DIA_DROME
ID DIA_DROME Reviewed; 1091 AA.
AC P48608; Q5BI26; Q9VIJ7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Protein diaphanous;
GN Name=dia; ORFNames=CG1768;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7821209; DOI=10.1242/dev.120.12.3367;
RA Castrillon D.H., Wasserman S.A.;
RT "Diaphanous is required for cytokinesis in Drosophila and shares domains of
RT similarity with the products of the limb deformity gene.";
RL Development 120:3367-3377(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=10751177; DOI=10.1242/dev.127.9.1887;
RA Afshar K., Stuart B., Wasserman S.A.;
RT "Functional analysis of the Drosophila diaphanous FH protein in early
RT embryonic development.";
RL Development 127:1887-1897(2000).
CC -!- FUNCTION: Required for cytokinesis in both mitosis and meiosis. Has a
CC role in actin cytoskeleton organization and is essential for many, if
CC not all, actin-mediated events involving membrane invagination. May
CC serve as a mediator between signaling molecules and actin organizers at
CC specific phases of the cell cycle. Possible component of the
CC contractile ring or may control its function.
CC {ECO:0000269|PubMed:10751177, ECO:0000269|PubMed:7821209}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:7821209}. Cleavage furrow
CC {ECO:0000269|PubMed:7821209}. Note=Localizes to the site where the
CC metaphase furrow is anticipated to form, to the growing tip of
CC cellularization furrows, and to contractile rings.
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}.
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DR EMBL; U11288; AAA67715.1; -; mRNA.
DR EMBL; AE014134; AAF53922.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11087.1; -; Genomic_DNA.
DR EMBL; BT021398; AAX33546.1; -; mRNA.
DR PIR; T13170; T13170.
DR RefSeq; NP_001260640.1; NM_001273711.1.
DR RefSeq; NP_476981.1; NM_057633.5.
DR RefSeq; NP_724285.1; NM_165341.3.
DR AlphaFoldDB; P48608; -.
DR SMR; P48608; -.
DR BioGRID; 61303; 26.
DR DIP; DIP-22062N; -.
DR IntAct; P48608; 9.
DR STRING; 7227.FBpp0297103; -.
DR PaxDb; P48608; -.
DR PRIDE; P48608; -.
DR DNASU; 35340; -.
DR EnsemblMetazoa; FBtr0081410; FBpp0080940; FBgn0011202.
DR EnsemblMetazoa; FBtr0081411; FBpp0080941; FBgn0011202.
DR EnsemblMetazoa; FBtr0335145; FBpp0307144; FBgn0011202.
DR GeneID; 35340; -.
DR KEGG; dme:Dmel_CG1768; -.
DR UCSC; CG1768-RA; d. melanogaster.
DR CTD; 35340; -.
DR FlyBase; FBgn0011202; dia.
DR VEuPathDB; VectorBase:FBgn0011202; -.
DR eggNOG; KOG1924; Eukaryota.
DR GeneTree; ENSGT00940000170492; -.
DR HOGENOM; CLU_002356_0_1_1; -.
DR InParanoid; P48608; -.
DR OMA; WEVKNPM; -.
DR OrthoDB; 1204639at2759; -.
DR PhylomeDB; P48608; -.
DR Reactome; R-DME-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DME-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-8980692; RHOA GTPase cycle.
DR Reactome; R-DME-9013026; RHOB GTPase cycle.
DR Reactome; R-DME-9013106; RHOC GTPase cycle.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR Reactome; R-DME-9035034; RHOF GTPase cycle.
DR SignaLink; P48608; -.
DR BioGRID-ORCS; 35340; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35340; -.
DR PRO; PR:P48608; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0011202; Expressed in adult hindgut (Drosophila) and 32 other tissues.
DR ExpressionAtlas; P48608; baseline and differential.
DR Genevisible; P48608; DM.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031430; C:M band; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0012506; C:vesicle membrane; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IMP:FlyBase.
DR GO; GO:0031267; F:small GTPase binding; IMP:FlyBase.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR GO; GO:0045010; P:actin nucleation; IDA:FlyBase.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IMP:FlyBase.
DR GO; GO:0003383; P:apical constriction; IMP:FlyBase.
DR GO; GO:0106036; P:assembly of apicomedial cortex actomyosin; IDA:FlyBase.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0032507; P:maintenance of protein location in cell; IMP:FlyBase.
DR GO; GO:0007110; P:meiosis I cytokinesis; IMP:FlyBase.
DR GO; GO:0007111; P:meiosis II cytokinesis; IMP:FlyBase.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0045448; P:mitotic cell cycle, embryonic; IMP:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0097320; P:plasma membrane tubulation; IMP:FlyBase.
DR GO; GO:0007279; P:pole cell formation; IMP:FlyBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:FlyBase.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR GO; GO:0009306; P:protein secretion; IMP:FlyBase.
DR GO; GO:0030589; P:pseudocleavage involved in syncytial blastoderm formation; IMP:FlyBase.
DR GO; GO:0110020; P:regulation of actomyosin structure organization; IMP:FlyBase.
DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
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; IPR010465; Drf_DAD.
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 Pfam; PF06345; Drf_DAD; 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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..1091
FT /note="Protein diaphanous"
FT /id="PRO_0000194892"
FT DOMAIN 59..431
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 512..596
FT /note="FH1"
FT DOMAIN 601..1001
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1022..1054
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 446..500
FT /evidence="ECO:0000255"
FT COILED 967..1021
FT /evidence="ECO:0000255"
FT COMPBIAS 507..589
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 733
FT /note="H -> Q (in Ref. 1; AAA67715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1091 AA; 123171 MW; A4379D7A089B5EE7 CRC64;
MSRHEKTKST GGGLLDSLFG RPSKSKGGTI SSGTLAHGGR PVSADNYVVP GVEDFEQYIQ
QLSVAELDAK FLEIIEDMNI PKDKREPLLA KSKEERQKMI MWHLKGKNSL ERSANSRFEK
PIDYVEYLQN GEHSTHKVYQ CVESLRVALT SNPISWIKEF GVAGIGTIEK LLARSKNNAS
YEKIEFEAIR CLKAIMNNTW GLNVVLNPDQ HSVVLLLAQS LDPRKPQTMC EALKLLASFC
IVYERNGYEK VLRAITTIAA TSFKASERFR PIVDALFASD QQDPKRDLAC HSLIFINTLT
NTPTDLNFRL HLRCEIMRMG LYDRLDEFTK IVEASNNENL QQHFKIFNEI REDDFEEFVQ
RFDNVTFNMD DATDCFDVLK NLVTDTTSEP YFLSILQHLL YIRDDFYFRP AYYQLIEECI
SQIVFHKGYC DPNFENRNFN IDTSLLLDDI VEKAKAKESK RSEEYEKKIE QLESAKQEAE
AKAAHLEEKV KLMEANGVAA PSPNKLPKVN IPMPPPPPGG GGAPPPPPPP MPGRAGGGPP
PPPPPPMPGR AGGPPPPPPP PGMGGPPPPP MPGMMRPGGG PPPPPMMMGP MVPVLPHGLK
PKKKWDVKNP MKRANWKAIV PAKMSDKAFW VKCQEDKLAQ DDFLAELAVK FSSKPVKKEQ
KDAVDKPTTL TKKNVDLRVL DSKTAQNLAI MLGGSLKHLS YEQIKICLLR CDTDILSSNI
LQQLIQYLPP PEHLKRLQEI KAKGEPLPPI EQFAATIGEI KRLSPRLHNL NFKLTYADMV
QDIKPDIVAG TAACEEIRNS KKFSKILELI LLLGNYMNSG SKNEAAFGFE ISYLTKLSNT
KDADNKQTLL HYLADLVEKK FPDALNFYDD LSHVNKASRV NMDAIQKAMR QMNSAVKNLE
TDLQNNKVPQ CDDDKFSEVM GKFAEECRQQ VDVLGKMQLQ MEKLYKDLSE YYAFDPSKYT
MEEFFADIKT FKDAFQAAHN DNVRVREELE KKRRLQEARE QSAREQQERQ QRKKAVVDMD
APQTQEGVMD SLLEALQTGS AFGQRNRQAR RQRPAGAERR AQLSRSRSRT RVTNGQLMTR
EMILNEVLGS A
