P11048 (LMNA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lamin-A

Gene names

Name:

lmna

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	665 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Subcellular location	Nucleus.
Miscellaneous	There are at least five different lamins in Xenopus: the somatic lamins L(I), L(II), and A; the oocyte germinal vesicle lamin L(III); and the male germ cells lamin l(IV).
Sequence similarities	Belongs to the intermediate filament family.

Ontologies

Keywords
Cellular component	Intermediate filament Nucleus
Domain	Coiled coil
PTM	Acetylation Lipoprotein Methylation Prenylation
Gene Ontology (GO)
Cellular_component	intermediate filament Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 662	662	Lamin-A		PRO_0000063815
	Propeptide	663 – 665	3	Removed in mature form By similarity		PRO_0000403466
Regions
	Region	1 – 29	29	Head
	Region	30 – 383	354	Rod
	Region	30 – 66	37	Coil 1A
	Region	67 – 76	10	Linker 1
	Region	77 – 214	138	Coil 1B
	Region	215 – 238	24	Linker 2
	Region	239 – 383	145	Coil 2
	Region	384 – 664	281	Tail
	Motif	413 – 418	6	Nuclear localization signal Potential
	Compositional bias	559 – 568	10	Poly-His
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	662	1	Cysteine methyl ester By similarity
	Lipidation	662	1	S-farnesyl cysteine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P11048 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 9FA64F2F1AF99293	FASTA	665	74,919
	10 20 30 40 50 60 METPGQKRAT RSTHTPLSPT RITRLQEKED LQGLNDRLAV YIDKVRSLEL ENARLRLRIT 70 80 90 100 110 120 ESEDVISREV TGIKSAYETE LADARKTLDS VAKERARLQL ELSKIREEHK ELKARNAKKE 130 140 150 160 170 180 SDLLTAQARL KDLEALLNSK DAALTTALGE KRNLENEIRE LKAHIAKLEA SLADTKKQLQ 190 200 210 220 230 240 DEMLRRVDTE NRNQTLKEEL EFQKSIYNEE MRETKRRHET RLVEVDNGRQ REFESKLADA 250 260 270 280 290 300 LHELRAQHEG QIGLYKEELG KTYNAKLENA KQSAERNSSL VGEAQEEIQQ SRIRIDSLSA 310 320 330 340 350 360 QLSQLQKQLA AREAKLRDLE DAYARERDSS RRLLADKDRE MAEMRARMQQ QLDEYQELLD 370 380 390 400 410 420 IKLALDMEIN AYRKLLEGEE ERLRLSPSPN TQKRSARTIA SHSGAHISSS ASKRRRLEEG 430 440 450 460 470 480 ESRSSSFTQH ARTTGKVSVE EVDPEGKYVR LRNKSNEDQS LGNWQIKRQI GDETPIVYKF 490 500 510 520 530 540 PPRLTLKAGQ TVTIWASGAG ATNSPPSDLV WKAQSSWGTG DSIRTALLTS SNEEVAMRKL 550 560 570 580 590 600 VRTVVINDED DEDNDDMEHH HHHHHHHHDG QNSSGDPGEY NLRSRTIVCT SCGRPAEKSV 610 620 630 640 650 660 LASQGSGLVT GSSGSSSSSV TLTRTYRSTG GTSGGSGLGE SPVTRNFIVG NGQRAQVAPQ NCSIM

References

[1]	"A new lamin in Xenopus somatic tissues displays strong homology to human lamin A." Wolin S.L., Krohne G., Kirschner M.W. EMBO J. 6:3809-3818(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The gene structure of Xenopus nuclear lamin A: a model for the evolution of A-type from B-type lamins by exon shuffling." Stick R. Chromosoma 101:566-574(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X06345 mRNA. Translation: CAA29652.1.
PIR	S02358.
RefSeq	NP_001095210.1. NM_001101740.1.
UniGene	Xl.1237.
3D structure databases
ProteinModelPortal	P11048.
SMR	P11048. Positions 25-61, 309-382, 425-546.
ModBase	Search...
Proteomic databases
PRIDE	P11048.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	373673.
KEGG	xla:373673.
Organism-specific databases
CTD	4000.
Xenbase	XB-GENE-920728. lmna.
Phylogenomic databases
HOVERGEN	HBG013015.
KO	K12641.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR001322. Lamin_tail_dom. [Graphical view]
PANTHER	PTHR23239. PTHR23239. 1 hit.
Pfam	PF00038. Filament. 1 hit. PF00932. LTD. 1 hit. [Graphical view]
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LMNA_XENLA

Accession

Primary (citable) accession number: P11048

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program