Reviewed, UniProtKB/Swiss-Prot P19339 (SXL_DROME)

Names and origin

Protein names

Recommended name:
    Protein sex-lethal

Gene names

Name:	Sxl
Synonyms:	Sx1
ORF Names:	CG18350

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

General annotation (Comments)

Function	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. Ref.1 Ref.2 Ref.6
Subunit structure	Part of a complex containing fl2d, Sxl and vir.
Tissue specificity	Expressed in somatic tissues, but not in the pole cells, which are the precursors of the germline.
Developmental stage	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. Ref.1 Ref.2
Domain	The Gly-Asn rich domain is required for the cooperative interaction with RNA and for regulating the splicing activity.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	Differentiation Sexual differentiation Transcription Transcription regulation
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	alternative nuclear mRNA splicing, via spliceosome Ref.9 Traceable author statement. Source: FlyBase dosage compensation Traceable author statement. Source: FlyBase female germ-line sex determination Traceable author statement. Source: FlyBase female somatic sex determination Traceable author statement. Source: FlyBase germ cell development Traceable author statement. Source: FlyBase imaginal disc growth Inferred from mutant phenotype. Source: FlyBase negative regulation of nuclear mRNA splicing, via spliceosome Traceable author statement. Source: FlyBase negative regulation of translation Inferred from direct assay. Source: FlyBase oocyte differentiation Inferred from direct assay. Source: FlyBase reciprocal meiotic recombination Traceable author statement. Source: FlyBase regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW sex determination, primary response to X:A ratio Traceable author statement. Source: FlyBase sex differentiation Traceable author statement. Source: FlyBase smoothened signaling pathway Inferred from direct assay. Source: FlyBase transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	protein complex Inferred from physical interaction. Source: FlyBase
Molecular function	growth factor activity Inferred from direct assay. Source: FlyBase identical protein binding Inferred from physical interaction. Source: IntAct mRNA 3'-UTR binding Inferred from direct assay. Source: FlyBase mRNA 5'-UTR binding Inferred from direct assay. Source: FlyBase nucleotide binding Inferred from electronic annotation. Source: InterPro poly-pyrimidine tract binding Inferred from direct assay. Source: FlyBase translation repressor activity, nucleic acid binding Traceable author statement. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-199603,EBI-199603
	Q9VWI4	1	EBI-199603,EBI-88331
	Q9W579	1	EBI-199603,EBI-164781
CG9624-RA	Q9VFL8	1	EBI-199603,EBI-112485
Dredd	O77260	1	EBI-199603,EBI-196048
Nup58	Q9VDV3	1	EBI-199603,EBI-123251
serp	Q9VW34	1	EBI-199603,EBI-178576

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist.
Isoform MS3 (identifier: P19339-1) Also known as: CF1; D; female-specific; L; 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 1 (identifier: P19339-2) The sequence of this isoform differs from the canonical sequence as follows:      1-25: MYGNNNPGSNNNNGGYPPYGYNNKS → MDFNFDTVTPCSTMSSYYNFKMA
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Sequence conflict	15	1	S → C in AAA28885. Ref.1
Isoform A (identifier: P19339-10) Also known as: E; The sequence of this isoform differs from the canonical sequence as follows:      1-32: Missing.      42-49: Missing.
Note: No experimental confirmation available.
Isoform C (identifier: P19339-8) 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.
Isoform CM1 (identifier: P19339-3) Also known as: B; F; The sequence of this isoform differs from the canonical sequence as follows:      26-48: SGGRGFGMSHSLPSGMSRYAFSP → RHIFFHSPERSSHHYHRKAKDTH      49-354: Missing.
Isoform G (identifier: P19339-7) Also known as: J; The sequence of this isoform differs from the canonical sequence as follows:      42-49: Missing.
Note: No experimental confirmation available.
Isoform I (identifier: P19339-9) The sequence of this isoform differs from the canonical sequence as follows:      3-25: GNNNPGSNNNNGGYPPYGYNNKS → RNGIDSSY
Note: No experimental confirmation available.
Isoform K (identifier: P19339-11) The sequence of this isoform differs from the canonical sequence as follows:      27-42: GGRGFGMSHSLPSGMS → PERSSHHYHRKAKDTH      43-354: Missing.
Note: No experimental confirmation available.
Isoform MS11 (identifier: P19339-4) Also known as: H; The sequence of this isoform differs from the canonical sequence as follows:      42-49: Missing.      332-354: GRSIKSQQRFQNSHPYFDAKKFI → DGAMEKLRSLFDAICDAIFGLDSENFADLLDGLYRRKYHYPYL
Isoform MS16 (identifier: P19339-5) The sequence of this isoform differs from the canonical sequence as follows:      332-354: GRSIKSQQRFQNSHPYFDAKKFI → GENFADLLDGLYRRKYHYPYL
Isoform O (identifier: P19339-6) 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 354

