Q9VU84 (DBNL_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Drebrin-like protein

Gene names

ORF Names:

CG10083

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actin-binding adapter protein. Binds to F-actin but is not involved in actin polymerization, capping or bundling. Does not bind G-actin By similarity. Does not seem to be involved in actin-based lamella protrusion during cell migration. Ref.5
Subcellular location	Cytoplasm › cytoskeleton By similarity.
Sequence similarities	Belongs to the ABP1 family. Contains 1 ADF-H domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Domain	Coiled coil Repeat SH3 domain
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	actin binding Inferred by curator Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 531	531	Drebrin-like protein		PRO_0000270188
Regions
	Domain	2 – 133	132	ADF-H
	Domain	472 – 531	60	SH3
	Coiled coil	177 – 220	44	Potential
	Compositional bias	321 – 358	38	Pro-rich
Amino acid modifications
	Modified residue	242	1	Phosphoserine Ref.7
	Modified residue	328	1	Phosphoserine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9VU84 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: A1CAAFA251F151C7	FASTA	531	58,729
	10 20 30 40 50 60 MAVSFEKNRA QIVAAWKDVL DDKSDTNWSL FGYEGQTNEL KVVATGDGGV DELNEDLNSG 70 80 90 100 110 120 KIMYAFVRIE DPKTGLNKYL LINWQGEGAP VLRKGTCANH IRDVSNLLSG AHLTINARNE 130 140 150 160 170 180 DDIDLDRLLK KLSTVSSAYS FKEPRGAMEE QKAPVGTNYT RVIPTKELNA SVMQDFWKKE 190 200 210 220 230 240 EAEEKLRQEA EKESKRLELQ KLEQEQRSRE EKEHKEREKL VISTTKLQPA HVPIKTSPQP 250 260 270 280 290 300 LSPEKTAPGF ANNLTDAERM RQARNQEARE LIGSRVGAAK AMFTKHTSEG QLQSKLNTQP 310 320 330 340 350 360 PAKPARNSIA QRINVFNQNQ PQDAPVPSPP RAASPAKPLP VEAPEPVVPA PAIAPAAPVA 370 380 390 400 410 420 AEVVSTIAEV EESQPVDDLP LAHESEQFST IKRSPHSKSN SLQSQSPDET TSSNETDTAV 430 440 450 460 470 480 SQEQEEEVRT KVSVTVQQSQ SVKSSGMSTL ERNALTDLVN EDDFICQETL GDLGQRARAL 490 500 510 520 530 YDYQAADETE ITFDPGDVIT HIDQIDEGWW QGLGPDGTYG LFPANYVEII N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"Flying through the Drosophila cytoskeletal genome." Goldstein L.S., Gunawardena S. J. Cell Biol. 150:F63-F68(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[5]	"Molecular requirements for actin-based lamella formation in Drosophila S2 cells." Rogers S.L., Wiedemann U., Stuurman N., Vale R.D. J. Cell Biol. 162:1079-1088(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, MASS SPECTROMETRY.
[7]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014296 Genomic DNA. Translation: AAF49805.1. AY119287 mRNA. Translation: AAM51147.1. BT021389 mRNA. Translation: AAX33537.1.
RefSeq	NP_648657.1. NM_140400.2.
UniGene	Dm.13622.
3D structure databases
HSSP	HSSP built from PDB template 2D1X based on UniProtKB Q14247.
ProteinModelPortal	Q9VU84.
SMR	Q9VU84. Positions 1-138, 472-529.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1645145.
Proteomic databases
PaxDb	Q9VU84.
PRIDE	Q9VU84.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0075819; FBpp0075561; FBgn0036372.
GeneID	39520.
KEGG	dme:Dmel_CG10083.
UCSC	CG10083-RA. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0036372. CG10083.
Phylogenomic databases
eggNOG	NOG265859.
GeneTree	ENSGT00530000062953.
InParanoid	Q9VU84.
OMA	EQETFYE.
OrthoDB	EOG46HDS6.
PhylomeDB	Q9VU84.
Gene expression databases
Bgee	Q9VU84.
Family and domain databases
InterPro	IPR002108. Actin-bd_cofilin/tropomyosin. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00241. Cofilin_ADF. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00452. SH3DOMAIN.
SMART	SM00102. ADF. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS51263. ADF_H. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	39520.
NextBio	814077.

Entry information

Entry name

DBNL_DROME

Accession

Primary (citable) accession number: Q9VU84
Secondary accession number(s): Q8MRS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project