[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=205947 [NCBI, ExPASy, EBI, Israel, Japan] Reddy V.B., Thimmappaya B., Dhar R., Subramanian K.N., Zain B.S., Pan J., Ghosh P.K., Celma M.L., Weissman S.M.; "The genome of simian virus 40."; Science 200:494-502(1978).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=776; DOI=10.1038/273113a0; PubMed=205802 [NCBI, ExPASy, EBI, Israel, Japan] Fiers W., Contreras R., Haegeman G., Rogiers R., van de Voorde A., van Heuverswyn H., van Herreweghe J., Volckaert G., Ysebaert M.; "Complete nucleotide sequence of SV40 DNA."; Nature 273:113-120(1978).
[3]	NUCLEAR LOCALIZATION SIGNAL. PubMed=8551602 [NCBI, ExPASy, EBI, Israel, Japan] Ishii N., Minami N., Chen E.Y., Medina A.L., Chico M.M., Kasamatsu H.; "Analysis of a nuclear localization signal of simian virus 40 major capsid protein Vp1."; J. Virol. 70:1317-1322(1996).
[4]	PHOSPHORYLATION AT THR-340. PubMed=2464591 [NCBI, ExPASy, EBI, Israel, Japan] Babe L.M., Brew K., Matsuura S.E., Scott W.A.; "Epitopes on the major capsid protein of simian virus 40."; J. Biol. Chem. 264:2665-2671(1989).
[5]	DISULFIDE BONDS IN INTER-PENTAMER. PubMed=10501505 [NCBI, ExPASy, EBI, Israel, Japan] Jao C.C., Weidman M.K., Perez A.R., Gharakhanian E.; "Cys9, Cys104 and Cys207 of simian virus 40 Vp1 are essential for inter-pentamer disulfide-linkage and stabilization in cell-free lysates."; J. Gen. Virol. 80:2481-2489(1999).
[6]	X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS). DOI=10.1038/354278a0; PubMed=1659663 [NCBI, ExPASy, EBI, Israel, Japan] Liddinngton R.C., Yan Y., Moulai J., Sahli R., Benjamin T.L., Harrison S.C.; "Structure of simian virus 40 at 3.8-A resolution."; Nature 354:278-284(1991).
[7]	X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 4-364. DOI=10.1016/S0969-2126(96)00020-2; PubMed=8805523 [NCBI, ExPASy, EBI, Israel, Japan] Stehle T., Gamblin S.J., Yan Y., Harrison S.C.; "The structure of simian virus 40 refined at 3.1-A resolution."; Structure 4:165-182(1996).

Comments

FUNCTION: Forms the icosaedric capsid of the virus protecting the viral genome. This capsid is composed of 360 VP1, assembled in 72 pentamers. Each pentamer are linked via the C-terminal end of VP1.
SUBUNIT: The virus capsid is composed of 75 icosahedral units, each of which is composed of five disulfide-linked copies of VP1.
SUBCELLULAR LOCATION: Virion. Nucleus.

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing and alternative initiation.

Name	VP1
Isoform ID	P03087-1
This is the isoform sequence displayed in this entry.

Name	VP2
Isoform ID	P03093-1
This isoform is stored in UniProtKB/Swiss-Prot entry P03093.

Name	VP3
Isoform ID	P03093-2
Note: Produced by alternative initiation at Met-119 of isoform VP2.
This isoform is stored in UniProtKB/Swiss-Prot entry P03093.

Name	Agno
Isoform ID	P03084-1
Note: Produced by alternative initiation of isoform VP1 and VP2.
This isoform is stored in UniProtKB/Swiss-Prot entry P03084.

DOMAIN: The intrinsically disordered C-terminal region interacts with neighbouring pentamers. The unstructured nature of this region allows to make different interactions depending on the stuctural context: pentamers present at the 12 icosahedral fivefold axes bind five pentamers, when pentamers present at the 60 icosahedral six-fold axes interacts with six pentamers.
SIMILARITY: Belongs to the polyomaviruses coat protein VP1 family.
WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure; URL="http://viperdb.scripps.edu/info_page.php?VDB=1sva";.
WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; Note=SV40 His-VP1*; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_oth_other_780";.

