Reviewed,
UniProtKB/Swiss-Prot P08928 (LAM0_DROME)
Last modified
June 16, 2009.
Version 91.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lamin Dm0 | ||||
| Gene names |
| ||||
| 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 | 622 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Ref.1 |
| Subunit structure | Interacts directly with LBR. Ref.8 |
| Subcellular location | |
| Tissue specificity | Constitutively expressed in all tissues. Ref.7 |
| Developmental stage | Constitutively expressed in all developmental stages, especially during the first 6-9 hours. Ref.7 |
| Post-translational modification | Three forms of lamin have been identified in D.melanogaster, lamin Dm0 is rapidly processed to lamin Dm1 in the cytoplasm, Dm1 is then assembled in the nuclear envelope and is then phosphorylated, forming lamin Dm2. Ref.9 |
| Sequence similarities | Belongs to the intermediate filament family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 622 | 622 | Lamin Dm0 | PRO_0000063828 | |||||
Regions | |||||||||
| Region | 1 – 56 | 56 | Head | ||||||
| Region | 55 – 91 | 37 | Coil 1A | ||||||
| Region | 57 – 408 | 352 | Rod | ||||||
| Region | 92 – 103 | 12 | Linker 1 | ||||||
| Region | 104 – 241 | 138 | Coil 1B | ||||||
| Region | 242 – 265 | 24 | Linker 2 | ||||||
| Region | 266 – 408 | 143 | Coil 2 | ||||||
| Region | 409 – 622 | 214 | Tail | ||||||
| Motif | 446 – 451 | 6 | Nuclear localization signal Potential | ||||||
| Compositional bias | 28 – 33 | 6 | Poly-Pro | ||||||
Sites | |||||||||
| Site | 289 | 1 | Heptad change of phase | ||||||
| Site | 353 | 1 | Heptad change of phase | ||||||
Amino acid modifications | |||||||||
| Modified residue | 10 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 12 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 20 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 25 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 34 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 39 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 41 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 42 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 45 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 47 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 235 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 249 | 1 | Phosphotyrosine Ref.9 | ||||||
| Modified residue | 250 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 311 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 413 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 435 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 442 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 455 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 459 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 595 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 597 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 615 | 1 | Phosphoserine Ref.9 | ||||||
| Lipidation | 619 | 1 | S-farnesyl cysteine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 135 | 1 | E → R in CAA30259. Ref.1 | ||||||
| Sequence conflict | 270 – 271 | 2 | EL → DV in CAA30259. Ref.1 | ||||||
| Sequence conflict | 290 | 1 | Y → I in CAA30259. Ref.1 | ||||||
| Sequence conflict | 290 | 1 | Y → I in CAA34351. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Drosophila nuclear lamin precursor Dm0 is translated from either of two developmentally regulated mRNA species apparently encoded by a single gene." Gruenbaum Y., Landesman Y., Drees B., Bare J.W., Saumweber H., Paddy M.R., Sedat J.W., Smith D.E., Benton B.M., Fisher P.A. J. Cell Biol. 106:585-596(1988) [PubMed: 3126192] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, POST-TRANSLATIONAL MODIFICATION. Tissue: Embryo. |
| [2] | Stuurman N., Maus N., Fisher P.A. Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 24-39 AND 254-263. |
| [3] | "Molecular analysis of the Drosophila nuclear lamin gene." Osman M., Paz M., Landesman Y., Fainsod A., Gruenbaum Y. Genomics 8:217-224(1990) [PubMed: 2123469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [4] | "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. Venter J.C.Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley. |
| [5] | "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. Lewis S.E.Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. |
| [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. |
| [7] | "Expression of Drosophila lamin C is developmentally regulated: analogies with vertebrate A-type lamins." Riemer D., Stuurman N., Berrios M., Hunter C., Fisher P.A., Weber K. J. Cell Sci. 108:3189-3198(1995) [PubMed: 7593280] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. |
| [8] | "The lamin B receptor of Drosophila melanogaster." Wagner N., Weber D., Seitz S., Krohne G. J. Cell Sci. 117:2015-2028(2004) [PubMed: 15054108] [Abstract] Cited for: SUBUNIT, INTERACTION WITH LBR. |
| [9] | "Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; THR-12; THR-20; SER-25; SER-34; THR-39; SER-41; SER-42; SER-45; THR-47; SER-235; TYR-249; SER-250; SER-311; THR-413; THR-435; SER-442; SER-455; SER-459; SER-595; THR-597 AND SER-615, MASS SPECTROMETRY. Tissue: Embryo. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| X07278 mRNA. Translation: CAA30259.1. X16275 Genomic DNA. Translation: CAA34351.1. AE014134 Genomic DNA. Translation: AAF52262.1. BT001506 mRNA. Translation: AAN71261.1. | |
| PIR | A29965. A37103. |
| RefSeq | NP_476616.1. |
| UniGene | Dm.312 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GK7 based on UniProtKB P08670. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:2663N. |
| IntAct | P08928. 11 interactions. |
Genome annotation databases | |
| Ensembl | FBgn0002525. Drosophila melanogaster. [Contig view] |
| GeneID | 33782. |
| KEGG | dme:Dmel_CG6944. |
| NMPDR | fig|7227.3.peg.902. |
Organism-specific databases | |
| FlyBase | FBgn0002525. Lam. |
Phylogenomic databases | |
| HOGENOM | P08928. |
| OMA | P08928. INDEYQS. |
Gene expression databases | |
| ArrayExpress | P08928. |
| GermOnline | CG6944. Drosophila melanogaster. |
Family and domain databases | |
| InterPro | IPR016044. F. IPR001664. IF. IPR001322. IF_tail_C. IPR018039. Intermediate_filament_CS. [Graphical view] |
| PANTHER | PTHR23239. IF. 1 hit. |
| Pfam | PF00038. Filament. 1 hit. PF00932. IF_tail. 1 hit. [Graphical view] |
| PROSITE | PS00226. IF. False negative. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 785227. |
Entry information
| Entry name | LAM0_DROME | ||||||||
| Accession | Primary (citable) accession number: P08928 Secondary accession number(s): Q9VMQ0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with


