Reviewed, UniProtKB/Swiss-Prot Q7KRI2 (LOLAL_DROME)

Names and origin

Protein names

Recommended name:
    Longitudinals lacking protein-like
      Short name=Lola-like protein
Alternative name(s):
    Batman protein

Gene names

Name:	lolal
Synonyms:	ban
ORF Names:	CG5738

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	127 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required, together with Trl, for maintaining the repressed state of target genes including homeotic genes Scr and Ubx. May also be involved in the activation of homeotic genes. Binds to a DNA Polycomb response element (PRE) at the bithorax complex. Also binds to polytene chromosomes at several hundred sites, many of which are shared with Trl and ph-p. Required during embryonic development.
Subunit structure	The BTB domain interacts with the BTB domain of Trl in vitro. Found in a Pc-containing complex.
Subcellular location	Nucleus.
Sequence similarities	Contains 1 BTB (POZ) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator Chromatin regulator Developmental protein Repressor
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW chromatin silencing Ref.6 Inferred from mutant phenotype. Source: FlyBase embryonic development via the syncytial blastoderm Ref.6 Inferred from mutant phenotype. Source: UniProtKB positive regulation of transcription, DNA-dependent Ref.6 Inferred from genetic interaction. Source: UniProtKB
Cellular component	PcG protein complex Ref.5 Inferred from physical interaction. Source: UniProtKB condensed nuclear chromosome Ref.6 Inferred from direct assay. Source: UniProtKB polytene chromosome Ref.6 Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.5 Ref.6 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
bip2	Q9V4D4	1	EBI-84493,EBI-109298
ken	O77459	1	EBI-84493,EBI-193057
pfk	Q9VZU3	1	EBI-84493,EBI-147795
rib	Q9V8S2	1	EBI-84493,EBI-134581
Trl	Q08605	1	EBI-84493,EBI-300317
ttk	P42282	1	EBI-84493,EBI-77008

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 127	127	Longitudinals lacking protein-like		PRO_0000186221
Regions
	Domain	33 – 98	66	BTB

Sequences

	Sequence		Length	Mass (Da)
	Q7KRI2-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 3D5DE2C4E2E06B2D	FASTA	127	14,489
	10 20 30 40 50 60 MMSSDQQFFL KWNDFQTNMV TSFRHLRDEK SFTDVTLACE GQTCKAHKMV LSACSPYFKA 70 80 90 100 110 120 LLEENPSKHP IIILKDVSYI HLQAILEFMY AGEVNVSQEQ LPAFLKTADR LKVKGLAETP SSIKREG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Advantages of a P-element construct containing MtnA sequences for the identification of patterning and cell determination genes in Drosophila melanogaster." Faucheux M., Netter S., Bloyer S., Moussa M., Boissonneau E., Lemeunier F., Wegnez M., Theodore L. Mol. Genet. Genomics 265:14-22(2001) [PubMed: 11370860] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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.
[3]	"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.
[4]	"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.
[5]	"Trl-GAGA directly interacts with lola like and both are part of the repressive complex of Polycomb group of genes." Mishra K., Chopra V.S., Srinivasan A., Mishra R.K. Mech. Dev. 120:681-689(2003) [PubMed: 12834867] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRL, IDENTIFICATION IN A COMPLEX WITH PC.
[6]	"Batman interacts with polycomb and trithorax group genes and encodes a BTB/POZ protein that is included in a complex containing GAGA factor." Faucheux M., Roignant J.-Y., Netter S., Charollais J., Antoniewski C., Theodore L. Mol. Cell. Biol. 23:1181-1195(2003) [PubMed: 12556479] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRL, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF308476 mRNA. Translation: AAG45054.1. AE013599 Genomic DNA. Translation: AAF57739.1. AE013599 Genomic DNA. Translation: AAM68180.1. AE013599 Genomic DNA. Translation: AAM68181.1. AY060364 mRNA. Translation: AAL25403.1.
RefSeq	NP_524778.1. NP_725756.1. NP_725757.1. NP_725758.1.
UniGene	Dm.1712
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q7KRI2.
Genome annotation databases
Ensembl	CG5738. Drosophila melanogaster. [Contig view]
GeneID	44703.
KEGG	dme:Dmel_CG5738.
Organism-specific databases
FlyBase	FBgn0022238. lolal.
Phylogenomic databases
HOGENOM	Q7KRI2.
Gene expression databases
ArrayExpress	Q7KRI2.
GermOnline	CG5738. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. IPR013069. BTB_POZ. [Graphical view]
Gene3D	G3DSA:3.30.710.10. BTB/POZ_fold. 1 hit.
Pfam	PF00651. BTB. 1 hit. [Graphical view]
SMART	SM00225. BTB. 1 hit. [Graphical view]
PROSITE	PS50097. BTB. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	837561.

Entry information

Entry name

LOLAL_DROME

Accession

Primary (citable) accession number: Q7KRI2
Secondary accession number(s): A4UZN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	July 5, 2004
Last modified:	November 25, 2008
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project