P09774 (AST3_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Achaete-scute complex protein T3

Alternative name(s):
Protein lethal of scute
Short name=Lethal of sc

Gene names

Name:	l(1)sc
Synonyms:	l'sc, T3
ORF Names:	CG3839

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	257 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	AS-C proteins are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system.
Subunit structure	Efficient DNA binding requires dimerization with another bHLH protein.
Tissue specificity	L1SC, SC and AC strongly label the presumptive stomatogastric nervous system, while ASE is more prominent in the presumptive procephalic lobe.
Miscellaneous	AS-C proteins are expressed first earlier in ectoderm and then in the internalized neuroblasts, while T8 is expressed in presumptive neural precursors, once they have segregated from the ectoderm.
Sequence similarities	Contains 1 basic helix-loop-helix (bHLH) domain.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Ligand	DNA-binding
Molecular function	Developmental protein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	myoblast cell fate determination Traceable author statement. Source: FlyBase neuroblast fate determination Traceable author statement. Source: FlyBase peripheral nervous system development Non-traceable author statement. Source: FlyBase ventral cord development Traceable author statement. Source: FlyBase
Molecular function	protein heterodimerization activity Inferred from physical interaction. Source: FlyBase sequence-specific DNA binding Inferred from direct assay. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 257	257	Achaete-scute complex protein T3		PRO_0000127135
Regions
	Domain	97 – 146	50	Helix-loop-helix motif
	DNA binding	86 – 96	11	Basic motif
Experimental info
	Sequence conflict	198	1	H → R in CAA31065. Ref.1
	Sequence conflict	257	1	Q → R in AAM52020. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P09774 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: 1AEC8FA0B3144F87	FASTA	257	28,972
	10 20 30 40 50 60 MTSICSSKFQ QQHYQLTNSN IFLLQHQHHH QTQQHQLIAP KIPLGTSQLQ NMQQSQQSNV 70 80 90 100 110 120 GPMLSSQKKK FNYNNMPYGE QLPSVARRNA RERNRVKQVN NGFVNLRQHL PQTVVNSLSN 130 140 150 160 170 180 GGRGSSKKLS KVDTLRIAVE YIRGLQDMLD DGTASSTRHI YNSADESSND GSSYNDYNDS 190 200 210 220 230 240 LDSSQQFLTG ATQSAQSHSY HSASPTPSYS GSEISGGGYI KQELQEQDLK FDSFDSFSDE 250 QPDDEELLDY ISSWQEQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The achaete-scute gene complex of Drosophila melanogaster comprises four homologous genes." Alonso M.C., Cabrera C.V. EMBO J. 7:2585-2591(1988) [PubMed: 2461300] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: Canton-S.
[2]	"Molecular characterization of the lethal of scute genetic function." Martin-Bermudo M.D., Gonzalez F., Dominguez M., Rodriguez I., Ruiz-Gomez M., Romani S., Modolell J., Jimenez F. Development 118:1003-1012(1993) [PubMed: 8076513] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Canton-S. 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. Strain: Berkeley.
[5]	"From sequence to chromosome: the tip of the X chromosome of D. melanogaster." Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M. Science 287:2220-2222(2000) [PubMed: 10731137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Oregon-R.
[6]	"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]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X12549 Genomic DNA. Translation: CAA31065.1. X71806 mRNA. Translation: CAA50680.1. AE014298 Genomic DNA. Translation: AAF45500.1. AL024453 Genomic DNA. Translation: CAA19656.1. AY121693 mRNA. Translation: AAM52020.1.
PIR	S01165.
RefSeq	NP_476623.1. NM_057275.4.
UniGene	Dm.1705.
3D structure databases
ProteinModelPortal	P09774.
SMR	P09774. Positions 87-151.
ModBase	Search...
Protein-protein interaction databases
IntAct	P09774. 1 interaction.
STRING	P09774.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0070074; FBpp0070073; FBgn0002561.
GeneID	30983.
KEGG	dme:Dmel_CG3839.
NMPDR	fig|7227.3.peg.15889.
Organism-specific databases
FlyBase	FBgn0002561. l(1)sc.
Phylogenomic databases
eggNOG	inNOG10728.
GeneTree	EMGT00050000001630.
InParanoid	P09774.
OMA	DYISSWQ.
OrthoDB	EOG4QNKCG.
PhylomeDB	P09774.
Gene expression databases
ArrayExpress	P09774.
Bgee	P09774.
GermOnline	CG3839. Drosophila melanogaster.
Family and domain databases
InterPro	IPR015660. ASH. IPR011598. HLH_DNA-bd. [Graphical view]
Gene3D	G3DSA:4.10.280.10. HLH_DNA_bd. 1 hit.
KO	K09067.
PANTHER	PTHR13935. ASH. 1 hit.
Pfam	PF00010. HLH. 1 hit. [Graphical view]
SMART	SM00353. HLH. 1 hit. [Graphical view]
SUPFAM	SSF47459. HLH_basic. 1 hit.
PROSITE	PS50888. HLH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	771316.

Entry information

Entry name

AST3_DROME

Accession

Primary (citable) accession number: P09774
Secondary accession number(s): Q24387, Q8MRA5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	February 21, 2001
Last modified:	January 25, 2012
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project