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O70566 (DIAP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein diaphanous homolog 2
Alternative name(s):
Diaphanous-related formin-2
Short name=DRF2
Short name=mDia3
Gene names
Name:Diaph2
Synonyms:Diap2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1098 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in oogenesis.

Subunit structure

Interacts with MAPRE1 and APC. Ref.3

Developmental stage

Expressed in liver, heart, kidney, ovary and testis, at E16, P6 and P16.

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.

Sequence caution

The sequence BAC40476.1 differs from that shown. Reason: Probable cloning artifact.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10981098Protein diaphanous homolog 2
PRO_0000194896

Regions

Domain90 – 463374GBD/FH3
Domain544 – 62077FH1
Domain625 – 1025401FH2
Domain1048 – 107831DAD
Coiled coil375 – 41642 Potential
Coiled coil490 – 53950 Potential
Coiled coil999 – 105052 Potential
Compositional bias1035 – 10384Poly-Lys
Compositional bias1069 – 10724Arg/Lys-rich (basic)

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Experimental info

Sequence conflict750 – 7512KY → RD in CAA75871. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O70566 [UniParc].

Last modified February 16, 2004. Version 2.
Checksum: BB19D49E049EA8CA

FASTA1,098124,871
        10         20         30         40         50         60 
MEELGAAASG AGGGGGGGEE HGGGRSNKRG AGNRAANEEE TRNKPKLRDR ITSFRKSATK 

        70         80         90        100        110        120 
REKPVIQHSI DYQTAVVEIP PALIVHDDRS LILSEKEVLD LFEKMMEDMN LNEEKKAPLR 

       130        140        150        160        170        180 
KKDFSIKREM VVQYISATSK SIVGSKVLGG LKNSKHEFTL SSQEYVHELR SGISDEKLLN 

       190        200        210        220        230        240 
CLESLRVSLT SHPVSWVNNF GYEGLGVLLD VLEKLLDKKQ QENIDKKNQY KVIQCLKAFM 

       250        260        270        280        290        300 
NNKFGLQRIL GDERSLLLLA RAIDPKQQNM MTEIVKILSA ICIVGEENIL DKLLGGITAA 

       310        320        330        340        350        360 
AELNNRERFS PIVEGLENNE ALHLQVACMQ FINALVTSPY DLDFRIHLRN EFLRCGLKAM 

       370        380        390        400        410        420 
LPTLKEIENE GLDIQLRVFE ENKEDDLSEL SHRLNDIRAE MDDINEVYHL LYNMLKDTAA 

       430        440        450        460        470        480 
EPYLLSILQH FLLIRNDYYI RPQYYKIIEE CVSQIVLHCS GMDPDFKYRQ RIDFDFTHLL 

       490        500        510        520        530        540 
DACVNKAKVE ENEQKAMEFS KKFDEEFTAR QEAQAELQKR DEKIKELETE IQQLRGQGVP 

       550        560        570        580        590        600 
SAIPGPPPPP PLPGAGPCPP PPPPPPPPPP LPGVVPPPPP PLPGMPGIPP PPPPPLSGVP 

       610        620        630        640        650        660 
PPPPPPGGVF PLLSGPIELP YGMKQKKLYK PDIPMKRINW SKIEPKELSE NCVWLKLKEE 

       670        680        690        700        710        720 
KYENADLFAK LALTFPSQMK GQRNTEAAEE NRSGPPKKKV KELRILDTKT AQNLSIFLGS 

       730        740        750        760        770        780 
YRMPYEEIKN IILEVNEEML SEALIQNLVK YLPDQNALRE LAQLKSEYDD LCEPEQFGVV 

       790        800        810        820        830        840 
MSTVKMLRPR LTSILFKLTF EEHVNNIKPS IIAVTLACEE LKKSESFKRL LELILLVGNY 

       850        860        870        880        890        900 
MNSGSRNAQS LGFKINFLCK IKDTKSADQK STLLHFLAEI CDEKYRDILK FPDELEHVES 

       910        920        930        940        950        960 
AGKVSAQILK SNLVAMEQSI LHLEKNIKNF PPAESHHDKF VEKMMSFTQN AREQYDKLST 

       970        980        990       1000       1010       1020 
MHSNMLKLYE SLGEYFIFDP NTVNMEEFFG DLNTFRTLFL EALKENHKRK EMEEKSRRAK 

      1030       1040       1050       1060       1070       1080 
LAKEKAEQEK LERQKKKKQL IDINKEGDET GVMDNLLEAL QSGAAFRDRR KRIPRNPDNR 

      1090 
RPPLERSRSR HNGAMSSK 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
Strain: NOD.
Tissue: Thymus.
[2]"A human homologue of the Drosophila melanogaster diaphanous gene is disrupted in a patient with premature ovarian failure: evidence for conserved function in oogenesis and implications for human sterility."
Bione S., Sala C., Manzini C., Arrigo G., Zuffardi O., Banfi S., Borsani G., Jonveaux P., Philippe C., Zuccotti M., Ballabio A., Toniolo D.
Am. J. Hum. Genet. 62:533-541(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 750-1098.
Strain: BALB/c.
[3]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK088648 mRNA. Translation: BAC40476.1. Sequence problems.
Y15910 mRNA. Translation: CAA75871.1.
RefSeqXP_006528645.1. XM_006528582.1.
UniGeneMm.10763.

3D structure databases

ProteinModelPortalO70566.
SMRO70566. Positions 627-1067.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-5023280.

PTM databases

PhosphoSiteO70566.

Proteomic databases

MaxQBO70566.
PaxDbO70566.
PRIDEO70566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000113320; ENSMUSP00000108946; ENSMUSG00000034480.
GeneID54004.
KEGGmmu:54004.

Organism-specific databases

CTD54004.
MGIMGI:1858500. Diap2.

Phylogenomic databases

eggNOGNOG149898.
GeneTreeENSGT00730000110702.
HOGENOMHOG000293231.
HOVERGENHBG051357.
KOK05741.
PhylomeDBO70566.

Gene expression databases

BgeeO70566.
CleanExMM_DIAP2.
GenevestigatorO70566.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR027644. DIAPH2.
IPR014767. Diaphanous_autoregulatory.
IPR010465. Drf_DAD.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view]
PANTHERPTHR23213:SF174. PTHR23213:SF174. 1 hit.
PfamPF06345. Drf_DAD. 1 hit.
PF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 1 hit.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio13841926.
PROO70566.
SOURCESearch...

Entry information

Entry nameDIAP2_MOUSE
AccessionPrimary (citable) accession number: O70566
Secondary accession number(s): Q8C2G8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 16, 2004
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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