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Protein

Protein doublesex

Gene

dsx

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi44 – 9148DMPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • axon midline choice point recognition Source: FlyBase
  • central nervous system development Source: FlyBase
  • courtship behavior Source: FlyBase
  • female analia development Source: FlyBase
  • female sex differentiation Source: FlyBase
  • female somatic sex determination Source: FlyBase
  • genital disc development Source: FlyBase
  • genital disc morphogenesis Source: FlyBase
  • genital disc sexually dimorphic development Source: FlyBase
  • imaginal disc-derived female genitalia development Source: FlyBase
  • imaginal disc-derived male genitalia development Source: FlyBase
  • male analia development Source: FlyBase
  • male courtship behavior Source: FlyBase
  • male courtship behavior, veined wing generated song production Source: FlyBase
  • male sex differentiation Source: FlyBase
  • male somatic sex determination Source: FlyBase
  • mRNA splicing, via spliceosome Source: FlyBase
  • negative regulation of developmental pigmentation Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • positive regulation of transcription, DNA-templated Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • regulation of imaginal disc growth Source: FlyBase
  • regulation of transcription, DNA-templated Source: FlyBase
  • regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • sex comb development Source: FlyBase
  • sex determination Source: FlyBase
  • sex differentiation Source: FlyBase
  • sex-specific pigmentation Source: FlyBase
  • somatic sex determination Source: FlyBase
  • spermatogenesis Source: FlyBase
  • transcription from RNA polymerase II promoter Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Differentiation, Sexual differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein doublesex
Gene namesi
Name:dsx
ORF Names:CG11094
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0000504. dsx.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471C → A or H: Abolishes DNA-binding. 1 Publication
Mutagenesisi50 – 501H → Y: Abolishes DNA-binding. 1 Publication
Mutagenesisi59 – 591H → Y: Abolishes DNA-binding. 1 Publication
Mutagenesisi68 – 681C → D or Y: Abolishes DNA-binding. 1 Publication
Mutagenesisi70 – 701C → Y: Abolishes DNA-binding. 1 Publication
Mutagenesisi91 – 911R → Q: Abolishes DNA-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 549549Protein doublesexPRO_0000207041Add
BLAST

Proteomic databases

PaxDbiP23023.
PRIDEiP23023.

Expressioni

Gene expression databases

BgeeiFBgn0000504.
GenevisibleiP23023. DM.

Interactioni

GO - Molecular functioni

  • protein homodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi66125. 46 interactions.
DIPiDIP-17110N.
IntActiP23023. 3 interactions.
STRINGi7227.FBpp0303107.

Structurei

Secondary structure

1
549
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 484Combined sources
Turni49 – 513Combined sources
Turni55 – 584Combined sources
Helixi60 – 623Combined sources
Turni64 – 674Combined sources
Helixi71 – 8010Combined sources
Helixi354 – 36613Combined sources
Helixi371 – 3733Combined sources
Helixi374 – 38310Combined sources
Turni384 – 3863Combined sources
Helixi388 – 39710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LPVNMR-A35-86[»]
1ZV1X-ray1.60A/B350-397[»]
2JZ0NMR-A/B350-397[»]
2JZ1NMR-A/B350-397[»]
ProteinModelPortaliP23023.
SMRiP23023. Positions 35-86, 350-408.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23023.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi119 – 224106His-richAdd
BLAST
Compositional biasi267 – 29630Gly/Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 DM DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3815. Eukaryota.
ENOG410XSK9. LUCA.
GeneTreeiENSGT00550000074486.
InParanoidiP23023.
OrthoDBiEOG091G179Z.
PhylomeDBiP23023.

Family and domain databases

Gene3Di4.10.1040.10. 1 hit.
InterProiIPR001275. DM_DNA-bd.
IPR026607. DMRT/dsx/mab-3.
IPR014932. DSX_dimer.
[Graphical view]
PANTHERiPTHR12322. PTHR12322. 2 hits.
PfamiPF00751. DM. 1 hit.
PF08828. DSX_dimer. 1 hit.
[Graphical view]
ProDomiPD015828. DSX_dimer. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00301. DM. 1 hit.
SM01143. DSX_dimer. 1 hit.
[Graphical view]
SUPFAMiSSF82927. SSF82927. 1 hit.
PROSITEiPS40000. DM_1. 1 hit.
PS50809. DM_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Male (identifier: P23023-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MVSEENWNSD TMSDSDMIDS KNDVCGGASS SSGSSISPRT PPNCARCRNH
60 70 80 90 100
GLKITLKGHK RYCKFRYCTC EKCRLTADRQ RVMALQTALR RAQAQDEQRA
110 120 130 140 150
LHMHEVPPAN PAATTLLSHH HHVAAPAHVH AHHVHAHHAH GGHHSHHGHV
160 170 180 190 200
LHHQQAAAAA AAAPSAPASH LGGSSTAASS IHGHAHAHHV HMAAAAAASV
210 220 230 240 250
AQHQHQSHPH SHHHHHQNHH QHPHQQPATQ TALRSPPHSD HGGSVGPATS
260 270 280 290 300
SSGGGAPSSS NAAAATSSNG SSGGGGGGGG GSSGGGAGGG RSSGTSVITS
310 320 330 340 350
ADHHMTTVPT PAQSLEGSCD SSSPSPSSTS GAAILPISVS VNRKNGANVP
360 370 380 390 400
LGQDVFLDYC QKLLEKFRYP WELMPLMYVI LKDADANIEE ASRRIEEARV
410 420 430 440 450
EINRTVAQIY YNYYTPMALV NGAPMYLTYP SIEQGRYGAH FTHLPLTQIC
460 470 480 490 500
PPTPEPLALS RSPSSPSGPS AVHNQKPSRP GSSNGTVHSA ASPTMVTTMA
510 520 530 540
TTSSTPTLSR RQRSRSATPT TPPPPPPAHS SSNGAYHHGH HLVSSTAAT
Length:549
Mass (Da):57,409
Last modified:November 1, 1991 - v1
Checksum:i3C1B92724E4CE083
GO
Isoform Female (identifier: P23023-2) [UniParc]FASTAAdd to basket
Also known as: B, C

