DIAP2_MOUSE
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 03-AUG-2022, entry version 156.
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};
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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; 284 antibodies from 34 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
