Reviewed, UniProtKB/Swiss-Prot P48608 (DIA_DROME)

Names and origin

Protein names

Recommended name:
    Protein diaphanous

Gene names

Name:	dia
ORF Names:	CG1768

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1091 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for cytokinesis in both mitosis and meiosis. Has a role in actin cytoskeleton organization and is essential for many, if not all, actin-mediated events involving membrane invagination. May serve as a mediator between signaling molecules and actin organizers at specific phases of the cell cycle. Possible component of the contractile ring or may control its function. Ref.1 Ref.5
Subcellular location	Cytoplasm › cytoskeleton. Note: Localizes to the site where the metaphase furrow is anticipated to form, to the growing tip of cellularization furrows, and to contractile rings. Ref.1
Domain	DRFs are regulated by intramolecular GBD-DAD binding where Rho-GTP activates the DRFs by disrupting the GBD-DAD interaction By similarity.
Sequence similarities	Belongs to the formin homology family. Diaphanous subfamily. Contains 1 DAD (diaphanous autoregulatory) domain. Contains 1 FH1 (formin homology 1) domain. Contains 1 FH2 (formin homology 2) domain. Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm Cytoskeleton
Domain	Coiled coil
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	actin filament organization Ref.5 Inferred from mutant phenotype. Source: FlyBase cytokinesis after meiosis I Inferred from mutant phenotype. Source: FlyBase cytokinesis after meiosis II Inferred from mutant phenotype. Source: FlyBase cytokinesis, contractile ring formation Inferred from mutant phenotype. Source: FlyBase maintenance of protein location in cell Inferred from mutant phenotype. Source: FlyBase mitotic cell cycle, embryonic Ref.5 Inferred from mutant phenotype. Source: FlyBase open tracheal system development Inferred from mutant phenotype. Source: FlyBase pole cell formation Ref.5 Inferred from mutant phenotype. Source: FlyBase spermatogenesis Inferred from mutant phenotype. Source: FlyBase spindle assembly Inferred from mutant phenotype. Source: FlyBase
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	Rho GTPase binding Inferred from electronic annotation. Source: InterPro actin binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VZQ7	1	EBI-135200,EBI-162402

