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Q91Z67

- SRGP2_MOUSE

UniProt

Q91Z67 - SRGP2_MOUSE

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Protein

SLIT-ROBO Rho GTPase-activating protein 2

Gene

Srgap2

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

Functioni

RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral cortex. May play a role for cognition, learning and memory. In non-neuronal cells, it may also play a role in cell migration by regulating the formation of lamellipodia and filopodia.2 Publications

GO - Molecular functioni

  1. protein homodimerization activity Source: UniProtKB
  2. Rac GTPase activator activity Source: UniProtKB
  3. Rac GTPase binding Source: UniProtKB

GO - Biological processi

  1. actin filament severing Source: UniProtKB
  2. dendritic spine development Source: UniProtKB
  3. extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration Source: UniProtKB
  4. filopodium assembly Source: UniProtKB
  5. negative regulation of neuron migration Source: UniProtKB
  6. neuron projection morphogenesis Source: UniProtKB
  7. positive regulation of Rac GTPase activity Source: UniProtKB
  8. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
SLIT-ROBO Rho GTPase-activating protein 2
Short name:
srGAP2
Alternative name(s):
Formin-binding protein 2
Formin-binding protein 27
Short name:
FBP-27
Gene namesi
Name:Srgap2
Synonyms:Fbp27, Fnbp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:109605. Srgap2.

Subcellular locationi

Cell membrane By similarity. Cell projectiondendritic spine By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell junctionsynapsepostsynaptic cell membrane. Cell projectionlamellipodium By similarity. Cytoplasmic vesiclephagosome. Nucleus By similarity. Cytoplasm By similarity
Note: Recruited to actin-rich phagosomes during phagocytosis. Translocates from nucleus to cytoplasm during development (By similarity).By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytosol Source: UniProtKB
  3. dendritic spine head Source: UniProtKB
  4. mitochondrial inner membrane Source: MGI
  5. nucleus Source: UniProtKB-KW
  6. phagocytic vesicle Source: UniProtKB
  7. plasma membrane Source: UniProtKB
  8. postsynaptic density Source: UniProtKB
  9. postsynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

Mice are viable and show no abnormality of cortical lamination. However, a delay in dendritic spine maturation coupled to an increase in spine neck and spine density is observed.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi527 – 5271R → L: Unable to stimulate RAC1 GTPase activity and to induce neurite branching. No effect on filopodia biogenesis and neurite outgrowth. 1 Publication
Mutagenesisi765 – 7651W → A: Loss of the ability to induce filopodia and to initiate neurite outgrowht. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10711071SLIT-ROBO Rho GTPase-activating protein 2PRO_0000056768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei927 – 9271Omega-N-methylated arginine; by PRMT5By similarity
Modified residuei930 – 9301PhosphoserineBy similarity

Post-translational modificationi

Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ91Z67.
PaxDbiQ91Z67.
PRIDEiQ91Z67.

PTM databases

PhosphoSiteiQ91Z67.

Expressioni

Developmental stagei

Expressed throughout cortical development culminating at P1. Expression is reduced but still present in the adult cortex. Expressed in the cortical wall both in neuronal progenitors in the ventricular zone and post-mitotic neurons in the cortical plate (at protein level).1 Publication

Gene expression databases

BgeeiQ91Z67.
CleanExiMM_SRGAP2.
GenevestigatoriQ91Z67.

Interactioni

Subunit structurei

Homodimer. Interacts with FASLG (By similarity). Interacts with PRMT5 (By similarity). Probably interacts with ROBO1 and ROBO2. Interacts with RAC1; specifically stimulates RAC1 GTPase activity. Interacts (via SH3 domain) with FMNL1 (activated by RAC1); regulates the actin filament severing activity of FMNL1. Interacts (via SH3 domain) with FMNL3. Interacts (via SH3 domain) with GPHN.By similarity3 Publications

Protein-protein interaction databases

BioGridi199721. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ91Z67.
SMRiQ91Z67. Positions 723-787.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 8766FCHPROSITE-ProRule annotationAdd
BLAST
Domaini489 – 679191Rho-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini728 – 78760SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 502502F-BAR domainBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili363 – 40139Sequence AnalysisAdd
BLAST
Coiled coili940 – 96829Sequence AnalysisAdd
BLAST

Domaini

The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions.