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

J02400; AAB59923.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A31426; A31426.
E03631; VVVP14.

RefSeq

NP_043126.1; -.

3D structure databases

PDB

1SVA; X-ray; 3.10 A; 1/2/3/4/5/6=4-364.	[ExPASy / RCSB / EBI]
3BWQ; X-ray; 2.30 A; A/B/C/D/E=33-300.	[ExPASy / RCSB / EBI]
3BWR; X-ray; 2.25 A; A/B/C/D/E=33-300.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1SVA; -.
3BWQ; -.
3BWR; -.

DisProt

DP00182; -.

ModBase

P03087.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000662; Capsid_VP1_Polyomavir.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.175.10; Polyoma_coat_VP1; 1.

Pfam

PF00718; Polyoma_coat; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF003376; Capsid_VP1_Polyomavir; 1.

ProDom

PD002267; Polyoma_coat_VP1; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Genome annotation databases

GeneID

1489530; -.

Other

LinkHub

P03087; -.

UniRef

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

Keywords

3D-structure; Alternative initiation; Alternative splicing; Capsid protein; Late protein; Nucleus; Phosphoprotein; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 364`	`364`	`Capsid protein VP1.`	`PRO_0000115028`
`REGION`	`304 364`	`61`	`Intrinsically disordered.`
`MOTIF`	`1 19`	`19`	`Bipartite nuclear localization signal.`
`MOD_RES`	`340 340`		`Phosphothreonine.`
`DISULFID`	`12 12`		`Interchain.`
`DISULFID`	`107 107`		`Interchain.`
`DISULFID`	`210 210`		`Interchain.`
`VARIANT`	`101 101`	`1`	`I -> L (in strain: 776).`
`STRAND`	`47 54`	`8`
`HELIX`	`63 65`	`3`
`HELIX`	`85 87`	`3`
`STRAND`	`92 97`	`6`
`STRAND`	`107 122`	`16`
`HELIX`	`125 129`	`5`
`STRAND`	`132 135`	`4`
`STRAND`	`137 139`	`3`
`STRAND`	`151 160`	`10`
`STRAND`	`163 166`	`4`
`HELIX`	`187 190`	`4`
`STRAND`	`197 199`	`3`
`TURN`	`203 205`	`3`
`HELIX`	`208 210`	`3`
`STRAND`	`211 213`	`3`
`STRAND`	`221 228`	`8`
`STRAND`	`236 242`	`7`
`HELIX`	`258 260`	`3`
`STRAND`	`261 275`	`15`
`STRAND`	`280 284`	`5`
`STRAND`	`287 299`	`13`
`STRAND`	`306 308`	`3`
`HELIX`	`326 328`	`3`
`STRAND`	`350 353`	`4`
`STRAND`	`355 361`	`7`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 40166 Da [This is the MW of the unprocessed precursor]

CRC64: F64689D3784557B3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKMAPTKRKG SCPGAAPKKP KEPVQVPKLV IKGGIEVLGV KTGVDSFTEV ECFLNPQMGN 

        70         80         90        100        110        120 
PDEHQKGLSK SLAAEKQFTD DSPDKEQLPC YSVARIPLPN INEDLTCGNI LMWEAVTVKT 

       130        140        150        160        170        180 
EVIGVTAMLN LHSGTQKTHE NGAGKPIQGS NFHFFAVGGE PLELQGVLAN YRTKYPAQTV 

       190        200        210        220        230        240 
TPKNATVDSQ QMNTDHKAVL DKDNAYPVEC WVPDPSKNEN TRYFGTYTGG ENVPPVLHIT 

       250        260        270        280        290        300 
NTATTVLLDE QGVGPLCKAD SLYVSAVDIC GLFTNTSGTQ QWKGLPRYFK ITLRKRSVKN 

       310        320        330        340        350        360 
PYPISFLLSD LINRRTQRVD GQPMIGMSSQ VEEVRVYEDT EELPGDPDMI RYIDEFGQTT 


TRMQ

P03087 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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