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 12-OCT-2022, entry version 157. DE RecName: Full=Protein diaphanous homolog 2; DE AltName: Full=Diaphanous-related formin-2; DE Short=DRF2; DE Short=mDia3; GN Name=Diaph2; Synonyms=Diap2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., 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., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., 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. RC STRAIN=BALB/cJ; RX 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., 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 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., Chen M., RA Wallar B.J., Alberts A.S., Gundersen G.G.; RT "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and RT promote cell migration."; RL Nat. Cell Biol. 6:820-830(2004). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: May be involved in oogenesis. CC -!- SUBUNIT: Interacts with MAPRE1 and APC. {ECO:0000269|PubMed:15311282}. CC -!- DEVELOPMENTAL STAGE: Expressed in liver, heart, kidney, ovary and CC testis, at 16 dpc, P6 and P16. CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory CC interaction with the GBD/FH3 domain. This autoinhibition is released CC upon competitive binding of an activated GTPase. The release of DAD CC allows the FH2 domain to then nucleate and elongate nonbranched actin CC filaments (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC40476.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; 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; ALT_SEQ; mRNA. DR EMBL; Y15910; CAA75871.1; -; mRNA. DR RefSeq; XP_006528645.1; XM_006528582.3. DR AlphaFoldDB; O70566; -. DR SMR; O70566; -. DR BioGRID; 207557; 11. DR IntAct; O70566; 2. DR STRING; 10090.ENSMUSP00000039334; -. DR iPTMnet; O70566; -. DR PhosphoSitePlus; O70566; -. DR EPD; O70566; -. DR MaxQB; O70566; -. DR PaxDb; O70566; -. DR PRIDE; O70566; -. DR ProteomicsDB; 279539; -. DR Antibodypedia; 471; 282 antibodies from 33 providers. DR DNASU; 54004; -. DR Ensembl; ENSMUST00000113320; ENSMUSP00000108946; ENSMUSG00000034480. DR GeneID; 54004; -. DR CTD; 1730; -. DR MGI; MGI:1858500; Diaph2. DR VEuPathDB; HostDB:ENSMUSG00000034480; -. DR eggNOG; KOG1924; Eukaryota. DR GeneTree; ENSGT00940000157822; -. DR HOGENOM; CLU_002356_0_0_1; -. DR InParanoid; O70566; -. DR PhylomeDB; O70566; -. DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins. DR Reactome; R-MMU-9013405; RHOD GTPase cycle. DR Reactome; R-MMU-9035034; RHOF GTPase cycle. DR BioGRID-ORCS; 54004; 3 hits in 37 CRISPR screens. DR ChiTaRS; Diaph2; mouse. DR PRO; PR:O70566; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; O70566; protein. DR Bgee; ENSMUSG00000034480; Expressed in olfactory tubercle and 231 other tissues. DR ExpressionAtlas; O70566; baseline and differential. DR Genevisible; O70566; MM. DR GO; GO:0005884; C:actin filament; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0003779; F:actin binding; IDA:MGI. DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro. DR GO; GO:0030041; P:actin filament polymerization; IDA:MGI. DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW. DR Gene3D; 1.10.20.40; -; 1. DR Gene3D; 1.20.58.2220; -; 1. DR Gene3D; 1.25.10.10; -; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR014767; DAD_dom. DR InterPro; IPR044933; DIA_GBD_sf. DR InterPro; IPR027644; DIAPH2. DR InterPro; IPR015425; FH2_Formin. DR InterPro; IPR042201; FH2_Formin_sf. DR InterPro; IPR010472; FH3_dom. DR InterPro; IPR014768; GBD/FH3_dom. DR InterPro; IPR010473; GTPase-bd. DR PANTHER; PTHR45691:SF3; PTHR45691:SF3; 1. DR Pfam; PF06367; Drf_FH3; 1. DR Pfam; PF06371; Drf_GBD; 1. DR Pfam; PF02181; FH2; 1. DR SMART; SM01139; Drf_FH3; 1. DR SMART; SM01140; Drf_GBD; 1. DR SMART; SM00498; FH2; 1. DR SUPFAM; SSF48371; SSF48371; 1. DR PROSITE; PS51231; DAD; 1. DR PROSITE; PS51444; FH2; 1. DR PROSITE; PS51232; GBD_FH3; 1. PE 1: Evidence at protein level; KW Acetylation; Coiled coil; Developmental protein; Differentiation; KW Oogenesis; Reference proteome; Repeat. FT CHAIN 1..1098 FT /note="Protein diaphanous homolog 2" FT /id="PRO_0000194896" FT DOMAIN 90..463 FT /note="GBD/FH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579" FT DOMAIN 544..620 FT /note="FH1" FT DOMAIN 625..1025 FT /note="FH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774" FT DOMAIN 1048..1078 FT /note="DAD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577" FT REGION 1..62 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 537..565 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 578..611 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 679..699 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1007..1047 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1063..1098 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 375..416 FT /evidence="ECO:0000255" FT COILED 490..539 FT /evidence="ECO:0000255" FT COILED 999..1050 FT /evidence="ECO:0000255" FT COMPBIAS 22..62 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 541..565 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 685..699 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1064..1092 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:O60879" FT CONFLICT 750..751 FT /note="KY -> RD (in Ref. 2; CAA75871)" FT /evidence="ECO:0000305" 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 //