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

Show »
Length:427
Mass (Da):44,768
Checksum:i75143686AC717315
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531K → N in AAL25296 (PubMed:12537569).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei398 – 42730ARVEI…APMYL → GQYVVNEYSRQHNLNIYDGG ELRNTTRQCG in isoform Female. 2 PublicationsVSP_001321Add
BLAST
Alternative sequencei428 – 549122Missing in isoform Female. 2 PublicationsVSP_001322Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA32372.
B32372.
RefSeqiNP_001262352.1. NM_001275423.1. [P23023-1]
NP_001287220.1. NM_001300291.1. [P23023-2]
NP_524272.4. NM_079548.5. [P23023-2]
NP_731197.1. NM_169202.1. [P23023-1]
NP_731198.1. NM_169203.2. [P23023-2]
UniGeneiDm.3308.

Genome annotation databases

EnsemblMetazoaiFBtr0081759; FBpp0081256; FBgn0000504. [P23023-1]
FBtr0330073; FBpp0303106; FBgn0000504. [P23023-1]
GeneIDi40940.
KEGGidme:Dmel_CG11094.
UCSCiCG11094-RA. d. melanogaster. [P23023-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA32372.
B32372.
RefSeqiNP_001262352.1. NM_001275423.1. [P23023-1]
NP_001287220.1. NM_001300291.1. [P23023-2]
NP_524272.4. NM_079548.5. [P23023-2]
NP_731197.1. NM_169202.1. [P23023-1]
NP_731198.1. NM_169203.2. [P23023-2]
UniGeneiDm.3308.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LPVNMR-A35-86[»]
1ZV1X-ray1.60A/B350-397[»]
2JZ0NMR-A/B350-397[»]
2JZ1NMR-A/B350-397[»]
ProteinModelPortaliP23023.
SMRiP23023. Positions 35-86, 350-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66125. 46 interactions.
DIPiDIP-17110N.
IntActiP23023. 3 interactions.
STRINGi7227.FBpp0303107.

Proteomic databases

PaxDbiP23023.
PRIDEiP23023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081759; FBpp0081256; FBgn0000504. [P23023-1]
FBtr0330073; FBpp0303106; FBgn0000504. [P23023-1]
GeneIDi40940.
KEGGidme:Dmel_CG11094.
UCSCiCG11094-RA. d. melanogaster. [P23023-1]

Organism-specific databases

CTDi40940.
FlyBaseiFBgn0000504. dsx.

Phylogenomic databases

eggNOGiKOG3815. Eukaryota.
ENOG410XSK9. LUCA.
GeneTreeiENSGT00550000074486.
InParanoidiP23023.
OrthoDBiEOG091G179Z.
PhylomeDBiP23023.

Miscellaneous databases

EvolutionaryTraceiP23023.
GenomeRNAii40940.
PROiP23023.

Gene expression databases

BgeeiFBgn0000504.
GenevisibleiP23023. DM.

Family and domain databases

Gene3Di4.10.1040.10. 1 hit.
InterProiIPR001275. DM_DNA-bd.
IPR026607. DMRT/dsx/mab-3.
IPR014932. DSX_dimer.
[Graphical view]
PANTHERiPTHR12322. PTHR12322. 2 hits.
PfamiPF00751. DM. 1 hit.
PF08828. DSX_dimer. 1 hit.
[Graphical view]
ProDomiPD015828. DSX_dimer. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00301. DM. 1 hit.
SM01143. DSX_dimer. 1 hit.
[Graphical view]
SUPFAMiSSF82927. SSF82927. 1 hit.
PROSITEiPS40000. DM_1. 1 hit.
PS50809. DM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDSX_DROME
AccessioniPrimary (citable) accession number: P23023
Secondary accession number(s): P23022
, Q0KIA7, Q95TA5, Q9VHY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: September 7, 2016
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Experimentally shown to bind zinc.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.