354

Protein sex-lethal

PRO_0000081967

Regions

Domain

125 – 203

79

RRM 1

Domain

211 – 291

81

RRM 2

Compositional bias

1 – 32

32

Asn/Gly-rich

Compositional bias

57 – 60

4

Poly-Ser

Compositional bias

312 – 319

8

Poly-Pro

Natural variations

Alternative sequence

1 – 32

32

Missing in isoform A.

VSP_019287

Alternative sequence

1 – 25

25

MYGNN…YNNKS → MDFNFDTVTPCSTMSSYYNF KMA in isoform 1, isoform C and isoform O.

VSP_005881

Alternative sequence

3 – 25

23

GNNNP…YNNKS → RNGIDSSY in isoform I.

VSP_019288

Alternative sequence

26 – 48

23

SGGRG…YAFSP → RHIFFHSPERSSHHYHRKAK DTH in isoform CM1.

VSP_005882

Alternative sequence

27 – 42

16

GGRGF…PSGMS → PERSSHHYHRKAKDTH in isoform K.

VSP_019289

Alternative sequence

42 – 49

8

Missing in isoform A, isoform C, isoform G, isoform MS11 and isoform O.

VSP_005883

Alternative sequence

43 – 354

312

Missing in isoform K.

VSP_019290

Alternative sequence

49 – 354

306

Missing in isoform CM1.

VSP_005884

Alternative sequence

332 – 354

23

GRSIK…AKKFI → DGAMEKLRSLFDAICDAIFG LDSENFADLLDGLYRRKYHY PYL in isoform MS11 and isoform O.

VSP_005885

Alternative sequence

332 – 354

23

GRSIK…AKKFI → GENFADLLDGLYRRKYHYPY L in isoform MS16.

VSP_005886

Natural variant

93

1

P → S

Natural variant

96

1

S → G

Secondary structure

1

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354

Helix Strand Turn

Details...

