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   04-NOV-2026, entry version 204.
DE   RecName: Full=Protein diaphanous;
GN   Name=dia; ORFNames=CG1768;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; 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).
RN   [6]
RP   INTERACTION WITH RHO1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DOMAIN,
RP   AND MUTAGENESIS OF 147-VAL--SER-151.
RX   PubMed=23853710; DOI=10.7554/elife.00666;
RA   Rousso T., Shewan A.M., Mostov K.E., Schejter E.D., Shilo B.Z.;
RT   "Apical targeting of the formin Diaphanous in Drosophila tubular
RT   epithelia.";
RL   Elife 2:e00666-e00666(2013).
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   -!- SUBUNIT: May interact (via CBD/FH3 domain) with Rho1.
CC       {ECO:0000269|PubMed:23853710}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:7821209}. Cleavage furrow
CC       {ECO:0000269|PubMed:7821209}. Apical cell membrane
CC       {ECO:0000269|PubMed:23853710}. 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 (PubMed:7821209).
CC       Recruited to the apical cell membrane of epithelial cells in a Rho1
CC       dependent manner, enhanced by phosphatidylinositol 4,5-bisphosphate
CC       (PtdIns[4,5]P(2)) enrichment established by sktl/skittles and Pten
CC       (PubMed:23853710). {ECO:0000269|PubMed:23853710,
CC       ECO:0000269|PubMed:7821209}.
CC   -!- DEVELOPMENTAL STAGE: In stage 15 embryos expressed in epithelial cells
CC       of various tubular tissues including trachea, hindgut and salivary
CC       gland (at protein level). {ECO:0000269|PubMed:23853710}.
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). DAD-mediated autoinhibition negatively
CC       regulates dia localization to the apical cell cortex (PubMed:23853710).
CC       {ECO:0000250, ECO:0000269|PubMed:23853710}.
CC   -!- DOMAIN: The N terminal basic region is enriched in basic amino acids
CC       that may mediate interaction with negatively charged
CC       phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)). It is
CC       required, but not sufficient on its own, for efficient apical
CC       localization in polarized epithelial cells.
CC       {ECO:0000269|PubMed:23853710}.
CC   -!- DOMAIN: The GTPase binding domain (GBD) probably mediates interaction
CC       with Rho1 required for disruption of autoinhibition and targeted
CC       recruitment to the apical membrane of polarised epithelial cells.
CC       {ECO:0000269|PubMed:23853710}.
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   FunCoup; P48608; 396.
DR   IntAct; P48608; 11.
DR   STRING; 7227.FBpp0297103; -.
DR   PaxDb; 7227-FBpp0297103; -.
DR   PeptideAtlas; 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   AGR; FB:FBgn0011202; -.
DR   CTD; 35340; -.
DR   FlyBase; FBgn0011202; dia.
DR   VEuPathDB; VectorBase:FBgn0011202; -.
DR   eggNOG; KOG1924; Eukaryota.
DR   HOGENOM; CLU_002356_0_1_1; -.
DR   InParanoid; P48608; -.
DR   OrthoDB; 1104827at2759; -.
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-9013149; RAC1 GTPase cycle.
DR   Reactome; R-DME-9013406; RHOQ GTPase cycle.
DR   Reactome; R-DME-9013423; RAC3 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 Malpighian tubule principal cell of lower ureter in Malpighian tubule and 169 other cell types or tissues.
DR   ExpressionAtlas; P48608; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
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:0030036; P:actin cytoskeleton organization; 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:0008104; P:intracellular protein localization; 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: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   FunFam; 1.20.58.630:FF:000002; Diaphanous, isoform D; 1.
DR   FunFam; 1.20.58.2220:FF:000015; Diaphanous, isoform E; 1.
DR   FunFam; 1.25.10.10:FF:000603; Diaphanous, isoform E; 1.
DR   Gene3D; 1.20.58.630; -; 1.
DR   Gene3D; 6.10.30.30; -; 1.
DR   Gene3D; 1.10.20.40; Formin, diaphanous GTPase-binding domain; 1.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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   PANTHER; PTHR45691; PROTEIN DIAPHANOUS; 1.
DR   PANTHER; PTHR45691:SF6; PROTEIN DIAPHANOUS; 1.
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; ARM repeat; 1.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell cycle; Cell division; Cell membrane; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Membrane; 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..56
FT                   /note="Basic region"
FT                   /evidence="ECO:0000269|PubMed:23853710"
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          455..496
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        25..34
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..572
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1010
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         147..151
FT                   /note="VALTS->DALTE: Disruption of interaction with small
FT                   GTPase Rho1 and failure to recruit to apical membranes."
FT                   /evidence="ECO:0000269|PubMed:23853710"
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
//