LipidDB ID

LipidDB-7227-00290

Entry Name

UniProt Accession

P08928; Q9VMQ0;

Theoretical PI

6.1

Molecular Weight

71300.22

Genbank Protein ID

CAA30259.1; CAA34351.1; AAF52262.1; AAN71261.1;

Genbank Nucleotide ID

X07278; X16275; AE014134; BT001506;

Protein Name

Lamin Dm0

Protein Synonyms/Alias

Gene Name

Lam

Gene Synonyms/Alias

CG6944;

Created Date

01-NOV-1988

Organism

Drosophila melanogaster (Fruit fly)

NCBI Taxa ID

7227

Reference

[1] Polychronidou M, Hellwig A, Grosshans J. Farnesylated nuclear proteinsKugelkern and lamin Dm0 affect nuclear morphology by directly interacting withthe nuclear membrane. Mol Biol Cell. 2010 Oct 1;21(19):3409-20. doi:10.1091/mbc.E10-03-0230. Epub 2010 Aug 4.[PMID:20685963]

Functional Description

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.

Sequence Annotation

Domain: 465 578 LTD.
Region: 2 56 Head.
Region: 55 91 Coil 1A.
Region: 57 408 Rod.
Region: 92 103 Linker 1.
Region: 104 241 Coil 1B.
Region: 242 265 Linker 2.
Region: 266 408 Coil 2.
Region: 409 619 Tail.
Motif: 446 451 Nuclear localization signal.
Functional site: 289 289 Heptad change of phase.
Functional site: 353 353 Heptad change of phase.
Modified residue: 2 2 N-acetylserine.
Modified residue: 10 10 Phosphothreonine.
Modified residue: 12 12 Phosphothreonine.
Modified residue: 20 20 Phosphothreonine.
Modified residue: 25 25 Phosphoserine.
Modified residue: 34 34 Phosphoserine.
Modified residue: 39 39 Phosphothreonine.
Modified residue: 41 41 Phosphoserine.
Modified residue: 42 42 Phosphoserine.
Modified residue: 45 45 Phosphoserine.
Modified residue: 47 47 Phosphothreonine.
Modified residue: 235 235 Phosphoserine.
Modified residue: 249 249 Phosphotyrosine.
Modified residue: 250 250 Phosphoserine.
Modified residue: 311 311 Phosphoserine.
Modified residue: 413 413 Phosphothreonine.
Modified residue: 435 435 Phosphothreonine.
Modified residue: 442 442 Phosphoserine.
Modified residue: 455 455 Phosphoserine.
Modified residue: 459 459 Phosphoserine.
Modified residue: 595 595 Phosphoserine.
Modified residue: 597 597 Phosphothreonine.
Modified residue: 615 615 Phosphoserine.
Modified residue: 619 619 Cysteine methyl ester.

Protein Length

622 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005813; C:centrosome; IDA:FlyBase
GO:0005638; C:lamin filament; IDA:FlyBase
GO:0005811; C:lipid particle; IDA:FlyBase
GO:0005875; C:microtubule associated complex; IDA:FlyBase
GO:0072686; C:mitotic spindle; IDA:FlyBase
GO:0005635; C:nuclear envelope; IDA:FlyBase
GO:0005637; C:nuclear inner membrane; IEA:InterPro
GO:0005652; C:nuclear lamina; IDA:FlyBase
GO:0005634; C:nucleus; IDA:FlyBase
GO:0005102; F:receptor binding; IPI:UniProtKB
GO:0005198; F:structural molecule activity; IMP:FlyBase
GO:0008344; P:adult locomotory behavior; IMP:FlyBase
GO:0007569; P:cell aging; IMP:FlyBase
GO:0007417; P:central nervous system development; IMP:FlyBase
GO:0051297; P:centrosome organization; IMP:FlyBase
GO:0040003; P:chitin-based cuticle development; IMP:FlyBase
GO:0006342; P:chromatin silencing; IDA:FlyBase
GO:0001745; P:compound eye morphogenesis; IMP:FlyBase
GO:0048546; P:digestive tract morphogenesis; IMP:FlyBase
GO:0035262; P:gonad morphogenesis; IMP:FlyBase
GO:0046331; P:lateral inhibition; IMP:FlyBase
GO:0007084; P:mitotic nuclear envelope reassembly; IDA:FlyBase
GO:0006998; P:nuclear envelope organization; IMP:FlyBase
GO:0071763; P:nuclear membrane organization; IDA:FlyBase
GO:0007097; P:nuclear migration; IMP:FlyBase
GO:0031081; P:nuclear pore distribution; IMP:FlyBase
GO:0006997; P:nucleus organization; IMP:UniProtKB
GO:0090435; P:protein localization to nuclear envelope; IMP:FlyBase
GO:0007283; P:spermatogenesis; IMP:FlyBase
GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase

Interpro

InterPro; IPR001664; IF
InterPro; IPR027696; Lamin
InterPro; IPR001322; Lamin_tail_dom

Pfam

Pfam; PF00038; Filament;
Pfam; PF00932; LTD;

SMART

PROSITE

PRINTS