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Protein

Protein sex-lethal

Gene

Sxl

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

Functioni

Sex determination switch protein which controls sexual development by sex-specific splicing. Regulates dosage compensation in females by suppressing hyperactivation of X-linked genes. Expression of the embryo-specific isoform is under the control of primary sex-determining signal, which depends on the ratio of X chromosomes relative to autosomes (X:A ratio). Expression occurs in 2X:2A cells, but not in X:2A cells. The X:A ratio seems to be signaled by the relative concentration of the X-linked transcription factors SIS-A and SIS-B. As a result, the embryo-specific product is expressed early only in female embryos and specifies female-adult specific splicing; in the male where it is not expressed, the default splicing gives rise to a truncated non-functional protein. The female-specific isoform specifies the splicing of its own transcript, thereby initiating a positive autoregulatory feedback loop leading to female development pathway. The female-specific isoform controls the sex-specific splicing of transformer (TRA); acts as a translational repressor for male-specific lethal-2 (MSL-2) and prevents male-less (MLE), MSL-1 and MSL-3 proteins from associating with the female X chromosome.3 Publications

GO - Molecular functioni

  • growth factor activity Source: FlyBase
  • mRNA 3'-UTR binding Source: FlyBase
  • mRNA 5'-UTR binding Source: FlyBase
  • mRNA binding Source: FlyBase
  • nucleotide binding Source: InterPro
  • poly(U) RNA binding Source: FlyBase
  • poly-pyrimidine tract binding Source: FlyBase
  • translation repressor activity, nucleic acid binding Source: FlyBase

GO - Biological processi

  • alternative mRNA splicing, via spliceosome Source: FlyBase
  • dosage compensation Source: FlyBase
  • female germ-line sex determination Source: FlyBase
  • female sex determination Source: FlyBase
  • female somatic sex determination Source: FlyBase
  • germ cell development Source: FlyBase
  • imaginal disc growth Source: FlyBase
  • mRNA splicing, via spliceosome Source: FlyBase
  • negative regulation of mRNA splicing, via spliceosome Source: FlyBase
  • negative regulation of translation Source: FlyBase
  • oocyte differentiation Source: FlyBase
  • oogenesis Source: FlyBase
  • reciprocal meiotic recombination Source: FlyBase
  • regulation of alternative mRNA splicing, via spliceosome Source: FlyBase
  • regulation of mRNA splicing, via spliceosome Source: FlyBase
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • sex determination Source: FlyBase
  • sex determination, primary response to X:A ratio Source: FlyBase
  • sex differentiation Source: FlyBase
  • smoothened signaling pathway Source: FlyBase
  • somatic sex determination Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Differentiation, Sexual differentiation, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein sex-lethal
Gene namesi
Name:Sxl
Synonyms:Sx1
ORF Names:CG43770
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0264270. Sxl.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • protein complex Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Protein sex-lethalPRO_0000081967Add
BLAST

Proteomic databases

PaxDbiP19339.
PRIDEiP19339.

Expressioni

Tissue specificityi

Expressed in somatic tissues, but not in the pole cells, which are the precursors of the germline.

Developmental stagei

Isoform 1 is embryo-specific. Isoform CM1 is male-specific. Isoforms MS3, MS11 and MS16 are female specific. Isoform 1 is expressed for a brief period during the syncytial blastoderm stage. Isoform MS11 is expressed in 4-7 hours embryo.2 Publications

Gene expression databases

BgeeiP19339.
ExpressionAtlasiP19339. differential.
GenevisibleiP19339. DM.

Interactioni

Subunit structurei

Part of a complex containing fl2d, Sxl and vir.1 Publication

GO - Molecular functioni

  • growth factor activity Source: FlyBase

Protein-protein interaction databases

BioGridi533777. 64 interactions.
DIPiDIP-44607N.
IntActiP19339. 8 interactions.
MINTiMINT-276991.
STRINGi7227.FBpp0303712.