Beta strand

125 – 130

6

Helix

138 – 146

9

Beta strand

151 – 155

5

Turn

160 – 163

4

Beta strand

167 – 175

9

Helix

176 – 186

11

Beta strand

197 – 200

4

Turn

207 – 210

4

Beta strand

212 – 217

6

Helix

224 – 231

8

Beta strand

233 – 235

3

Beta strand

237 – 244

8

Turn

246 – 248

3

Beta strand

251 – 261

11

Helix

262 – 272

11

Beta strand

285 – 288

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform MS3 (CF1) (D) (female-specific) (L) [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 4E443D3BC88B134E	FASTA	354	38,549
	10 20 30 40 50 60 MYGNNNPGSN NNNGGYPPYG YNNKSSGGRG FGMSHSLPSG MSRYAFSPQD TEFSFPSSSS 70 80 90 100 110 120 RRGYNDFPGC GGSGGNGGSA NNLGGGNMCH LPPMASNNSL NNLCGLSLGS GGSDDLMNDP 130 140 150 160 170 180 RASNTNLIVN YLPQDMTDRE LYALFRAIGP INTCRIMRDY KTGYSFGYAF VDFTSEMDSQ 190 200 210 220 230 240 RAIKVLNGIT VRNKRLKVSY ARPGGESIKD TNLYVTNLPR TITDDQLDTI FGKYGSIVQK 250 260 270 280 290 300 NILRDKLTGR PRGVAFVRYN KREEAQEAIS ALNNVIPEGG SQPLSVRLAE EHGKAKAAHF 310 320 330 340 350 MSQMGVVPAN VPPPPPQPPA HMAAAFNMMH RGRSIKSQQR FQNSHPYFDA KKFI
	Isoform 1. Checksum: FD5C0EE4F86C8A29	FASTA	352	38,542
	10 20 30 40 50 60 MDFNFDTVTP CSTMSSYYNF KMASGGRGFG MSHSLPSGMS RYAFSPQDTE FSFPSSSSRR 70 80 90 100 110 120 GYNDFPGCGG SGGNGGSANN LGGGNMCHLP PMASNNSLNN LCGLSLGSGG SDDLMNDPRA 130 140 150 160 170 180 SNTNLIVNYL PQDMTDRELY ALFRAIGPIN TCRIMRDYKT GYSFGYAFVD FTSEMDSQRA 190 200 210 220 230 240 IKVLNGITVR NKRLKVSYAR PGGESIKDTN LYVTNLPRTI TDDQLDTIFG KYGSIVQKNI 250 260 270 280 290 300 LRDKLTGRPR GVAFVRYNKR EEAQEAISAL NNVIPEGGSQ PLSVRLAEEH GKAKAAHFMS 310 320 330 340 350 QMGVVPANVP PPPPQPPAHM AAAFNMMHRG RSIKSQQRFQ NSHPYFDAKK FI
	Isoform A (E). Checksum: 8CB2DCA31C482659	FASTA	314	34,304
	10 20 30 40 50 60 MSHSLPSGMD TEFSFPSSSS RRGYNDFPGC GGSGGNGGSA NNLGGGNMCH LPPMASNNSL 70 80 90 100 110 120 NNLCGLSLGS GGSDDLMNDP RASNTNLIVN YLPQDMTDRE LYALFRAIGP INTCRIMRDY 130 140 150 160 170 180 KTGYSFGYAF VDFTSEMDSQ RAIKVLNGIT VRNKRLKVSY ARPGGESIKD TNLYVTNLPR 190 200 210 220 230 240 TITDDQLDTI FGKYGSIVQK NILRDKLTGR PRGVAFVRYN KREEAQEAIS ALNNVIPEGG 250 260 270 280 290 300 SQPLSVRLAE EHGKAKAAHF MSQMGVVPAN VPPPPPQPPA HMAAAFNMMH RGRSIKSQQR 310 FQNSHPYFDA KKFI
	Isoform C (N). Checksum: 98D4D7D547D4D55D	FASTA	344	37,605
	10 20 30 40 50 60 MDFNFDTVTP CSTMSSYYNF KMASGGRGFG MSHSLPSGMD TEFSFPSSSS RRGYNDFPGC 70 80 90 100 110 120 GGSGGNGGSA NNLGGGNMCH LPPMASNNSL NNLCGLSLGS GGSDDLMNDP RASNTNLIVN 130 140 150 160 170 180 YLPQDMTDRE LYALFRAIGP INTCRIMRDY KTGYSFGYAF VDFTSEMDSQ RAIKVLNGIT 190 200 210 220 230 240 VRNKRLKVSY ARPGGESIKD TNLYVTNLPR TITDDQLDTI FGKYGSIVQK NILRDKLTGR 250 260 270 280 290 300 PRGVAFVRYN KREEAQEAIS ALNNVIPEGG SQPLSVRLAE EHGKAKAAHF MSQMGVVPAN 310 320 330 340 VPPPPPQPPA HMAAAFNMMH RGRSIKSQQR FQNSHPYFDA KKFI
	Isoform CM1 (B) (F). Checksum: 0900E728FB154B24	FASTA	48	5,601
	10 20 30 40 MYGNNNPGSN NNNGGYPPYG YNNKSRHIFF HSPERSSHHY HRKAKDTH
	Isoform G (J). Checksum: DD93EDFA9C166C35	FASTA	346	37,612
	10 20 30 40 50 60 MYGNNNPGSN NNNGGYPPYG YNNKSSGGRG FGMSHSLPSG MDTEFSFPSS SSRRGYNDFP 70 80 90 100 110 120 GCGGSGGNGG SANNLGGGNM CHLPPMASNN SLNNLCGLSL GSGGSDDLMN DPRASNTNLI 130 140 150 160 170 180 VNYLPQDMTD RELYALFRAI GPINTCRIMR DYKTGYSFGY AFVDFTSEMD SQRAIKVLNG 190 200 210 220 230 240 ITVRNKRLKV SYARPGGESI KDTNLYVTNL PRTITDDQLD TIFGKYGSIV QKNILRDKLT 250 260 270 280 290 300 GRPRGVAFVR YNKREEAQEA ISALNNVIPE GGSQPLSVRL AEEHGKAKAA HFMSQMGVVP 310 320 330 340 ANVPPPPPQP PAHMAAAFNM MHRGRSIKSQ QRFQNSHPYF DAKKFI
	Isoform I. Checksum: D1129FB38DE66614	FASTA	339	37,047
