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P48679 (LMNA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prelamin-A/C

Cleaved into the following chain:

  1. Lamin-A/C
Gene names
Name:Lmna
Synonyms:Lmn1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics By similarity.

Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence By similarity.

Subunit structure

Homodimer of lamin A and lamin C. Interacts with lamin-associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin. Interacts with SREBF1, SREBF2, SUN1, SUN2 and TMEM43. Proteolytically processed isoform A interacts with NARF. Prelamin-A/C interacts with EMD. Interacts with MLIP; may regulate MLIP localization to the nucleus envelope. Interacts with DMPK; may regulate nuclear envelope stability By similarity.

Subcellular location

Nucleus By similarity. Nucleus envelope By similarity. Note: Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C By similarity.

Post-translational modification

Proteolytic cleavage of the C-terminal of 18 residues of prelamin-A/C results in the production of lamin-A/C. The prelamin-A/C maturation pathway includes farnesylation of CAAX motif, ZMPSTE24/FACE1 mediated cleavage of the last three amino acids, methylation of the C-terminal cysteine and endoproteolytic removal of the last 15 C-terminal amino acids. Proteolytic cleavage requires prior farnesylation and methylation, and absence of these blocks cleavage By similarity.

Sumoylation is necessary for the localization to the nuclear envelope By similarity.

Farnesylation of prelamin-A/C facilitates nuclear envelope targeting By similarity.

Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations.

Miscellaneous

The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively.

Sequence similarities

Belongs to the intermediate filament family.

Sequence caution

The sequence CAA47342.1 differs from that shown. Reason: Frameshift at positions 21, 83 and 584.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]

Note: Isoform A and isoform C are present in equal amounts in the lamina of mammals.
Isoform Lamin A (identifier: P48679-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Lamin C (identifier: P48679-2)

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 662662Prelamin-A/C
PRO_0000398841
Chain1 – 647647Lamin-A/C
PRO_0000063813
Propeptide648 – 66215Removed in Lamin-A/C form By similarity
PRO_0000398842
Propeptide663 – 6653Removed in Prelamin-A/C form and in Lamin-A/C form By similarity
PRO_0000403445

Regions

Region1 – 130130Interaction with MLIP By similarity
Region1 – 3333Head
Region34 – 383350Rod
Region34 – 7037Coil 1A
Region71 – 8010Linker 1
Region81 – 218138Coil 1B
Region219 – 24224Linker 2
Region243 – 383141Coil 2
Region384 – 665282Tail
Motif417 – 4226Nuclear localization signal Potential

Sites

Site2661Heptad change of phase
Site3251Stutter By similarity
Site3301Heptad change of phase
Site647 – 6482Cleavage; by endoprotease By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue31Phosphothreonine By similarity
Modified residue121Phosphoserine By similarity
Modified residue181Phosphoserine By similarity
Modified residue191Phosphothreonine By similarity
Modified residue221Phosphoserine By similarity
Modified residue1081N6-acetyllysine By similarity
Modified residue2121Phosphoserine By similarity
Modified residue2701N6-acetyllysine By similarity
Modified residue2771Phosphoserine By similarity
Modified residue3011Phosphoserine By similarity
Modified residue3111N6-acetyllysine By similarity
Modified residue3901Phosphoserine By similarity
Modified residue3921Phosphoserine Ref.4
Modified residue3951Phosphoserine By similarity
Modified residue3981Phosphoserine By similarity
Modified residue4041Phosphoserine By similarity
Modified residue4061Phosphoserine By similarity
Modified residue4071Phosphoserine By similarity
Modified residue4091Phosphoserine By similarity
Modified residue4141Phosphoserine By similarity
Modified residue4311Phosphoserine By similarity
Modified residue4501N6-acetyllysine By similarity
Modified residue4581Phosphoserine By similarity
Modified residue4631Phosphoserine By similarity
Modified residue4961Phosphothreonine Ref.4
Modified residue5051Phosphothreonine Ref.4
Modified residue5071Phosphoserine Ref.4
Modified residue5101Phosphothreonine Ref.4
Modified residue5731Phosphoserine By similarity
Modified residue5751Phosphoserine By similarity
Modified residue6291Phosphoserine By similarity
Modified residue6331Phosphoserine By similarity
Modified residue6371Phosphoserine By similarity
Modified residue6531Phosphoserine By similarity
Modified residue6621Cysteine methyl ester By similarity
Lipidation6621S-farnesyl cysteine By similarity
Cross-link201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Experimental info

Sequence conflict4701K → R in CAA47342. Ref.1
Sequence conflict5241T → S in CAA47342. Ref.1
Sequence conflict5841R → P in CAA47342. Ref.1
Sequence conflict6061A → P in CAA47342. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Lamin A [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9CC553005C8534E4

FASTA66574,324
        10         20         30         40         50         60 
METPSQRRPT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR SLETENAGLR 

        70         80         90        100        110        120 
LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA RLQLELSKVR EEFKELKARN 

       130        140        150        160        170        180 
TKKEGDLLAA QARLKDLEAL LNSKEAALST ALSEKRTLEG ELHDLRGQVA KLEAALGEAK 

       190        200        210        220        230        240 
KQLQDEMLRR VDAENRLQTL KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR 

       250        260        270        280        290        300 
LADALQELRA QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID 

       310        320        330        340        350        360 
SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAE KEREMAEMRA RMQQQLDEYQ 

       370        380        390        400        410        420 
ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG RASSHSSQSQ GGGSVTKKRK 

       430        440        450        460        470        480 
LESSESRSSF SQHARTSGRV AVEEVDEEGK FVRLRNKSNE DQSMGNWQIK RQNGDDPLMT 

       490        500        510        520        530        540 
YRFPPKFTLK AGQVVTIWAS GAGATHSPPT DLVWKAQNTW GCGTSLRTAL INATGEEVAM 

       550        560        570        580        590        600 
RKLVRSLTMV EDNDDEEEDG DELLHHHRGS HCSSSGDPAE YNLRSRTVLC GTCGQPADKA 

       610        620        630        640        650        660 
ASGSGAQVGG SISSGSSASS VTVTRSFRSV GGSGGGSFGD NLVTRSYLLG NSSPRTQSSQ 


NCSIM

« Hide

Isoform Lamin C (Sequence not available). ––

References

« Hide 'large scale' references
[1]"Lamin A gene expression is specifically suppressed in v-src-transformed cells."
Ozaki T., Sakiyama S.
FEBS Lett. 312:165-168(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Jonnalagadda V.S., Parnaik V.K.
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-663.
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"Proteome analysis of a rat liver nuclear insoluble protein fraction and localization of a novel protein, ISP36, to compartments in the interchromatin space."
Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K., Watanabe Y., Furukawa K., Horigome T.
FEBS J. 272:4327-4338(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 124-132; 209-215; 320-328 AND 629-643.
Tissue: Liver.
[4]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; THR-496; THR-505; SER-507 AND THR-510, MASS SPECTROMETRY.
Tissue: Renal collecting duct.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X66870 mRNA. Translation: CAA47342.1. Frameshift.
X76297 mRNA. Translation: CAA53945.1.
IPIIPI00201060.
PIRS27267.
RefSeqNP_001002016.1. NM_001002016.1.
UniGeneRn.44161.

3D structure databases

ProteinModelPortalP48679.
SMRP48679. Positions 29-65, 313-386, 428-549.
ModBaseSearch...

Protein-protein interaction databases

IntActP48679. 2 interactions.

PTM databases

PhosphoSiteP48679.

Proteomic databases

PaxDbP48679.
PRIDEP48679.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID60374.
KEGGrno:60374.
UCSCRGD:620456. rat.

Organism-specific databases

CTD4000.
RGD620456. Lmna.

Phylogenomic databases

eggNOGNOG325506.
HOGENOMHOG000007711.
HOVERGENHBG013015.
InParanoidP48679.
KOK12641.
OrthoDBEOG4S4PG2.

Gene expression databases

ArrayExpressP48679.
GenevestigatorP48679.
GermOnlineENSRNOG00000019638. Rattus norvegicus.

Family and domain databases

InterProIPR016044. F.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio612051.

Entry information

Entry nameLMNA_RAT
AccessionPrimary (citable) accession number: P48679
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents