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Protein

Prelamin-A/C

Gene

LMNA

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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. 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. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (By similarity).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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei266 – 2661Heptad change of phase
Sitei325 – 3251StutterBy similarity
Sitei330 – 3301Heptad change of phase

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Prelamin-A/C
Cleaved into the following chain:
Gene namesi
Name:LMNA
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Nucleus By similarity
  • Nucleus envelope By similarity
  • Nucleus lamina By similarity
  • Nucleusnucleoplasm 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 661661Prelamin-A/CPRO_0000398839Add
BLAST
Chaini1 – 646646Lamin-A/CPRO_0000063812Add
BLAST
Propeptidei647 – 66115Removed in Lamin-A/C formBy similarityPRO_0000398840Add
BLAST
Propeptidei662 – 6643Removed in Prelamin-A/C form and in Lamin-A/C formBy similarityPRO_0000403444

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei3 – 31PhosphothreonineBy similarity
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei18 – 181PhosphoserineBy similarity
Modified residuei19 – 191PhosphothreonineBy similarity
Modified residuei22 – 221PhosphoserineBy similarity
Modified residuei32 – 321N6-acetyllysine; alternateBy similarity
Modified residuei32 – 321N6-succinyllysine; alternateBy similarity
Cross-linki97 – 97Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei123 – 1231N6-acetyllysineBy similarity
Modified residuei135 – 1351N6-acetyllysineBy similarity
Modified residuei155 – 1551N6-acetyllysineBy similarity
Modified residuei171 – 1711N6-acetyllysine; alternateBy similarity
Modified residuei171 – 1711N6-succinyllysine; alternateBy similarity
Modified residuei201 – 2011N6-acetyllysine; alternateBy similarity
Cross-linki201 – 201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki208 – 208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei212 – 2121PhosphoserineBy similarity
Cross-linki233 – 233Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei260 – 2601N6-acetyllysine; alternateBy similarity
Cross-linki260 – 260Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei270 – 2701N6-acetyllysine; alternateBy similarity
Cross-linki270 – 270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei277 – 2771PhosphoserineBy similarity
Modified residuei301 – 3011PhosphoserineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei311 – 3111N6-acetyllysine; alternateBy similarity
Cross-linki311 – 311Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki378 – 378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei390 – 3901PhosphoserineBy similarity
Modified residuei392 – 3921PhosphoserineBy similarity
Modified residuei395 – 3951PhosphoserineBy similarity
Modified residuei403 – 4031PhosphoserineBy similarity
Modified residuei404 – 4041PhosphoserineBy similarity
Modified residuei407 – 4071PhosphoserineBy similarity
Modified residuei414 – 4141PhosphoserineBy similarity
Cross-linki417 – 417Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki420 – 420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei431 – 4311PhosphoserineBy similarity
Modified residuei450 – 4501N6-acetyllysineBy similarity
Modified residuei457 – 4571N6-acetyllysineBy similarity
Modified residuei458 – 4581PhosphoserineBy similarity
Modified residuei463 – 4631PhosphoserineBy similarity
Modified residuei496 – 4961PhosphothreonineBy similarity
Modified residuei505 – 5051PhosphothreonineBy similarity
Modified residuei546 – 5461PhosphoserineBy similarity
Modified residuei548 – 5481PhosphothreonineBy similarity
Modified residuei568 – 5681PhosphoserineBy similarity
Modified residuei571 – 5711PhosphoserineBy similarity
Modified residuei612 – 6121PhosphoserineBy similarity
Modified residuei616 – 6161PhosphoserineBy similarity
Modified residuei619 – 6191PhosphoserineBy similarity
Modified residuei628 – 6281PhosphoserineBy similarity
Modified residuei632 – 6321PhosphoserineBy similarity
Modified residuei636 – 6361PhosphoserineBy similarity
Modified residuei661 – 6611Cysteine methyl esterBy similarity
Lipidationi661 – 6611S-farnesyl cysteineBy similarity

Post-translational modificationi

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).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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei646 – 6472Cleavage; by endoproteaseBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

PaxDbiQ3ZD69.
PRIDEiQ3ZD69.

Interactioni

Subunit structurei

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 Interacts with SUV39H1; the interaction increases stability of SUV39H1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000006923.

Structurei

3D structure databases

ProteinModelPortaliQ3ZD69.
SMRiQ3ZD69. Positions 29-65, 313-386, 428-549.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini432 – 545114LTDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 130130Interaction with MLIPBy similarityAdd
BLAST
Regioni1 – 3333HeadAdd
BLAST
Regioni34 – 383350RodAdd
BLAST
Regioni34 – 7037Coil 1AAdd
BLAST
Regioni71 – 8010Linker 1
Regioni81 – 218138Coil 1BAdd
BLAST
Regioni219 – 24224Linker 2Add
BLAST
Regioni243 – 383141Coil 2Add
BLAST
Regioni384 – 664281TailAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi417 – 4226Nuclear localization signalSequence analysis

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiQ3ZD69.
KOiK12641.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
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.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Isoform A and isoform C are present in equal amounts in the lamina of mammals.

Isoform A (identifier: Q3ZD69-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
METPSQRRAT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR
60 70 80 90 100
SLETENAGLR LRITESEEVV SREVSGIKSA YEAELGDARK TLDSVAKERA
110 120 130 140 150
RLQLELSKVR EEFKELKARN TKKEGDLMAA QARLKDLEAL LNSKEAALST
160 170 180 190 200
ALSEKRTLEG ELHDLRGQVA KLEAALGEAK KQLQDEMLRR VDAENRLQTL
210 220 230 240 250
KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR LADALQDLRA
260 270 280 290 300
QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID
310 320 330 340 350
SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAD KEREMAEMRA
360 370 380 390 400
RMQQQLDEYQ ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG
410 420 430 440 450
RASSHSSQTQ SGGSVTKKRK LESSESRSSF SQHARTSGRV AVEEVDEEGK
460 470 480 490 500
FVRLRNKSNE DQSMGNWQIK RQNGDDPLLT YRFPPKFTLK AGQVVTIWAA
510 520 530 540 550
GAGATHSPPA DLVWKSQNTW GCGNSLRTAL INSTGEEVAM RKLVRSVTMI
560 570 580 590 600
EDDEDEDGDD LLHHHHGSHG SSSGDPAEYN LRSRTVLCGT CGQPADKASA
610 620 630 640 650
SSSGAQVGGS ISSGSSASSV TVTRSYRSVG GSGGGSFGDN LVTRSYLLGN
660
SRPRTQSPQN CSIM
Length:664
Mass (Da):74,219
Last modified:September 27, 2005 - v1
Checksum:iAFA882BBA33C4547
GO
Isoform C (identifier: Q3ZD69-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     567-572: GSHGSS → VSGSRR
     573-664: Missing.

Show »
Length:572
Mass (Da):65,171
Checksum:i381C67C43AC9BDC7
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei567 – 5726GSHGSS → VSGSRR in isoform C. CuratedVSP_017068
Alternative sequencei573 – 66492Missing in isoform C. CuratedVSP_017069Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY995338, AY995336, AY995337 Genomic DNA. Translation: AAY44741.1.
AY995338, AY995336, AY995337 Genomic DNA. Translation: AAY44742.1.
RefSeqiNP_001104727.1. NM_001111257.1. [Q3ZD69-1]
UniGeneiSsc.944.

Genome annotation databases

GeneIDi100126859.
KEGGissc:100126859.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY995338, AY995336, AY995337 Genomic DNA. Translation: AAY44741.1.
AY995338, AY995336, AY995337 Genomic DNA. Translation: AAY44742.1.
RefSeqiNP_001104727.1. NM_001111257.1. [Q3ZD69-1]
UniGeneiSsc.944.

3D structure databases

ProteinModelPortaliQ3ZD69.
SMRiQ3ZD69. Positions 29-65, 313-386, 428-549.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000006923.

Proteomic databases

PaxDbiQ3ZD69.
PRIDEiQ3ZD69.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100126859.
KEGGissc:100126859.

Organism-specific databases

CTDi4000.

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiQ3ZD69.
KOiK12641.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
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.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of the porcine LMNA gene exhibiting developmentally regulated expression."
    Jacobsen M., Horn P., Bendixen C.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiLMNA_PIG
AccessioniPrimary (citable) accession number: Q3ZD69
Secondary accession number(s): Q3ZD68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: September 27, 2005
Last modified: May 11, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.