databases

eggNOGi NOG149898.
GeneTreei ENSGT00730000110702.
HOGENOMi HOG000293231.
HOVERGENi HBG051357.
KOi K05740.
OrthoDBi EOG7G1V5D.
PhylomeDBi O08808.

Miscellaneous databases

EvolutionaryTracei O08808.
NextBioi 283706.
PROi O08808.
SOURCEi Search...

Gene expression databases

ArrayExpressi O08808.
Bgeei O08808.
CleanExi MM_DIAP1.
Genevestigatori O08808.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR014767. Diaphanous_autoregulatory.
IPR010465. Drf_DAD.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027653. Formin_Diaph1.
IPR009408. Formin_homology_1.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view ]
PANTHERi PTHR23213:SF17. PTHR23213:SF17. 1 hit.
Pfami PF06345. 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 ]
SMARTi SM00498. FH2. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin."
    Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G., Kakizuka A., Saito Y., Nakao K., Jockusch B.M., Narumiya S.
    EMBO J. 16:3044-3056(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION.
  2. "Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2."
    Fujiwara T., Mammoto A., Kim Y., Takai Y.
    Biochem. Biophys. Res. Commun. 271:626-629(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAIAP2.
  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. "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration."
    Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S., Chen M., Wallar B.J., Alberts A.S., Gundersen G.G.
    Nat. Cell Biol. 6:820-830(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APC AND MAPRE1.
  5. "Actin polymerization-driven molecular movement of mDia1 in living cells."
    Higashida C., Miyoshi T., Fujita A., Oceguera-Yanez F., Monypenny J., Andou Y., Narumiya S., Watanabe N.
    Science 303:2007-2010(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ACTIN.
  6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  8. "Identification of Neurochondrin as a new interaction partner of the FH3 domain of the Diaphanous-related formin Dia1."
    Schwaibold E.M., Brandt D.T.
    Biochem. Biophys. Res. Commun. 373:366-372(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NCDN.
  9. "SCAI acts as a suppressor of cancer cell invasion through the transcriptional control of beta1-integrin."
    Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P., Grosse R.
    Nat. Cell Biol. 11:557-568(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCAI.
  10. "The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization."
    Shimada A., Nyitrai M., Vetter I.R., Kuehlmann D., Bugyi B., Narumiya S., Geeves M.A., Wittinghofer A.
    Mol. Cell 13:511-522(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 826-1163, OLIGOMERIZATION, INTERACTION WITH ACTIN.
  11. "The regulation of mDia1 by autoinhibition and its release by Rho*GTP."
    Lammers M., Rose R., Scrima A., Wittinghofer A.
    EMBO J. 24:4176-4187(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 135-451 AND 1145-1200, DOMAIN DAD, AUTOINHIBITION.
  12. "Structural and mechanistic insights into the interaction between Rho and mammalian Dia."
    Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R., Wittinghofer A.
    Nature 435:513-518(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-451 IN COMPLEX WITH RHOC, HOMODIMERIZATION.

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: July 9, 2014
This is version 136 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

External Data

Dasty 3

Similar proteinsi