	10 20 30 40 50 60 MYRNGIDSSY SGGRGFGMSH SLPSGMSRYA FSPQDTEFSF PSSSSRRGYN DFPGCGGSGG 70 80 90 100 110 120 NGGSANNLGG GNMCHLPPMA SNNSLNNLCG LSLGSGGSDD LMNDPRASNT NLIVNYLPQD 130 140 150 160 170 180 MTDRELYALF RAIGPINTCR IMRDYKTGYS FGYAFVDFTS EMDSQRAIKV LNGITVRNKR 190 200 210 220 230 240 LKVSYARPGG ESIKDTNLYV TNLPRTITDD QLDTIFGKYG SIVQKNILRD KLTGRPRGVA 250 260 270 280 290 300 FVRYNKREEA QEAISALNNV IPEGGSQPLS VRLAEEHGKA KAAHFMSQMG VVPANVPPPP 310 320 330 PQPPAHMAAA FNMMHRGRSI KSQQRFQNSH PYFDAKKFI
	Isoform K. Checksum: 7AFD03F36F4BEA11	FASTA	42	4,763
	10 20 30 40 MYGNNNPGSN NNNGGYPPYG YNNKSSPERS SHHYHRKAKD TH
	Isoform MS11 (H). Checksum: E7202AB9FFD0772B	FASTA	366	39,846
	10 20 30 40 50 60 MYGNNNPGSN NNNGGYPPYG YNNKSSGGRG FGMSHSLPSG MDTEFSFPSS SSRRGYNDFP 70 80 90 100 110 120 GCGGSGGNGG SANNLGGGNM CHLPPMASNN SLNNLCGLSL GSGGSDDLMN DPRASNTNLI 130 140 150 160 170 180 VNYLPQDMTD RELYALFRAI GPINTCRIMR DYKTGYSFGY AFVDFTSEMD SQRAIKVLNG 190 200 210 220 230 240 ITVRNKRLKV SYARPGGESI KDTNLYVTNL PRTITDDQLD TIFGKYGSIV QKNILRDKLT 250 260 270 280 290 300 GRPRGVAFVR YNKREEAQEA ISALNNVIPE GGSQPLSVRL AEEHGKAKAA HFMSQMGVVP 310 320 330 340 350 360 ANVPPPPPQP PAHMAAAFNM MHRDGAMEKL RSLFDAICDA IFGLDSENFA DLLDGLYRRK YHYPYL
	Isoform MS16. Checksum: 30528D103AEA1523	FASTA	352	38,370
	10 20 30 40 50 60 MYGNNNPGSN NNNGGYPPYG YNNKSSGGRG FGMSHSLPSG MSRYAFSPQD TEFSFPSSSS 70 80 90 100 110 120 RRGYNDFPGC GGSGGNGGSA NNLGGGNMCH LPPMASNNSL NNLCGLSLGS GGSDDLMNDP 130 140 150 160 170 180 RASNTNLIVN YLPQDMTDRE LYALFRAIGP INTCRIMRDY KTGYSFGYAF VDFTSEMDSQ 190 200 210 220 230 240 RAIKVLNGIT VRNKRLKVSY ARPGGESIKD TNLYVTNLPR TITDDQLDTI FGKYGSIVQK 250 260 270 280 290 300 NILRDKLTGR PRGVAFVRYN KREEAQEAIS ALNNVIPEGG SQPLSVRLAE EHGKAKAAHF 310 320 330 340 350 MSQMGVVPAN VPPPPPQPPA HMAAAFNMMH RGENFADLLD GLYRRKYHYP YL
	Isoform O. Checksum: 180D2C7B3316D85D	FASTA	364	39,839
	10 20 30 40 50 60 MDFNFDTVTP CSTMSSYYNF KMASGGRGFG MSHSLPSGMD TEFSFPSSSS RRGYNDFPGC 70 80 90 100 110 120 GGSGGNGGSA NNLGGGNMCH LPPMASNNSL NNLCGLSLGS GGSDDLMNDP RASNTNLIVN 130 140 150 160 170 180 YLPQDMTDRE LYALFRAIGP INTCRIMRDY KTGYSFGYAF VDFTSEMDSQ RAIKVLNGIT 190 200 210 220 230 240 VRNKRLKVSY ARPGGESIKD TNLYVTNLPR TITDDQLDTI FGKYGSIVQK NILRDKLTGR 250 260 270 280 290 300 PRGVAFVRYN KREEAQEAIS ALNNVIPEGG SQPLSVRLAE EHGKAKAAHF MSQMGVVPAN 310 320 330 340 350 360 VPPPPPQPPA HMAAAFNMMH RDGAMEKLRS LFDAICDAIF GLDSENFADL LDGLYRRKYH YPYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3144435] [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: 1710769] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"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.
[5]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MS16). Strain: Berkeley. Tissue: Embryo.
[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: 1547493] [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: 8978052] [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: 1454517] [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: 12444081] [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: 7524663] [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: 9299339] [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: 10217141] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 122-289, RNA-BINDING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M23635 mRNA. Translation: AAA28885.1.
M23636 mRNA. Translation: AAA28884.1.
M59447 mRNA. Translation: AAA28922.1.
M59448 mRNA. Translation: AAA28921.1.
AE014298 Genomic DNA. Translation: AAG22410.1.
AE014298 Genomic DNA. Translation: AAF46240.2.
AE014298 Genomic DNA. Translation: AAF46241.3.
AE014298 Genomic DNA. Translation: AAN09197.1.
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: AAZ52511.1.
AE014298 Genomic DNA. Translation: AAZ52513.1.
AE014298 Genomic DNA. Translation: AAZ52514.1.
BT003583 mRNA. Translation: AAO39587.1.
S88324 Genomic DNA. Translation: AAB21845.1.
D84425 Genomic DNA. Translation: BAA20294.1.

PIR

A31639.
B31639. A39725.

RefSeq

NP_001027062.1.
NP_001027063.1.
NP_001027064.1.
NP_001027065.1.
NP_001027066.1.
NP_001162686.1.
NP_001162687.1.
NP_001162690.1.
NP_001162691.1.
NP_524791.3.
NP_727160.2.
NP_727161.2.
NP_727162.2.
NP_727163.2.
NP_727164.2.
NP_727165.2.
NP_727166.2.
NP_727167.2.
NP_727168.1.

UniGene

Dm.4502

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B7F	X-ray	2.60	A/B	122-289	[»]
1SXL	NMR	-	A	199-294	[»]
2SXL	NMR	-	A	122-209	[»]
3SXL	X-ray	2.70	A/B/C	113-294	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P19339. 69 interactions.

STRING

P19339.

Proteomic databases

PRIDE

P19339.

Genome annotation databases

Ensembl

FBtr0100200; FBpp0099570; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100201; FBpp0099571; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100202; FBpp0099572; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100203; FBpp0099573; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100205; FBpp0099575; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100206; FBpp0099576; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100207; FBpp0099577; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100208; FBpp0099578; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100209; FBpp0099579; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100210; FBpp0099580; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100211; FBpp0099581; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100212; FBpp0099582; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100214; FBpp0099584; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100215; FBpp0099585; FBgn0003659; Drosophila melanogaster. [Genome view]
FBtr0100217; FBpp0099587; FBgn0003659; Drosophila melanogaster. [Genome view]

GeneID

3772180.

KEGG

dme:Dmel_CG18350.

Organism-specific databases

CTD

3772180.

FlyBase

FBgn0003659. Sxl.

Phylogenomic databases

eggNOG

inNOG07181.

InParanoid

P19339.

OMA

TIVQKNI.

OrthoDB

EOG99CQFD.

PhylomeDB

P19339.

Enzyme and pathway databases

BioCyc

DMEL-XXX-02:DMEL-XXX-02-000922-MONOMER.

Gene expression databases

GermOnline

CG18350. Drosophila melanogaster.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR002343. Hud_Sxl_RNA.
IPR000504. RRM_RNP1.
IPR006546. Sex_lethal_SF.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.

Pfam

PF00076. RRM_1. 2 hits.
[Graphical view]

PRINTS

PR00961. HUDSXLRNA.

SMART

SM00360. RRM. 2 hits.
[Graphical view]

TIGRFAMs

TIGR01659. sex-lethal. 1 hit.

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

852740.

Entry information

Entry name

SXL_DROME

Accession

Primary (citable) accession number: P19339
Secondary accession number(s): A4V435 , A4V437, P19340, Q0KHV2, Q26466, Q2MGN7, Q2MGN8, Q2MGN9, Q2MGP1, Q7KVU6, Q7YZ92, Q8IRQ1, Q99141, Q9TYF5, Q9W3S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	February 9, 2010
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project