Sequence similaritiesi

Contains 1 FCH domain.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG264793.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000039980.
HOVERGENiHBG051637.
InParanoidiQ91Z67.
KOiK07526.
OMAiEDYCESP.
OrthoDBiEOG7966FQ.
PhylomeDBiQ91Z67.
TreeFamiTF315892.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS50133. FCH. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91Z67-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ
60 70 80 90 100
DFFRKKAEIE MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN
110 120 130 140 150
LLLNQVKRES RDHTTLSDIY LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ
160 170 180 190 200
DDLMKVLNEL YSVMKTYHMY NADSISAQSK LKEAEKQEEK QIGKSVKQED
210 220 230 240 250
RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT ENKLKAIKAR
260 270 280 290 300
NEYLLALEAT NASVFKYYIH DLSDIIDQCC DLGYHASLNR ALRTFLSAEL
310 320 330 340 350
NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG
360 370 380 390 400
DMASQLCAQQ PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD
410 420 430 440 450
IVTVEDFDVS DCFQYSNSME SVKSTVSETF MSKPSIAKRR ANQQETEQFY
460 470 480 490 500
FTKMKEYLEG RNLITKLQAK HDLLQKTLGE SQRTDCSLAR RSSTVRKQDS
510 520 530 540 550
SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN AFERGEDPLA
560 570 580 590 600
GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLIACVT MDNLQERAVH
610 620 630 640 650
IRKVLLVLPK PTLIIMRYLF AFLNHLSQFS EENMMDPYNL AICFGPSLMS
660 670 680 690 700
VPEGHDQVSC QAHVNELIKT IIIQHENIFP NPRELEGPIY SRGGSMEDYC
710 720 730 740 750
DSTHGETTSA EDSTQDVTAE HHTSDDECEP IEAIAKFDYV GRTARELSFK
760 770 780 790 800
KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ YIVVQDTEDG VVERSSPKSE
810 820 830 840 850
IEVMSEPPEE KVTARTGASC PSGGHVADIY LANINKQRKR PESGSIRKAF
860 870 880 890 900
RSDSHGLGSS LTDSSSLGVG ASCRPSSQPI MSQNLPKEGP DKCSISGHGS
910 920 930 940 950
LNSISRHSSL KNRMDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM
960 970 980 990 1000
NSALNELQEL ERQSSAKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL
1010 1020 1030 1040 1050
LKDPEPAFQR SASTAGDIAC AFRPVKSVKM AAPVKPPATR PKPTVFPKTN
1060 1070
ATSPGVNSSA SPQATDKSCT V
Length:1,071
Mass (Da):120,798
Last modified:January 9, 2007 - v2
Checksum:i9093C63476BA605D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti598 – 5981A → V in AAL27032. (PubMed:11672528)Curated
Sequence conflicti612 – 6121T → S in AAL27032. (PubMed:11672528)Curated
Sequence conflicti662 – 6621A → S in AAL27032. (PubMed:11672528)Curated
Sequence conflicti737 – 7371F → C in AAL27032. (PubMed:11672528)Curated
Sequence conflicti765 – 7651W → L in AAL27032. (PubMed:11672528)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC109299 Genomic DNA. No translation available.
AC120217 Genomic DNA. No translation available.
AC165436 Genomic DNA. No translation available.
BC151081 mRNA. Translation: AAI51082.1.
BC151082 mRNA. Translation: AAI51083.1.
BC158055 mRNA. Translation: AAI58056.1.
BC172152 mRNA. Translation: AAI72152.1.
AY057900 mRNA. Translation: AAL27032.1.
AK132220 mRNA. Translation: BAE21041.1.
U40752 mRNA. Translation: AAC52480.1.
CCDSiCCDS48355.1.
PIRiS64712.
RefSeqiNP_001074480.2. NM_001081011.2.
XP_006529197.1. XM_006529134.1.
XP_006529198.1. XM_006529135.1.
UniGeneiMm.276259.

Genome annotation databases

EnsembliENSMUST00000097588; ENSMUSP00000095195; ENSMUSG00000026425.
GeneIDi14270.
KEGGimmu:14270.
UCSCiuc007cng.2. mouse.