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi125 – 1306Combined sources
Helixi138 – 1469Combined sources
Beta strandi151 – 1555Combined sources
Turni160 – 1634Combined sources
Beta strandi167 – 1759Combined sources
Helixi176 – 18611Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi197 – 2004Combined sources
Turni207 – 2104Combined sources
Beta strandi212 – 2176Combined sources
Helixi224 – 2318Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi237 – 2448Combined sources
Turni246 – 2483Combined sources
Beta strandi251 – 26111Combined sources
Helixi262 – 27211Combined sources
Beta strandi285 – 2884Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B7FX-ray2.60A/B122-289[»]
1SXLNMR-A199-294[»]
2SXLNMR-A122-209[»]
3SXLX-ray2.70A/B/C111-294[»]
4QQBX-ray2.80A/B122-294[»]
ProteinModelPortaliP19339.
SMRiP19339. Positions 79-291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19339.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 20379RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini211 – 29181RRM 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 3232Asn/Gly-richAdd
BLAST
Compositional biasi57 – 604Poly-Ser
Compositional biasi312 – 3198Poly-Pro

Domaini

The Gly-Asn rich domain is required for the cooperative interaction with RNA and for regulating the splicing activity.

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IQXB. Eukaryota.
ENOG411112S. LUCA.
GeneTreeiENSGT00760000118913.
InParanoidiP19339.
KOiK18747.
OMAiDTEFTFP.
PhylomeDBiP19339.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR006546. Sxl.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
PRINTSiPR00961. HUDSXLRNA.
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
TIGRFAMsiTIGR01659. sex-lethal. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (14)i

Sequence statusi: Complete.

This entry describes 14 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform MS3 (identifier: P19339-1) [UniParc]FASTAAdd to basket

Also known as: CF1, D, female-specific, L, T

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
MYGNNNPGSN NNNGGYPPYG YNNKSSGGRG FGMSHSLPSG MSRYAFSPQD
60 70 80 90 100
TEFSFPSSSS RRGYNDFPGC GGSGGNGGSA NNLGGGNMCH LPPMASNNSL
110 120 130 140 150
NNLCGLSLGS GGSDDLMNDP RASNTNLIVN YLPQDMTDRE LYALFRAIGP
160 170 180 190 200
INTCRIMRDY KTGYSFGYAF VDFTSEMDSQ RAIKVLNGIT VRNKRLKVSY
210 220 230 240 250
ARPGGESIKD TNLYVTNLPR TITDDQLDTI FGKYGSIVQK NILRDKLTGR
260 270 280 290 300
PRGVAFVRYN KREEAQEAIS ALNNVIPEGG SQPLSVRLAE EHGKAKAAHF
310 320 330 340 350
MSQMGVVPAN VPPPPPQPPA HMAAAFNMMH RGRSIKSQQR FQNSHPYFDA

KKFI
Length:354
Mass (Da):38,549
Last modified:November 1, 1990 - v1
Checksum:i4E443D3BC88B134E
GO
Isoform 1 (identifier: P19339-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MYGNNNPGSNNNNGGYPPYGYNNKS → MDFNFDTVTPCSTMSSYYNFKMA

Show »
Length:352
Mass (Da):38,542
Checksum:iFD5C0EE4F86C8A29
GO
Isoform A (identifier: P19339-10) [UniParc]FASTAAdd to basket

Also known as: E, U

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.
     42-49: Missing.

Note: No experimental confirmation available.
Show »
Length:314
Mass (Da):34,304
Checksum:i8CB2DCA31C482659
GO
Isoform C (identifier: P19339-8) [UniParc]FASTAAdd to basket

Also known as: N

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MYGNNNPGSNNNNGGYPPYGYNNKS → MDFNFDTVTPCSTMSSYYNFKMA
     42-49: Missing.

Note: No experimental confirmation available.
Show »
Length:344
Mass (Da):37,605
Checksum:i98D4D7D547D4D55D
GO
Isoform CM1 (identifier: P19339-3) [UniParc]FASTAAdd to basket

Also known as: B, F, M

The sequence of this isoform differs from the canonical sequence as follows:
     26-48: SGGRGFGMSHSLPSGMSRYAFSP → RHIFFHSPERSSHHYHRKAKDTH
     49-354: Missing.

Show »
Length:48
Mass (Da):5,601
Checksum:i0900E728FB154B24
GO
Isoform G (identifier: P19339-7) [UniParc]FASTAAdd to basket

Also known as: J

The sequence of this isoform differs from the canonical sequence as follows:
     42-49: Missing.

