Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q24400 (MLP2_DROME)

Last modified November 4, 2008. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Muscle LIM protein Mlp84B
Gene names
Name: Mlp84B
Synonyms: LIM3
ORF Names: CG10699
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Hide | Top

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Plays a role in cell differentiation late in myogenesis. Transcription factor Mef2 is essential for expression.

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

In the embryo, expression is restricted to the somatic, viceral, and pharyngeal muscles. Within the somatic musculature, expression is localized at the ends of muscles fibers at the point of attachment to the epidermis (at protein level). There is no expression in cardiac mesoderm or in fat body.

Developmental stage

Expression is biphasic, peaking late in embryogenesis (16-24 hours embryos) and during the larval to pupal transition, when the musculature is differentiating. Found in developing muscles of the visceral and somatic mesoderm subsequent to the formation of the muscle precursor cells. Decreased levels are still detectable in adults.

Sequence similarities

Contains 5 LIM zinc-binding domains.

Hide | Top

Ontologies

Keywords

   Biological processDifferentiation
Myogenesis
   Cellular componentCytoplasm
Nucleus
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   Molecular functionDevelopmental protein
   Technical termComplete proteome

Gene Ontology (GO)

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Muscle LIM protein Mlp84B
PRO_0000075852

Regions

Domain12 – 6352LIM zinc-binding 1
Domain120 – 17253LIM zinc-binding 2
Domain222 – 27453LIM zinc-binding 3
Domain325 – 37753LIM zinc-binding 4
Domain421 – 47353LIM zinc-binding 5
Motif66 – 716Nuclear localization signal Potential
Motif175 – 1806Nuclear localization signal Potential
Compositional bias65 – 8016Gly-rich
Compositional bias178 – 18912Gly-rich
Compositional bias276 – 29116Gly-rich
Compositional bias379 – 39012Gly-rich
Compositional bias475 – 49016Gly-rich

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q24400-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2E559B9178E54C0E

FASTA49553,526
        10         20         30         40         50         60 
MPSFQPIEAP KCPRCGKSVY AAEERLAGGY VFHKNCFKCG MCNKSLDSTN CTEHERELYC 

        70         80         90        100        110        120 
KTCHGRKFGP KGYGFGTGAG TLSMDNGSQF LRENGDVPSV RNGARLEPRA IARAPEGEGC 

       130        140        150        160        170        180 
PRCGGYVYAA EQMLARGRSW HKECFKCGTC KKGLDSILCC EAPDKNIYCK GCYAKKFGPK 

       190        200        210        220        230        240 
GYGYGQGGGA LQSDCYAHDD GAPQIRAAID VDKIQARPGE GCPRCGGVVY AAEQKLSKGR 

       250        260        270        280        290        300 
EWHKKCFNCK DCHKTLDSIN ASDGPDRDVY CRTCYGKKWG PHGYGFACGS GFLQTDGLTE 

       310        320        330        340        350        360 
DQISANRPFY NPDTTSIKAR DGEGCPRCGG AVFAAEQQLS KGKVWHKKCY NCADCHRPLD 

       370        380        390        400        410        420 
SVLACDGPDG DIHCRACYGK LFGPKGFGYG HAPTLVSTSG ESTIQFPDGR PLAGPKTSGG 

       430        440        450        460        470        480 
CPRCGFAVFA AEQMISKTRI WHKRCFYCSD CRKSLDSTNL NDGPDGDIYC RACYGRNFGP 

       490 
KGVGYGLGAG ALTTF

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Two muscle-specific LIM proteins in Drosophila."
Stronach B.E., Siegrist S.E., Beckerle M.C.
J. Cell Biol. 134:1179-1195(1996) [PubMed: 8794860] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]"Muscle LIM proteins are associated with muscle sarcomeres and require dMEF2 for their expression during Drosophila myogenesis."
Stronach B.E., Renfranz P.J., Lilly B., Beckerle M.C.
Mol. Biol. Cell 10:2329-2342(1999) [PubMed: 10397768] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
[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. expand/collapse author list , 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. expand/collapse author list , 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.
[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. expand/collapse author list , 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 (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

X91245 mRNA. Translation: CAA62627.1.
AF090832 Genomic DNA. Translation: AAC61591.1.
AE014297 Genomic DNA. Translation: AAF54063.1.
BT003202 mRNA. Translation: AAO24957.1.
RefSeqNP_477122.1.
NP_731134.1.
UniGeneDm.5906

3D structure databases

HSSPHSSP built from PDB template 1CTL based on UniProtKB P32965.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:17587N.
IntActQ24400.

Genome annotation databases

EnsemblCG1019. Drosophila melanogaster. [Contig view]
GeneID40849.
KEGGdme:Dmel_CG1019.

Organism-specific databases

FlyBaseFBgn0014863. Mlp84B.

Phylogenomic databases

HOGENOMQ24400.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-010354-MON.
DMEL-XXX-02:DMEL-XXX-02-010355-MON.

Gene expression databases

ArrayExpressQ24400.
GermOnlineCG1019. Drosophila melanogaster.

Family and domain databases

InterProIPR001781. Znf_LIM.
[Graphical view]
Gene3DG3DSA:2.10.110.10. Znf_LIM. 5 hits.
PfamPF00412. LIM. 5 hits.
[Graphical view]
ProDomPD000094. LIM. 5 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00132. LIM. 5 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 5 hits.
PS50023. LIM_DOMAIN_2. 5 hits.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio820948.

Hide | Top

Entry information

Entry nameMLP2_DROME
AccessionPrimary (citable) accession number: Q24400
Secondary accession number(s): Q9VI62
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 4, 2008
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Hide | Top

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents