ID DIAP2_MOUSE Reviewed; 1098 AA. AC O70566; Q8C2G8; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 16-FEB-2004, sequence version 2. DT 31-OCT-2006, entry version 52. DE Protein diaphanous homolog 2 (Diaphanous-related formin-2) (DRF2) DE (mDia3). GN Name=Diaph2; Synonyms=Diap2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=NOD; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 750-1098 (ISOFORM 1). RC STRAIN=BALB/c; RX MEDLINE=98163437; PubMed=9497258; DOI=10.1086/301761; RA Bione S., Sala C., Manzini C., Arrigo G., Zuffardi O., Banfi S., RA Borsani G., Jonveaux P., Philippe C., Zuccotti M., Ballabio A., RA Toniolo D.; RT "A human homologue of the Drosophila melanogaster diaphanous gene is RT disrupted in a patient with premature ovarian failure: evidence for RT conserved function in oogenesis and implications for human RT sterility."; RL Am. J. Hum. Genet. 62:533-541(1998). RN [3] RP INTERACTION WITH APC AND MAPRE1. RX PubMed=15311282; DOI=10.1038/ncb1160; RA Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S., RA Chen M., Wallar B.J., Alberts A.S., Gundersen G.G.; RT "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho RT and promote cell migration."; RL Nat. Cell Biol. 6:820-830(2004). CC -!- FUNCTION: May be involved in oogenesis. CC -!- SUBUNIT: Interacts with MAPRE1 and APC. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O70566-1; Sequence=Displayed; CC Name=2; CC IsoId=O70566-2; Sequence=VSP_009424; CC Note=No experimental confirmation available; CC -!- DEVELOPMENTAL STAGE: Expressed in liver, heart, kidney, ovary and CC testis, at E16, P6 and P16. CC -!- DOMAIN: DRFs are regulated by intramolecular GBD-DAD binding where CC Rho-GTP activates the DRFs by disrupting the GBD-DAD interaction CC (By similarity). CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous CC subfamily. CC -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain. CC -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain. CC -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain. CC -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology CC 3) domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK088648; BAC40476.1; -; mRNA. DR EMBL; Y15910; CAA75871.1; -; mRNA. DR KEGG; mmu:54004; -. DR MGI; MGI:1858500; Diap2. DR ArrayExpress; O70566; -. DR GO; GO:0003779; F:actin binding; IDA:MGI. DR GO; GO:0030041; P:actin filament polymerization; IDA:MGI. DR InterPro; IPR010465; Drf_DAD. DR InterPro; IPR010472; Drf_FH3. DR InterPro; IPR010473; Drf_GTPase_bd. DR InterPro; IPR003104; FH2_actin_bd. DR Pfam; PF06345; Drf_DAD; 1. DR Pfam; PF06367; Drf_FH3; 1. DR Pfam; PF06371; Drf_GBD; 1. DR Pfam; PF02181; FH2; 1. DR SMART; SM00498; FH2; 1. DR PROSITE; PS51231; DAD; 1. DR PROSITE; PS51232; GBD_FH3; 1. KW Alternative splicing; Coiled coil; Developmental protein; KW Differentiation; Oogenesis; Repeat. FT CHAIN 1 1098 Protein diaphanous homolog 2. FT /FTId=PRO_0000194896. FT DOMAIN 90 463 GBD/FH3. FT DOMAIN 544 620 FH1. FT DOMAIN 625 1047 FH2. FT DOMAIN 1048 1078 DAD. FT COILED 375 416 Potential. FT COILED 490 539 Potential. FT COILED 999 1050 Potential. FT COMPBIAS 1035 1038 Poly-Lys. FT COMPBIAS 1069 1072 Arg/Lys-rich (basic). FT VAR_SEQ 1078 1098 DNRRPPLERSRSRHNGAMSSK -> GKTHCSLHSLVICEYS FT ISNPSSIKGKCTFSETYFS (in isoform 2). FT /FTId=VSP_009424. FT CONFLICT 750 751 KY -> RD (in Ref. 2). SQ SEQUENCE 1098 AA; 124871 MW; BB19D49E049EA8CA CRC64; MEELGAAASG AGGGGGGGEE HGGGRSNKRG AGNRAANEEE TRNKPKLRDR ITSFRKSATK REKPVIQHSI DYQTAVVEIP PALIVHDDRS LILSEKEVLD LFEKMMEDMN LNEEKKAPLR KKDFSIKREM VVQYISATSK SIVGSKVLGG LKNSKHEFTL SSQEYVHELR SGISDEKLLN CLESLRVSLT SHPVSWVNNF GYEGLGVLLD VLEKLLDKKQ QENIDKKNQY KVIQCLKAFM NNKFGLQRIL GDERSLLLLA RAIDPKQQNM MTEIVKILSA ICIVGEENIL DKLLGGITAA AELNNRERFS PIVEGLENNE ALHLQVACMQ FINALVTSPY DLDFRIHLRN EFLRCGLKAM LPTLKEIENE GLDIQLRVFE ENKEDDLSEL SHRLNDIRAE MDDINEVYHL LYNMLKDTAA EPYLLSILQH FLLIRNDYYI RPQYYKIIEE CVSQIVLHCS GMDPDFKYRQ RIDFDFTHLL DACVNKAKVE ENEQKAMEFS KKFDEEFTAR QEAQAELQKR DEKIKELETE IQQLRGQGVP SAIPGPPPPP PLPGAGPCPP PPPPPPPPPP LPGVVPPPPP PLPGMPGIPP PPPPPLSGVP PPPPPPGGVF PLLSGPIELP YGMKQKKLYK PDIPMKRINW SKIEPKELSE NCVWLKLKEE KYENADLFAK LALTFPSQMK GQRNTEAAEE NRSGPPKKKV KELRILDTKT AQNLSIFLGS YRMPYEEIKN IILEVNEEML SEALIQNLVK YLPDQNALRE LAQLKSEYDD LCEPEQFGVV MSTVKMLRPR LTSILFKLTF EEHVNNIKPS IIAVTLACEE LKKSESFKRL LELILLVGNY MNSGSRNAQS LGFKINFLCK IKDTKSADQK STLLHFLAEI CDEKYRDILK FPDELEHVES AGKVSAQILK SNLVAMEQSI LHLEKNIKNF PPAESHHDKF VEKMMSFTQN AREQYDKLST MHSNMLKLYE SLGEYFIFDP NTVNMEEFFG DLNTFRTLFL EALKENHKRK EMEEKSRRAK LAKEKAEQEK LERQKKKKQL IDINKEGDET GVMDNLLEAL QSGAAFRDRR KRIPRNPDNR RPPLERSRSR HNGAMSSK //