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Protein

Lamin Dm0

Gene

Lam

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei289 – 2891Heptad change of phase
Sitei353 – 3531Heptad change of phase

GO - Molecular functioni

  • receptor binding Source: UniProtKB
  • structural molecule activity Source: FlyBase

GO - Biological processi

  • adult locomotory behavior Source: FlyBase
  • cell aging Source: FlyBase
  • central nervous system development Source: FlyBase
  • centrosome organization Source: FlyBase
  • chitin-based cuticle development Source: FlyBase
  • chromatin silencing Source: FlyBase
  • compound eye morphogenesis Source: FlyBase
  • digestive tract morphogenesis Source: FlyBase
  • gonad morphogenesis Source: FlyBase
  • heterochromatin maintenance involved in chromatin silencing Source: FlyBase
  • lateral inhibition Source: FlyBase
  • mitotic nuclear envelope reassembly Source: FlyBase
  • negative regulation of cell proliferation Source: FlyBase
  • negative regulation of immune response Source: FlyBase
  • nuclear envelope organization Source: FlyBase
  • nuclear membrane organization Source: FlyBase
  • nuclear migration Source: FlyBase
  • nuclear pore distribution Source: FlyBase
  • nucleus organization Source: UniProtKB
  • protein localization to nuclear envelope Source: FlyBase
  • spermatogenesis Source: FlyBase
  • terminal branching, open tracheal system Source: FlyBase
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-DME-352238. Breakdown of the nuclear lamina.
R-DME-4419969. Depolymerisation of the Nuclear Lamina.

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin Dm0
Gene namesi
Name:Lam
ORF Names:CG6944
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0002525. Lam.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Nuclear periphery.

GO - Cellular componenti

  • centrosome Source: FlyBase
  • lamin filament Source: FlyBase
  • lipid particle Source: FlyBase
  • membrane Source: GOC
  • microtubule associated complex Source: FlyBase
  • mitotic spindle Source: FlyBase
  • nuclear envelope Source: FlyBase
  • nuclear lamina Source: FlyBase
  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 619618Lamin Dm0PRO_0000063828Add
BLAST
Propeptidei620 – 6223Removed in mature formBy similarityPRO_0000396785

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei10 – 101Phosphothreonine2 Publications
Modified residuei12 – 121Phosphothreonine2 Publications
Modified residuei20 – 201Phosphothreonine2 Publications
Modified residuei25 – 251Phosphoserine2 Publications
Modified residuei34 – 341Phosphoserine2 Publications
Modified residuei39 – 391Phosphothreonine2 Publications
Modified residuei41 – 411Phosphoserine2 Publications
Modified residuei42 – 421Phosphoserine2 Publications
Modified residuei45 – 451Phosphoserine2 Publications
Modified residuei47 – 471Phosphothreonine2 Publications
Modified residuei235 – 2351Phosphoserine2 Publications
Modified residuei249 – 2491Phosphotyrosine2 Publications
Modified residuei250 – 2501Phosphoserine2 Publications
Modified residuei311 – 3111Phosphoserine2 Publications
Modified residuei413 – 4131Phosphothreonine2 Publications
Modified residuei435 – 4351Phosphothreonine2 Publications
Modified residuei442 – 4421Phosphoserine2 Publications
Modified residuei455 – 4551Phosphoserine2 Publications
Modified residuei459 – 4591Phosphoserine1 Publication
Modified residuei595 – 5951Phosphoserine2 Publications
Modified residuei597 – 5971Phosphothreonine1 Publication
Modified residuei615 – 6151Phosphoserine2 Publications
Modified residuei619 – 6191Cysteine methyl esterBy similarity
Lipidationi619 – 6191S-farnesyl cysteineBy similarity

Post-translational modificationi

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 Dm2.2 Publications

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiP08928.
PRIDEiP08928.

PTM databases

iPTMnetiP08928.

Expressioni

Tissue specificityi

Constitutively expressed in all tissues.1 Publication

Developmental stagei

Constitutively expressed in all developmental stages, especially during the first 6-9 hours.1 Publication

Gene expression databases

BgeeiP08928.
ExpressionAtlasiP08928. differential.
GenevisibleiP08928. DM.

Interactioni

Subunit structurei

Interacts directly with LBR.1 Publication

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi59950. 15 interactions.
DIPiDIP-2663N.
IntActiP08928. 15 interactions.
MINTiMINT-853541.
STRINGi7227.FBpp0078733.

Structurei

3D structure databases

ProteinModelPortaliP08928.
SMRiP08928. Positions 54-143, 341-409, 468-572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini465 – 578114LTDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5655HeadAdd
BLAST
Regioni55 – 9137Coil 1AAdd
BLAST
Regioni57 – 408352RodAdd
BLAST
Regioni92 – 10312Linker 1Add
BLAST
Regioni104 – 241138Coil 1BAdd
BLAST
Regioni242 – 26524Linker 2Add
BLAST
Regioni266 – 408143Coil 2Add
BLAST
Regioni409 – 619211TailAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi446 – 4516Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 336Poly-Pro

Sequence similaritiesi

Belongs to the intermediate filament family.Curated
Contains 1 LTD domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
GeneTreeiENSGT00830000128282.
InParanoidiP08928.
KOiK07611.
OMAiWQLQRLI.
OrthoDBiEOG7MD4PW.
PhylomeDBiP08928.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF74853. SSF74853. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKSRRAGT ATPQPGNTST PRPPSAGPQP PPPSTHSQTA SSPLSPTRHS
60 70 80 90 100
RVAEKVELQN LNDRLATYID RVRNLETENS RLTIEVQTTR DTVTRETTNI
110 120 130 140 150
KNIFEAELLE TRRLLDDTAR DRARAEIDIK RLWEENEELK NKLDKKTKEC
160 170 180 190 200
TTAEGNVRMY ESRANELNNK YNQANADRKK LNEDLNEALK ELERLRKQFE
210 220 230 240 250
ETRKNLEQET LSRVDLENTI QSLREELSFK DQIHSQEINE SRRIKQTEYS
260 270 280 290 300
EIDGRLSSEY DAKLKQSLQE LRAQYEEQMQ INRDEIQSLY EDKIQRLQEA
310 320 330 340 350
AARTSNSTHK SIEELRSTRV RIDALNANIN ELEQANADLN ARIRDLERQL
360 370 380 390 400
DNDRERHGQE IDLLEKELIR LREEMTQQLK EYQDLMDIKV SLDLEIAAYD
410 420 430 440 450
KLLVGEEARL NITPATNTAT VQSFSQSLRN STRATPSRRT PSAAVKRKRA
460 470 480 490 500
VVDESEDHSV ADYYVSASAK GNVEIKEIDP EGKFVRLFNK GSEEVAIGGW
510 520 530 540 550
QLQRLINEKG PSTTYKFHRS VRIEPNGVIT VWSADTKASH EPPSSLVMKS
560 570 580 590 600
QKWVSADNTR TILLNSEGEA VANLDRIKRI VSQHTSSSRL SRRRSVTAVD
610 620
GNEQLYHQQG DPQQSNEKCA IM
Length:622
Mass (Da):71,300
Last modified:October 25, 2005 - v4
Checksum:iB77E48AA5CD9A8BD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351E → R in CAA30259 (PubMed:3126192).Curated
Sequence conflicti270 – 2712EL → DV in CAA30259 (PubMed:3126192).Curated
Sequence conflicti290 – 2901Y → I in CAA30259 (PubMed:3126192).Curated
Sequence conflicti290 – 2901Y → I in CAA34351 (PubMed:3126192).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07278 mRNA. Translation: CAA30259.1.
X16275 Genomic DNA. Translation: CAA34351.1.
AE014134 Genomic DNA. Translation: AAF52262.1.
BT001506 mRNA. Translation: AAN71261.1.
PIRiA29965.
A37103.
RefSeqiNP_001245892.1. NM_001258963.2.
NP_001245893.1. NM_001258964.2.
NP_001285629.1. NM_001298700.1.
NP_476616.1. NM_057268.5.
UniGeneiDm.312.

Genome annotation databases

EnsemblMetazoaiFBtr0079100; FBpp0078733; FBgn0002525.
FBtr0307058; FBpp0297901; FBgn0002525.
FBtr0307059; FBpp0297902; FBgn0002525.
FBtr0346460; FBpp0312110; FBgn0002525.
GeneIDi33782.
KEGGidme:Dmel_CG6944.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07278 mRNA. Translation: CAA30259.1.
X16275 Genomic DNA. Translation: CAA34351.1.
AE014134 Genomic DNA. Translation: AAF52262.1.
BT001506 mRNA. Translation: AAN71261.1.
PIRiA29965.
A37103.
RefSeqiNP_001245892.1. NM_001258963.2.
NP_001245893.1. NM_001258964.2.
NP_001285629.1. NM_001298700.1.
NP_476616.1. NM_057268.5.
UniGeneiDm.312.

3D structure databases

ProteinModelPortaliP08928.
SMRiP08928. Positions 54-143, 341-409, 468-572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59950. 15 interactions.
DIPiDIP-2663N.
IntActiP08928. 15 interactions.
MINTiMINT-853541.
STRINGi7227.FBpp0078733.

PTM databases

iPTMnetiP08928.

Proteomic databases

PaxDbiP08928.
PRIDEiP08928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079100; FBpp0078733; FBgn0002525.
FBtr0307058; FBpp0297901; FBgn0002525.
FBtr0307059; FBpp0297902; FBgn0002525.
FBtr0346460; FBpp0312110; FBgn0002525.
GeneIDi33782.
KEGGidme:Dmel_CG6944.

Organism-specific databases

CTDi33782.
FlyBaseiFBgn0002525. Lam.

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
GeneTreeiENSGT00830000128282.
InParanoidiP08928.
KOiK07611.
OMAiWQLQRLI.
OrthoDBiEOG7MD4PW.
PhylomeDBiP08928.

Enzyme and pathway databases

ReactomeiR-DME-352238. Breakdown of the nuclear lamina.
R-DME-4419969. Depolymerisation of the Nuclear Lamina.

Miscellaneous databases

GenomeRNAii33782.
NextBioi785227.
PROiP08928.

Gene expression databases

BgeeiP08928.
ExpressionAtlasiP08928. differential.
GenevisibleiP08928. DM.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF74853. SSF74853. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION 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 AND SER-615.
    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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiLAM0_DROME
AccessioniPrimary (citable) accession number: P08928
Secondary accession number(s): Q9VMQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 25, 2005
Last modified: May 11, 2016
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.