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1091	1091	Protein diaphanous		PRO_0000194892
Regions
	Domain	59 – 431	373	GBD/FH3
	Domain	512 – 596	85	FH1
	Domain	601 – 1001	401	FH2
	Domain	1022 – 1054	33	DAD
	Coiled coil	446 – 500	55	Potential
	Coiled coil	967 – 1021	55	Potential
	Compositional bias	512 – 518	7	Poly-Pro
	Compositional bias	519 – 522	4	Poly-Gly
	Compositional bias	524 – 532	9	Poly-Pro
	Compositional bias	539 – 548	10	Poly-Pro
	Compositional bias	554 – 561	8	Poly-Pro
	Compositional bias	566 – 572	7	Poly-Pro
	Compositional bias	581 – 585	5	Poly-Pro
	Compositional bias	1050 – 1053	4	Arg-rich (basic)
Experimental info
	Sequence conflict	733	1	H → Q in AAA67715. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P48608-1 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: A4379D7A089B5EE7	FASTA	1,091	123,171
	10 20 30 40 50 60 MSRHEKTKST GGGLLDSLFG RPSKSKGGTI SSGTLAHGGR PVSADNYVVP GVEDFEQYIQ 70 80 90 100 110 120 QLSVAELDAK FLEIIEDMNI PKDKREPLLA KSKEERQKMI MWHLKGKNSL ERSANSRFEK 130 140 150 160 170 180 PIDYVEYLQN GEHSTHKVYQ CVESLRVALT SNPISWIKEF GVAGIGTIEK LLARSKNNAS 190 200 210 220 230 240 YEKIEFEAIR CLKAIMNNTW GLNVVLNPDQ HSVVLLLAQS LDPRKPQTMC EALKLLASFC 250 260 270 280 290 300 IVYERNGYEK VLRAITTIAA TSFKASERFR PIVDALFASD QQDPKRDLAC HSLIFINTLT 310 320 330 340 350 360 NTPTDLNFRL HLRCEIMRMG LYDRLDEFTK IVEASNNENL QQHFKIFNEI REDDFEEFVQ 370 380 390 400 410 420 RFDNVTFNMD DATDCFDVLK NLVTDTTSEP YFLSILQHLL YIRDDFYFRP AYYQLIEECI 430 440 450 460 470 480 SQIVFHKGYC DPNFENRNFN IDTSLLLDDI VEKAKAKESK RSEEYEKKIE QLESAKQEAE 490 500 510 520 530 540 AKAAHLEEKV KLMEANGVAA PSPNKLPKVN IPMPPPPPGG GGAPPPPPPP MPGRAGGGPP 550 560 570 580 590 600 PPPPPPMPGR AGGPPPPPPP PGMGGPPPPP MPGMMRPGGG PPPPPMMMGP MVPVLPHGLK 610 620 630 640 650 660 PKKKWDVKNP MKRANWKAIV PAKMSDKAFW VKCQEDKLAQ DDFLAELAVK FSSKPVKKEQ 670 680 690 700 710 720 KDAVDKPTTL TKKNVDLRVL DSKTAQNLAI MLGGSLKHLS YEQIKICLLR CDTDILSSNI 730 740 750 760 770 780 LQQLIQYLPP PEHLKRLQEI KAKGEPLPPI EQFAATIGEI KRLSPRLHNL NFKLTYADMV 790 800 810 820 830 840 QDIKPDIVAG TAACEEIRNS KKFSKILELI LLLGNYMNSG SKNEAAFGFE ISYLTKLSNT 850 860 870 880 890 900 KDADNKQTLL HYLADLVEKK FPDALNFYDD LSHVNKASRV NMDAIQKAMR QMNSAVKNLE 910 920 930 940 950 960 TDLQNNKVPQ CDDDKFSEVM GKFAEECRQQ VDVLGKMQLQ MEKLYKDLSE YYAFDPSKYT 970 980 990 1000 1010 1020 MEEFFADIKT FKDAFQAAHN DNVRVREELE KKRRLQEARE QSAREQQERQ QRKKAVVDMD 1030 1040 1050 1060 1070 1080 APQTQEGVMD SLLEALQTGS AFGQRNRQAR RQRPAGAERR AQLSRSRSRT RVTNGQLMTR 1090 EMILNEVLGS A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene." Castrillon D.H., Wasserman S.A. Development 120:3367-3377(1994) [PubMed: 7821209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Functional analysis of the Drosophila diaphanous FH protein in early embryonic development." Afshar K., Stuart B., Wasserman S.A. Development 127:1887-1897(2000) [PubMed: 10751177] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U11288 mRNA. Translation: AAA67715.1. AE014134 Genomic DNA. Translation: AAF53922.1. AE014134 Genomic DNA. Translation: AAN11087.1. BT021398 mRNA. Translation: AAX33546.1.
PIR	T13170.
RefSeq	NP_476981.1. NP_724285.1.
UniGene	Dm.4235
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:22062N.
IntAct	P48608. 2 interactions.
Proteomic databases
PRIDE	P48608.
Genome annotation databases
Ensembl	FBgn0011202. Drosophila melanogaster. [Contig view]
GeneID	35340.
KEGG	dme:Dmel_CG1768.
Organism-specific databases
FlyBase	FBgn0011202. dia.
Phylogenomic databases
HOGENOM	P48608.
OMA	P48608. MEANGVA.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-009674-MON. DMEL-XXX-02:DMEL-XXX-02-009675-MON.
Gene expression databases
ArrayExpress	P48608.
GermOnline	CG1768. Drosophila melanogaster.
Family and domain databases
InterPro	IPR014767. Diaphanous_autoregulatory. IPR010465. Drf_DAD. IPR010472. Drf_FH3. IPR010473. Drf_GTPase_bd. IPR015425. FH2_actin_bd. IPR003104. FH2_actin_bd_DRF. IPR014768. GTPase_bd/formin_homology_3. [Graphical view]
Pfam	PF06345. Drf_DAD. 1 hit. PF06367. Drf_FH3. 1 hit. PF06371. Drf_GBD. 1 hit. PF02181. FH2. 1 hit. [Graphical view]
SMART	SM00498. FH2. 1 hit. [Graphical view]
PROSITE	PS51231. DAD. 1 hit. PS51444. FH2. 1 hit. PS51232. GBD_FH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	793046.

Entry information

Entry name

DIA_DROME

Accession

Primary (citable) accession number: P48608
Secondary accession number(s): Q5BI26, Q9VIJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 21, 2001
Last modified:	June 16, 2009
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project