P40796 (LA_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
La protein homolog

Alternative name(s):
La autoantigen homolog
La ribonucleoprotein

Gene names

Name:	La
ORF Names:	CG10922

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

General annotation (Comments)

Function	May be involved in transcription termination by RNA polymerase III. Binds RNA and DNA. Binds to precursors of RNA polymerase III transcripts. May play a specialized role during fly development.
Subcellular location	Nucleus Probable.
Developmental stage	Expressed throughout embryonic, larval, pupal, and adult development. Expression throughout the embryo is followed by a restricted pattern of mesodermal expression that is later confined to the visceral mesoderm, gonads, gut, and salivary glands.
Sequence similarities	Contains 1 HTH La-type RNA-binding domain. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	DNA-binding RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	RNA processing Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Inferred from electronic annotation. Source: InterPro
Molecular function	5S rRNA primary transcript binding Inferred from direct assay Ref.2. Source: FlyBase DNA binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA binding Non-traceable author statement. Source: FlyBase nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 390	390	La protein homolog		PRO_0000207606
Regions
	Domain	44 – 137	94	HTH La-type RNA-binding
	Domain	149 – 234	86	RRM
Amino acid modifications
	Modified residue	7	1	Phosphothreonine Ref.5
	Modified residue	9	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	169	1	A → T in AAA20518. Ref.1
	Sequence conflict	182 – 183	2	KH → NS in AAA20518. Ref.1
	Sequence conflict	283	1	A → R in AAA20518. Ref.1
	Sequence conflict	329	1	K → N in AAA20518. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P40796 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: A8099288B90446A5	FASTA	390	44,885
	10 20 30 40 50 60 MAEVAETPSV EAQEEVAQPA EAQVLEAKNG DAKKDPAPAA EEAAGGFTKQ ERAIIRQVEY 70 80 90 100 110 120 YFGDANLNRD KFLREQIGKN EDGWVPLSVL VTFKRLASLS TDLSEIVAAL NKSEEGLVEI 130 140 150 160 170 180 SEDKLSLRRH PERPIPEHNE ERRKEIQERT AYAKGFPLDS QISELLDFAA NYDKVVNLTM 190 200 210 220 230 240 RKHYDKPTKS YKFKGSIFLT FETKDQAKAF LEQEKIVYKE RELLRKWQVD YLKEKQEEYA 250 260 270 280 290 300 QKNEKRKNKK EAKPEPAFEL PKNAIVVFEG APETSSREEI REAFEKIKDF EVAYIEFAKG 310 320 330 340 350 360 ETKGSVRLTE ADAAEKYIAK VEEGKLKFKD EVSLSLRKAT EEEEKEFIDK AIEFMKKRRD 370 380 390 FTRNKGKRFN RKRHGGNDHK HGGGKKARGD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Developmental characterization of a Drosophila RNA-binding protein homologous to the human systemic lupus erythematosus-associated La/SS-B autoantigen." Bai C., Li Z., Tolias P.P. Mol. Cell. Biol. 14:5123-5129(1994) [PubMed: 8035794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Canton-S. Tissue: Ovary.
[2]	"La proteins from Drosophila melanogaster and Saccharomyces cerevisiae: a yeast homolog of the La autoantigen is dispensable for growth." Yoo C.J., Wolin S.L. Mol. Cell. Biol. 14:5412-5424(1994) [PubMed: 8035818] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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]	"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7 AND SER-9, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U07652 mRNA. Translation: AAA20518.1. L32988 mRNA. Translation: AAA21776.1. AE014134 Genomic DNA. Translation: AAF53885.1.
PIR	A53773. A53781.
RefSeq	NP_477014.1. NM_057666.4. NP_724257.1. NM_165326.2.
UniGene	Dm.4836.
3D structure databases
ProteinModelPortal	P40796.
SMR	P40796. Positions 45-235, 257-367.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-19001N.
IntAct	P40796. 3 interactions.
MINT	MINT-785398.
STRING	P40796.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0081373; FBpp0080905; FBgn0011638. FBtr0081374; FBpp0080906; FBgn0011638.
GeneID	35305.
KEGG	dme:Dmel_CG10922.
Organism-specific databases
CTD	35305.
FlyBase	FBgn0011638. La.
Phylogenomic databases
eggNOG	inNOG07032.
InParanoid	P40796.
OMA	EHNEERR.
OrthoDB	EOG4GF1X7.
PhylomeDB	P40796.
Gene expression databases
ArrayExpress	P40796.
Bgee	P40796.
GermOnline	CG10922. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002344. Lupus_La. IPR006630. Lupus_La_RNA-bd. IPR012677. Nucleotide-bd_a/b_plait. IPR014886. RRM_3. IPR000504. RRM_dom. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K11090.
Pfam	PF05383. La. 1 hit. PF08777. RRM_3. 1 hit. [Graphical view]
PRINTS	PR00302. LUPUSLA.
SMART	SM00715. LA. 1 hit. SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50961. HTH_LA. 1 hit. PS50102. RRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	792866.

Entry information

Entry name

LA_DROME

Accession

Primary (citable) accession number: P40796
Secondary accession number(s): Q24375, Q9VIN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project