Note: No experimental confirmation available.
Show »
Length:346
Mass (Da):37,612
Checksum:iDD93EDFA9C166C35
GO
Isoform W (identifier: P19339-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     42-49: Missing.
     333-354: RSIKSQQRFQNSHPYFDAKKFI → ENFADLLDGLYRRKYHYPYL

Note: No experimental confirmation available.
Show »
Length:344
Mass (Da):37,433
Checksum:i1093D98D4591E81E
GO
Isoform K (identifier: P19339-11) [UniParc]FASTAAdd to basket

Also known as: Q

The sequence of this isoform differs from the canonical sequence as follows:
     27-42: GGRGFGMSHSLPSGMS → PERSSHHYHRKAKDTH
     43-354: Missing.

Note: No experimental confirmation available.
Show »
Length:42
Mass (Da):4,763
Checksum:i7AFD03F36F4BEA11
GO
Isoform MS11 (identifier: P19339-4) [UniParc]FASTAAdd to basket

Also known as: H

The sequence of this isoform differs from the canonical sequence as follows:
     42-49: Missing.
     332-354: GRSIKSQQRFQNSHPYFDAKKFI → DGAMEKLRSLFDAICDAIFGLDSENFADLLDGLYRRKYHYPYL

Show »
Length:366
Mass (Da):39,846
Checksum:iE7202AB9FFD0772B
GO
Isoform MS16 (identifier: P19339-5) [UniParc]FASTAAdd to basket

Also known as: P

The sequence of this isoform differs from the canonical sequence as follows:
     333-354: RSIKSQQRFQNSHPYFDAKKFI → ENFADLLDGLYRRKYHYPYL

Show »
Length:352
Mass (Da):38,370
Checksum:i30528D103AEA1523
GO
Isoform O (identifier: P19339-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MYGNNNPGSNNNNGGYPPYGYNNKS → MDFNFDTVTPCSTMSSYYNFKMA
     42-49: Missing.
     332-354: GRSIKSQQRFQNSHPYFDAKKFI → DGAMEKLRSLFDAICDAIFGLDSENFADLLDGLYRRKYHYPYL

Note: No experimental confirmation available.
Show »
Length:364
Mass (Da):39,839
Checksum:i180D2C7B3316D85D
GO
Isoform R (identifier: P19339-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MYGNNNPGSNNNNGGYPPYGYNNKS → MDFNFDTVTPCSTMSSYYNFKMA
     42-49: Missing.
     333-354: RSIKSQQRFQNSHPYFDAKKFI → ENFADLLDGLYRRKYHYPYL

Note: No experimental confirmation available.
Show »
Length:342
Mass (Da):37,426
Checksum:iAABC024FFCF99F76
GO
Isoform S (identifier: P19339-13) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.

Note: No experimental confirmation available.
Show »
Length:322
Mass (Da):35,241
Checksum:i54C3A1F020F451FF
GO
Isoform V (identifier: P19339-14) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MYGNNNPGSNNNNGGYPPYGYNNKS → MDFNFDTVTPCSTMSSYYNFKMARNGIDSSY

Note: No experimental confirmation available.
Show »
Length:360
Mass (Da):39,435
Checksum:iA56D6D64FB33528B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931P → S in AAA28921 (PubMed:1710769).Curated
Sequence conflicti96 – 961S → G in AAA28921 (PubMed:1710769).Curated
Sequence conflicti96 – 961S → G in ACY56908 (Ref. 5) Curated
Sequence conflicti96 – 961S → G in ADD20766 (Ref. 5) Curated
Sequence conflicti273 – 2731N → K in ACY56908 (Ref. 5) Curated
Isoform 1 (identifier: P19339-2)
Sequence conflicti15 – 151S → C in AAB21845 (PubMed:1547493).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3232Missing in isoform A and isoform S. 1 PublicationVSP_019287Add
BLAST
Alternative sequencei1 – 2525MYGNN…YNNKS → MDFNFDTVTPCSTMSSYYNF KMA in isoform 1, isoform C, isoform O and isoform R. CuratedVSP_005881Add
BLAST
Alternative sequencei1 – 2525MYGNN…YNNKS → MDFNFDTVTPCSTMSSYYNF KMARNGIDSSY in isoform V. 1 PublicationVSP_040526Add
BLAST
Alternative sequencei26 – 4823SGGRG…YAFSP → RHIFFHSPERSSHHYHRKAK DTH in isoform CM1. 1 PublicationVSP_005882Add
BLAST
Alternative sequencei27 – 4216GGRGF…PSGMS → PERSSHHYHRKAKDTH in isoform K. CuratedVSP_019289Add
BLAST
Alternative sequencei42 – 498Missing in isoform A, isoform C, isoform G, isoform W, isoform MS11, isoform O and isoform R. 2 PublicationsVSP_005883
Alternative sequencei43 – 354312Missing in isoform K. CuratedVSP_019290Add
BLAST
Alternative sequencei49 – 354306Missing in isoform CM1. 1 PublicationVSP_005884Add
BLAST
Alternative sequencei332 – 35423GRSIK…AKKFI → DGAMEKLRSLFDAICDAIFG LDSENFADLLDGLYRRKYHY PYL in isoform MS11 and isoform O. 1 PublicationVSP_005885Add
BLAST
Alternative sequencei333 – 35422RSIKS…AKKFI → ENFADLLDGLYRRKYHYPYL in isoform W, isoform MS16 and isoform R. 2 PublicationsVSP_005886Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23635 mRNA. Translation: AAA28885.1.
M23636 mRNA. Translation: AAA28884.1.
M59447 mRNA. Translation: AAA28922.1.
M59448 mRNA. Translation: AAA28921.1.
AE014298 Genomic DNA. Translation: AAF46240.2.
AE014298 Genomic DNA. Translation: AAF46241.4.
AE014298 Genomic DNA. Translation: AAG22410.1.
AE014298 Genomic DNA. Translation: AAG22411.1.
AE014298 Genomic DNA. Translation: AAN09197.1.
AE014298 Genomic DNA. Translation: AAN09198.1.
AE014298 Genomic DNA. Translation: AAN09200.2.
AE014298 Genomic DNA. Translation: AAN09201.2.
AE014298 Genomic DNA. Translation: AAO41638.2.
AE014298 Genomic DNA. Translation: AAZ52509.1.
AE014298 Genomic DNA. Translation: AAZ52510.1.
AE014298 Genomic DNA. Translation: AAZ52511.1.
AE014298 Genomic DNA. Translation: AAZ52512.1.
AE014298 Genomic DNA. Translation: AAZ52513.1.
AE014298 Genomic DNA. Translation: AAZ52514.1.
AE014298 Genomic DNA. Translation: ACZ95222.1.
AE014298 Genomic DNA. Translation: ACZ95223.1.
AE014298 Genomic DNA. Translation: ACZ95224.1.
AE014298 Genomic DNA. Translation: ACZ95225.1.
AE014298 Genomic DNA. Translation: ACZ95226.1.
BT003583 mRNA. Translation: AAO39587.1.
BT099922 mRNA. Translation: ACX32993.1.
BT100240 mRNA. Translation: ACY56908.1.
BT120392 mRNA. Translation: ADD20766.1.
S88324 Genomic DNA. Translation: AAB21845.1.
D84425 Genomic DNA. Translation: BAA20294.1.
PIRiA31639.
A39725. B31639.
RefSeqiNP_001027062.1. NM_001031891.3. [P19339-6]
NP_001027063.1. NM_001031892.2. [P19339-8]
NP_001027064.1. NM_001031893.2. [P19339-3]
NP_001027065.1. NM_001031894.1. [P19339-1]
NP_001027066.1. NM_001031895.1. [P19339-11]
NP_001162686.1. NM_001169215.2. [P19339-5]
NP_001162687.1. NM_001169216.2. [P19339-11]
NP_001162688.1. NM_001169217.2. [P19339-12]
NP_001162689.1. NM_001169218.3. [P19339-13]
NP_001162690.1. NM_001169219.1. [P19339-1]
NP_001259305.1. NM_001272376.1. [P19339-11]
NP_001259306.1. NM_001272377.1. [P19339-3]
NP_524791.3. NM_080052.4. [P19339-8]
NP_727160.2. NM_167110.3. [P19339-7]
NP_727161.3. NM_167111.3. [P19339-9]
NP_727162.2. NM_167112.2. [P19339-1]
NP_727163.2. NM_167113.3. [P19339-10]
NP_727164.2. NM_167114.2. [P19339-4]
NP_727165.2. NM_167115.3. [P19339-10]
NP_727166.2. NM_167116.2. [P19339-7]
NP_727167.2. NM_167117.2. [P19339-3]
NP_727168.1. NM_167118.2. [P19339-3]
UniGeneiDm.4502.

Genome annotation databases

EnsemblMetazoaiFBtr0331255; FBpp0303697; FBgn0264270. [P19339-1]
FBtr0331262; FBpp0303704; FBgn0264270. [P19339-1]
FBtr0331268; FBpp0303710; FBgn0264270. [P19339-1]
GeneIDi3772180.
KEGGidme:Dmel_CG43770.
UCSCiCG18350-RE. d. melanogaster.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23635 mRNA. Translation: AAA28885.1.
M23636 mRNA. Translation: AAA28884.1.
M59447 mRNA. Translation: AAA28922.1.
M59448 mRNA. Translation: AAA28921.1.
AE014298 Genomic DNA. Translation: AAF46240.2.
AE014298 Genomic DNA. Translation: AAF46241.4.
AE014298 Genomic DNA. Translation: AAG22410.1.
AE014298 Genomic DNA. Translation: AAG22411.1.
AE014298 Genomic DNA. Translation: AAN09197.1.
AE014298 Genomic DNA. Translation: AAN09198.1.
AE014298 Genomic DNA. Translation: AAN09200.2.
AE014298 Genomic DNA. Translation: AAN09201.2.
AE014298 Genomic DNA. Translation: AAO41638.2.
AE014298 Genomic DNA. Translation: AAZ52509.1.
AE014298 Genomic DNA. Translation: AAZ52510.1.
AE014298 Genomic DNA. Translation: AAZ52511.1.
AE014298 Genomic DNA. Translation: AAZ52512.1.
AE014298 Genomic DNA. Translation: AAZ52513.1.
AE014298 Genomic DNA. Translation: AAZ52514.1.
AE014298 Genomic DNA. Translation: ACZ95222.1.
AE014298 Genomic DNA. Translation: ACZ95223.1.
AE014298 Genomic DNA. Translation: ACZ95224.1.
AE014298 Genomic DNA. Translation: ACZ95225.1.
AE014298 Genomic DNA. Translation: ACZ95226.1.
BT003583 mRNA. Translation: AAO39587.1.
BT099922 mRNA. Translation: ACX32993.1.
BT100240 mRNA. Translation: ACY56908.1.
BT120392 mRNA. Translation: ADD20766.1.
S88324 Genomic DNA. Translation: AAB21845.1.
D84425 Genomic DNA. Translation: BAA20294.1.
PIRiA31639.
A39725. B31639.
RefSeqiNP_001027062.1. NM_001031891.3. [P19339-6]
NP_001027063.1. NM_001031892.2. [P19339-8]
NP_001027064.1. NM_001031893.2. [P19339-3]
NP_001027065.1. NM_001031894.1. [P19339-1]
NP_001027066.1. NM_001031895.1. [P19339-11]
NP_001162686.1. NM_001169215.2. [P19339-5]
NP_001162687.1. NM_001169216.2. [P19339-11]
NP_001162688.1. NM_001169217.2. [P19339-12]
NP_001162689.1. NM_001169218.3. [P19339-13]
NP_001162690.1. NM_001169219.1. [P19339-1]
NP_001259305.1. NM_001272376.1. [P19339-11]
NP_001259306.1. NM_001272377.1. [P19339-3]
NP_524791.3. NM_080052.4. [P19339-8]
NP_727160.2. NM_167110.3. [P19339-7]
NP_727161.3. NM_167111.3. [P19339-9]
NP_727162.2. NM_167112.2. [P19339-1]
NP_727163.2. NM_167113.3. [P19339-10]
NP_727164.2. NM_167114.2. [P19339-4]
NP_727165.2. NM_167115.3. [P19339-10]
NP_727166.2. NM_167116.2. [P19339-7]
NP_727167.2. NM_167117.2. [P19339-3]
NP_727168.1. NM_167118.2. [P19339-3]
UniGeneiDm.4502.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B7FX-ray2.60A/B122-289[»]
1SXLNMR-A199-294[»]
2SXLNMR-A122-209[»]
3SXLX-ray2.70A/B/C111-294[»]
4QQBX-ray2.80A/B122-294[»]
ProteinModelPortaliP19339.
SMRiP19339. Positions 79-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi533777. 64 interactions.
DIPiDIP-44607N.
IntActiP19339. 8 interactions.
MINTiMINT-276991.
STRINGi7227.FBpp0303712.

Proteomic databases

PaxDbiP19339.
PRIDEiP19339.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0331255; FBpp0303697; FBgn0264270. [P19339-1]
FBtr0331262; FBpp0303704; FBgn0264270. [P19339-1]
FBtr0331268; FBpp0303710; FBgn0264270. [P19339-1]
GeneIDi3772180.
KEGGidme:Dmel_CG43770.
UCSCiCG18350-RE. d. melanogaster.

