[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). PubMed=2249665 [NCBI, ExPASy, EBI, Israel, Japan] Doering V., Stick R.; "Gene structure of nuclear lamin LIII of Xenopus laevis; a model for the evolution of IF proteins from a lamin-like ancestor."; EMBO J. 9:4073-4081(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Ovary; PubMed=3181134 [NCBI, ExPASy, EBI, Israel, Japan] Stick R.; "cDNA cloning of the developmentally regulated lamin LIII of Xenopus laevis."; EMBO J. 7:3189-3197(1988).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Embryo; NIH - Xenopus Gene Collection (XGC) project; Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.

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 inner membrane; Lipid-anchor; Nucleoplasmic side.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	B3A
Isoform ID	P10999-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	B3B
Isoform ID	P10999-2
Features which should be applied to build the isoform sequence: VSP_002473.

DEVELOPMENTAL STAGE: Expressed in oocytes.
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).
SIMILARITY: Belongs to the intermediate filament family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X13169; CAA31567.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC078034; AAH78034.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S01301; S01301.

NP_001081545.1; -.

3D structure databases

HSSP

P02545; 1IVT. [HSSP ENTRY / PDB]

ModBase

P10999.

Organism-specific databases

Xenbase

XB-FEAT-920612; lmnb3.

Ontologies

GO:0005882;	Cellular component: intermediate filament (inferred from electronic annotation from UniProtKB-KW).
GO:0005637;	Cellular component: nuclear inner membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005198;	Molecular function: structural molecule activity (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR016044; F.
IPR001664; IF.
IPR001322; IF_tail_C.
IPR018039; Intermediate_filament_CS.
Graphical view of domain structure.

PANTHER

PTHR23239; IF; 1.

Pfam

PF00038; Filament; 1.
PF00932; IF_tail; 1.
Pfam graphical view of domain structure.

PROSITE

PS00226; IF; 1.

Genome annotation databases

GeneID

397910; -.

KEGG

xla:397910; -.

Phylogenomic databases

HOVERGEN

P10999; -.

Other

ProtoNet

P10999.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Coiled coil; Intermediate filament; Lipoprotein; Membrane; Nucleus; Phosphoprotein; Prenylation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 583`	`583`	`Lamin-L(III).`	`PRO_0000063825`
`REGION`	`1 32`	`32`	`Head.`
`REGION`	`33 384`	`352`	`Rod.`
`REGION`	`33 67`	`35`	`Coil 1A.`
`REGION`	`68 79`	`12`	`Linker 1.`
`REGION`	`80 215`	`136`	`Coil 1B.`
`REGION`	`216 242`	`27`	`Linker 2.`
`REGION`	`243 384`	`142`	`Coil 2.`
`REGION`	`385 583`	`199`	`Tail.`
`COMPBIAS`	`550 565`	`16`	`Asp/Glu-rich (highly acidic; could be involved in chromatin binding).`
`LIPID`	`580 580`		`S-farnesyl cysteine (By similarity).`
`VAR_SEQ`	`572 583`		`SHQSVDPSCSIM -> TKRRKKKCCSVS (in isoform 2).`	`VSP_002473`
`CONFLICT`	`349 349`		`Q -> H (in Ref. 2; CAA31567).`

Sequence information

Length: 583 AA [This is the length of the unprocessed precursor]

Molecular weight: 67291 Da [This is the MW of the unprocessed precursor]

CRC64: 6BDBD1CF25ACEE92 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATSTPSRAR EHASAAQSPG SPTRISRMQE KEDLRHLNDR LAAYIERVRS LEADKSLLKI 

        70         80         90        100        110        120 
QLEEREEVSS REVTNLRQLY ETELADARKL LDQTANERAR LQVELGKVRE EYRQLQARNS 

       130        140        150        160        170        180 
KKENDLSLAQ NQLRDLESKL NTKEAELATA LSGKRGLEEQ LQEQRAQIAG LESSLRDTTK 

       190        200        210        220        230        240 
QLHDEMLWRV DLENKMQTIR EQLDFQKNIH TQEVKEIKKR HDTRIVEIDS GRRVEFESKL 

       250        260        270        280        290        300 
AEALQELRRD HEQQILEYKE HLEKNFSAKL ENAQLAAAKN SDYASATREE IMATKLRVDT 

       310        320        330        340        350        360 
LSSQLNHYQK QNSALEAKVR DLQDMLDRAH DMHRRQMTEK DREVTEIRQT LQGQLEEYEQ 

       370        380        390        400        410        420 
LLDVKLALDM EINAYRKMLE GEEQRLKLSP SPSQRSTVSR ASTSQTSRLL RGKKRKLDET 

       430        440        450        460        470        480 
GRSVTKRSYK VVQQASSTGP VSVEDIDPEG NYVRLLNNTE EDFSLHGWVV KRMHMSLPEI 

       490        500        510        520        530        540 
AFKLPCRFIL KSSQRVTIWA AGAGAVHSPP TDLVWKSQKT WGTGDNIKIT LLDSTGEECA 

       550        560        570        580 
ERTLYRVIGE EGETDEDFVE EEELERQFRS QSHQSVDPSC SIM

P10999 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools