P23023 (DSX_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein doublesex

Gene names

Name:	dsx
ORF Names:	CG11094

Organism

Drosophila melanogaster (Fruit fly)

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	549 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Controls somatic sexual differentiation. Binds directly and specifically to the FBE (fat body enhancer) of the yolk protein 1 and 2 genes (Yp1 and Yp2). This enhancer is sufficient to direct the female-specific transcription characteristic of the Yp genes in adult fat bodies. Involved in regulation of male-specific expression of takeout in brain-associated fat body. Ref.7
Subcellular location	Nucleus.
Miscellaneous	Experimentally shown to bind zinc.
Sequence similarities	Contains 1 DM DNA-binding domain.

Ontologies

Keywords
Biological process	Differentiation Sexual differentiation Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding Metal-binding Zinc
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	axon midline choice point recognition Inferred from mutant phenotype. Source: FlyBase central nervous system development Traceable author statement. Source: FlyBase female analia development Non-traceable author statement. Source: FlyBase female somatic sex determination Non-traceable author statement. Source: FlyBase genital disc morphogenesis Traceable author statement. Source: FlyBase genital disc sexually dimorphic development Traceable author statement. Source: FlyBase imaginal disc-derived female genitalia development Inferred from mutant phenotype. Source: FlyBase imaginal disc-derived male genitalia development Inferred from genetic interaction. Source: FlyBase male analia development Non-traceable author statement. Source: FlyBase male courtship behavior, veined wing generated song production Non-traceable author statement. Source: FlyBase male sex differentiation Traceable author statement. Source: FlyBase male somatic sex determination Non-traceable author statement. Source: FlyBase negative regulation of developmental pigmentation Traceable author statement. Source: FlyBase negative regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: FlyBase nuclear mRNA splicing, via spliceosome Traceable author statement. Source: FlyBase positive regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: FlyBase regulation of imaginal disc growth Traceable author statement. Source: FlyBase sex comb development Traceable author statement. Source: FlyBase sex-specific pigmentation Non-traceable author statement. Source: FlyBase spermatogenesis Non-traceable author statement. Source: FlyBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	mRNA binding Non-traceable author statement. Source: FlyBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from direct assay. Source: FlyBase sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Non-traceable author statement. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
C901	Q9VZ44	1	EBI-196709,EBI-172504
Cas	Q9XZU1	1	EBI-196709,EBI-126291
CG34168-RA	Q9VJM1	1	EBI-196709,EBI-121063

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Male (identifier: P23023-1)

Also known as: A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Female (identifier: P23023-2)

Also known as: B; C;

The sequence of this isoform differs from the canonical sequence as follows:
     398-427: ARVEINRTVAQIYYNYYTPMALVNGAPMYL → GQYVVNEYSRQHNLNIYDGGELRNTTRQCG
     428-549: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 549

549

Protein doublesex

PRO_0000207041

Regions

DNA binding

44 – 91

48

DM Ref.5 Ref.6

Compositional bias

119 – 224

106

His-rich

Compositional bias

267 – 296

30

Gly/Ser-rich

Natural variations

Alternative sequence

398 – 427

30

ARVEI…APMYL → GQYVVNEYSRQHNLNIYDGG ELRNTTRQCG in isoform Female.

VSP_001321

Alternative sequence

428 – 549

122

Missing in isoform Female.

VSP_001322

Experimental info

Mutagenesis

47

1

C → A or H: Abolishes DNA-binding.

Mutagenesis

50

1

H → Y: Abolishes DNA-binding.

Mutagenesis

59

1

H → Y: Abolishes DNA-binding.

Mutagenesis

68

1

C → D or Y: Abolishes DNA-binding.

Mutagenesis

70

1

C → Y: Abolishes DNA-binding.

Mutagenesis

91

1

R → Q: Abolishes DNA-binding.

Sequence conflict

53

1

K → N in AAL25296. Ref.4

Secondary structure

1

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549

Helix Strand Turn

Details...

Helix

45 – 48

4

Turn

49 – 51

3

Turn

55 – 58

4

Helix

60 – 62

3

Turn

64 – 67

4

Helix

71 – 80

10

Helix

354 – 366

13

Helix

371 – 373

3

Helix

374 – 383

10

Turn

384 – 386

3

Helix

388 – 397

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform Male (A) [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 3C1B92724E4CE083	FASTA	549	57,409
	10 20 30 40 50 60 MVSEENWNSD TMSDSDMIDS KNDVCGGASS SSGSSISPRT PPNCARCRNH GLKITLKGHK 70 80 90 100 110 120 RYCKFRYCTC EKCRLTADRQ RVMALQTALR RAQAQDEQRA LHMHEVPPAN PAATTLLSHH 130 140 150 160 170 180 HHVAAPAHVH AHHVHAHHAH GGHHSHHGHV LHHQQAAAAA AAAPSAPASH LGGSSTAASS 190 200 210 220 230 240 IHGHAHAHHV HMAAAAAASV AQHQHQSHPH SHHHHHQNHH QHPHQQPATQ TALRSPPHSD 250 260 270 280 290 300 HGGSVGPATS SSGGGAPSSS NAAAATSSNG SSGGGGGGGG GSSGGGAGGG RSSGTSVITS 310 320 330 340 350 360 ADHHMTTVPT PAQSLEGSCD SSSPSPSSTS GAAILPISVS VNRKNGANVP LGQDVFLDYC 370 380 390 400 410 420 QKLLEKFRYP WELMPLMYVI LKDADANIEE ASRRIEEARV EINRTVAQIY YNYYTPMALV 430 440 450 460 470 480 NGAPMYLTYP SIEQGRYGAH FTHLPLTQIC PPTPEPLALS RSPSSPSGPS AVHNQKPSRP 490 500 510 520 530 540 GSSNGTVHSA ASPTMVTTMA TTSSTPTLSR RQRSRSATPT TPPPPPPAHS SSNGAYHHGH HLVSSTAAT
	Isoform Female (B) (C) [UniParc]. Checksum: 75143686AC717315	FASTA	427	44,768
	10 20 30 40 50 60 MVSEENWNSD TMSDSDMIDS KNDVCGGASS SSGSSISPRT PPNCARCRNH GLKITLKGHK 70 80 90 100 110 120 RYCKFRYCTC EKCRLTADRQ RVMALQTALR RAQAQDEQRA LHMHEVPPAN PAATTLLSHH 130 140 150 160 170 180 HHVAAPAHVH AHHVHAHHAH GGHHSHHGHV LHHQQAAAAA AAAPSAPASH LGGSSTAASS 190 200 210 220 230 240 IHGHAHAHHV HMAAAAAASV AQHQHQSHPH SHHHHHQNHH QHPHQQPATQ TALRSPPHSD 250 260 270 280 290 300 HGGSVGPATS SSGGGAPSSS NAAAATSSNG SSGGGGGGGG GSSGGGAGGG RSSGTSVITS 310 320 330 340 350 360 ADHHMTTVPT PAQSLEGSCD SSSPSPSSTS GAAILPISVS VNRKNGANVP LGQDVFLDYC 370 380 390 400 410 420 QKLLEKFRYP WELMPLMYVI LKDADANIEE ASRRIEEGQY VVNEYSRQHN LNIYDGGELR NTTRQCG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Drosophila doublesex gene controls somatic sexual differentiation by producing alternatively spliced mRNAs encoding related sex-specific polypeptides." Burtis K.C., Baker B.S. Cell 56:997-1010(1989) [PubMed: 2493994] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS FEMALE AND MALE). Tissue: Larva and Pupae.
[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, ALTERNATIVE SPLICING. Strain: Berkeley.
[4]	"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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM FEMALE). Strain: Berkeley. Tissue: Head.
[5]	"The doublesex proteins of Drosophila melanogaster bind directly to a sex-specific yolk protein gene enhancer." Burtis K.C., Coschigano K.T., Baker B.S., Wensink P.C. EMBO J. 10:2577-2582(1991) [PubMed: 1907913] [Abstract] Cited for: DNA-BINDING.
[6]	"The Drosophila doublesex proteins share a novel zinc finger related DNA binding domain." Erdman S.E., Burtis K.C. EMBO J. 12:527-535(1993) [PubMed: 8440242] [Abstract] Cited for: DNA-BINDING DOMAIN, MUTAGENESIS.
[7]	"The Drosophila takeout gene is regulated by the somatic sex-determination pathway and affects male courtship behavior." Dauwalder B., Tsujimoto S., Moss J., Mattox W. Genes Dev. 16:2879-2892(2002) [PubMed: 12435630] [Abstract] Cited for: FUNCTION. Strain: Canton-S.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M25292 mRNA. Translation: AAA17840.1.
M25293 mRNA. Translation: AAA17841.1.
M25294 mRNA. Translation: AAA17842.1.
AE014297 Genomic DNA. Translation: AAF54169.1.
AE014297 Genomic DNA. Translation: AAN13385.1.
AY060257 mRNA. Translation: AAL25296.1.
BT029258 mRNA. Translation: ABK30895.1.

PIR

A32372.
B32372.

RefSeq

NP_524272.4. NM_079548.4.
NP_731197.1. NM_169202.1.
NP_731198.1. NM_169203.1.

UniGene

Dm.3308.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LPV	NMR	-	A	35-86	[»]
1ZV1	X-ray	1.60	A/B	350-397	[»]
2JZ0	NMR	-	A/B	350-397	[»]
2JZ1	NMR	-	A/B	350-397	[»]

ProteinModelPortal

P23023.

SMR

P23023. Positions 35-86, 350-408.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17110N.

IntAct

P23023. 3 interactions.

MINT

MINT-276845.

STRING

P23023.

Proteomic databases

PRIDE

P23023.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0081759; FBpp0081256; FBgn0000504.

GeneID

40940.

KEGG

dme:Dmel_CG11094.

NMPDR

fig|7227.3.peg.11616.

UCSC

CG11094-RA. d. melanogaster.

Organism-specific databases

CTD

40940.

FlyBase

FBgn0000504. dsx.

Phylogenomic databases

eggNOG

inNOG11008.

GeneTree

EMGT00050000002224.

InParanoid

P23023.

OMA

MIDSKND.

OrthoDB

EOG4N2Z5N.

PhylomeDB

P23023.

Gene expression databases

ArrayExpress

P23023.

Bgee

P23023.

GermOnline

CG11094. Drosophila melanogaster.

Family and domain databases

InterPro

IPR001275. DM_DNA-bd.
IPR014932. DSX_dimer.
[Graphical view]

Gene3D

G3DSA:4.10.1040.10. DM_DNA_bd. 1 hit.

Pfam

PF00751. DM. 1 hit.
PF08828. DSX_dimer. 1 hit.
[Graphical view]

ProDom

PD015828. DSX_dimer. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00301. DM. 1 hit.
[Graphical view]

SUPFAM

SSF82927. DM_DNA_bd. 1 hit.

PROSITE

PS40000. DM_1. 1 hit.
PS50809. DM_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

821382.

Entry information

Entry name

DSX_DROME

Accession

Primary (citable) accession number: P23023
Secondary accession number(s): P23022 , Q0KIA7, Q95TA5, Q9VHY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	January 25, 2012
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project