Organism-specific databases

CTDi3772180.
FlyBaseiFBgn0264270. Sxl.

Phylogenomic databases

eggNOGiENOG410IQXB. Eukaryota.
ENOG411112S. LUCA.
GeneTreeiENSGT00760000118913.
InParanoidiP19339.
KOiK18747.
OMAiDTEFTFP.
PhylomeDBiP19339.

Miscellaneous databases

ChiTaRSiSxl. fly.
EvolutionaryTraceiP19339.
GenomeRNAii3772180.
NextBioi852740.
PROiP19339.

Gene expression databases

BgeeiP19339.
ExpressionAtlasiP19339. differential.
GenevisibleiP19339. DM.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR006546. Sxl.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
PRINTSiPR00961. HUDSXLRNA.
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
TIGRFAMsiTIGR01659. sex-lethal. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sex-lethal, a Drosophila sex determination switch gene, exhibits sex-specific RNA splicing and sequence similarity to RNA binding proteins."
    Bell L.R., Maine E.M., Schedl P., Cline T.W.
    Cell 55:1037-1046(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MS3 AND CM1), FUNCTION, DEVELOPMENTAL STAGE.
    Strain: Oregon-R.
  2. "The complex set of late transcripts from the Drosophila sex determination gene sex-lethal encodes multiple related polypeptides."
    Samuels M.E., Schedl P., Cline T.W.
    Mol. Cell. Biol. 11:3584-3602(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MS3; MS11 AND MS16), FUNCTION, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  3. "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.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; W; MS16 AND V).
    Strain: Berkeley.
    Tissue: Embryo and Head.
  6. "The primary sex determination signal of Drosophila acts at the level of transcription."
    Keyes L.N., Cline T.W., Schedl P.
    Cell 68:933-943(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26 (ISOFORM 1), FUNCTION.
    Tissue: Embryo.
  7. "Regulation of the gene Sex-lethal: a comparative analysis of Drosophila melanogaster and Drosophila subobscura."
    Penalva L.O.F., Sakamoto H., Navarro-Sabate A., Sakashita E., Granadino B., Segarra C., Sanchez L.
    Genetics 144:1653-1664(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41 (ISOFORM MS3).
  8. "Control of Drosophila Sex-lethal pre-mRNA splicing by its own female-specific product."
    Sakamoto H., Inoue K., Higuchi I., Ono Y., Shimura Y.
    Nucleic Acids Res. 20:5533-5540(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  9. "Biochemical function of female-lethal (2)D/Wilms' tumor suppressor-1-associated proteins in alternative pre-mRNA splicing."
    Ortega A., Niksic M., Bachi A., Wilm M., Sanchez L., Hastie N., Valcarcel J.
    J. Biol. Chem. 278:3040-3047(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH FL(2)D AND VIR.
  10. "Resonance assignments and solution structure of the second RNA-binding domain of sex-lethal determined by multidimensional heteronuclear magnetic resonance."
    Lee A.L., Kanaar R., Rio D.C., Wemmer D.E.
    Biochemistry 33:13775-13786(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 199-294.
  11. "A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-terminal RNA-binding domain of Drosophila sex-lethal."
    Inoue M., Muto Y., Sakamoto H., Kigawa T., Takio K., Shimura Y., Yokoyama S.
    J. Mol. Biol. 272:82-94(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 122-209.
  12. "Structural basis for recognition of the tra mRNA precursor by the Sex-lethal protein."
    Handa N., Nureki O., Kurimoto K., Kim I., Sakamoto H., Shimura Y., Muto Y., Yokoyama S.
    Nature 398:579-585(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 122-289, RNA-BINDING.

Entry informationi

Entry nameiSXL_DROME
AccessioniPrimary (citable) accession number: P19339
Secondary accession number(s): A4V434
, A4V435, A4V436, A4V437, C9QP40, D0IQK2, D3PFI6, E1JJI8, E1JJI9, E1JJJ0, E1JJJ2, E1JJJ3, P19340, Q0KHV2, Q26466, Q2MGN7, Q2MGN8, Q2MGN9, Q2MGP1, Q7KVU6, Q7YZ92, Q8IRQ1, Q99141, Q9TYF5, Q9W3S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 11, 2016
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

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.