Cross-referencesi

Web resourcesi

Protein Spotlight

Branching out - Issue 143 of October 2012

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC109299 Genomic DNA. No translation available.
AC120217 Genomic DNA. No translation available.
AC165436 Genomic DNA. No translation available.
BC151081 mRNA. Translation: AAI51082.1 .
BC151082 mRNA. Translation: AAI51083.1 .
BC158055 mRNA. Translation: AAI58056.1 .
BC172152 mRNA. Translation: AAI72152.1 .
AY057900 mRNA. Translation: AAL27032.1 .
AK132220 mRNA. Translation: BAE21041.1 .
U40752 mRNA. Translation: AAC52480.1 .
CCDSi CCDS48355.1.
PIRi S64712.
RefSeqi NP_001074480.2. NM_001081011.2.
XP_006529197.1. XM_006529134.1.
XP_006529198.1. XM_006529135.1.
UniGenei Mm.276259.

3D structure databases

ProteinModelPortali Q91Z67.
SMRi Q91Z67. Positions 723-787.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199721. 1 interaction.

PTM databases

PhosphoSitei Q91Z67.

Proteomic databases

MaxQBi Q91Z67.
PaxDbi Q91Z67.
PRIDEi Q91Z67.

Protocols and materials databases

DNASUi 14270.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000097588 ; ENSMUSP00000095195 ; ENSMUSG00000026425 .
GeneIDi 14270.
KEGGi mmu:14270.
UCSCi uc007cng.2. mouse.

Organism-specific databases

CTDi 23380.
MGIi MGI:109605. Srgap2.

Phylogenomic databases

eggNOGi NOG264793.
GeneTreei ENSGT00760000118863.
HOGENOMi HOG000039980.
HOVERGENi HBG051637.
InParanoidi Q91Z67.
KOi K07526.
OMAi EDYCESP.
OrthoDBi EOG7966FQ.
PhylomeDBi Q91Z67.
TreeFami TF315892.

Miscellaneous databases

ChiTaRSi Srgap2. mouse.
NextBioi 285639.
PROi Q91Z67.
SOURCEi Search...

Gene expression databases

Bgeei Q91Z67.
CleanExi MM_SRGAP2.
Genevestigatori Q91Z67.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
InterProi IPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00611. FCH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
SMARTi SM00055. FCH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEi PS50133. FCH. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Signal transduction in neuronal migration: roles of GTPase activating proteins and the small GTPase Cdc42 in the Slit-Robo pathway."
    Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H., Wen L., Brady-Kalnay S.M., Mei L., Wu J.Y., Xiong W.C., Rao Y.
    Cell 107:209-221(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 432-836.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1071.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains."
    Chan D.C., Bedford M.T., Leder P.
    EMBO J. 15:1045-1054(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 732-782.
    Strain: FVB.
  6. "The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis."
    Guerrier S., Coutinho-Budd J., Sassa T., Gresset A., Jordan N.V., Chen K., Jin W.L., Frost A., Polleux F.
    Cell 138:990-1004(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEURON MIGRATION AND MORPHOGENESIS, DEVELOPMENTAL STAGE, SUBUNIT, INTERACTION WITH RAC1, MUTAGENESIS OF ARG-527 AND TRP-765.
  7. Cited for: INTERACTION WITH FMNL1; FMNL3 AND ROBO2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "SH3 domain-based phototrapping in living cells reveals Rho family GAP signaling complexes."
    Okada H., Uezu A., Mason F.M., Soderblom E.J., Moseley M.A. III, Soderling S.H.
    Sci. Signal. 4:RS13-RS13(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPHN.
  9. "Inhibition of SRGAP2 function by its human-specific paralogs induces neoteny during spine maturation."
    Charrier C., Joshi K., Coutinho-Budd J., Kim J.E., Lambert N., de Marchena J., Jin W.L., Vanderhaeghen P., Ghosh A., Sassa T., Polleux F.
    Cell 149:923-935(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DENDRITIC SPINE MATURATION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSRGP2_MOUSE
AccessioniPrimary (citable) accession number: Q91Z67
Secondary accession number(s): B2RY13, Q3V1V8, Q61054
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 9, 2007
Last modified: November 26, 2014
This is version 104 of the entry and version 2 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3