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Protein

Triplex capsid protein VP23

Gene

UL18

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of VP5, which are linked together by heterotrimers called triplex. These triplex are formed by a single molecule of VP19C and two copies of VP23 which bridge major capsid protein VP5 multimers together. Triplexes occupy the local threeflod positions between capsid hexamers and pentamers. Additionally, VP19C is required for efficient transport of VP23 to the nucleus, which is the site of capsid assembly.5 Publications

GO - Molecular functioni

  1. structural molecule activity Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Triplex capsid protein VP23
Gene namesi
Name:UL18
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000009294: Genome

Subcellular locationi

GO - Cellular componenti

  1. host cell nucleus Source: UniProtKB-SubCell
  2. viral capsid Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Triplex capsid protein VP23PRO_0000115725Add
BLAST

Interactioni

Subunit structurei

Interacts with VP19C and VP5.

Protein-protein interaction databases

DIPiDIP-1093N.

Family & Domainsi

Sequence similaritiesi

Belongs to the herpesviridae VP23 family.Curated

Family and domain databases

InterProiIPR002690. Herpes_V23.
[Graphical view]
PfamiPF01802. Herpes_V23. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10202-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLADGFETDI AIPSGISRPD AAALQRCEGR VVFLPTIRRQ LTLADVAHES
60 70 80 90 100
FVSGGVSPDT LGLLLAYRRR FPAVITRVLP TRIVACPLDV GLTHAGTVNL
110 120 130 140 150
RNTSPVDLCN GDPISLVPPV FEGQATDVRL DSLDLTLRFP VPLPSPLARE
160 170 180 190 200
IVARLVARGI RDLNPSPRNP GGLPDLNVLY YNGSRLSLLA DVQQLGPVNA
210 220 230 240 250
ELRSLVLNMV YSITEGTTII LTLIPRLFAL SAQDGYVNAL LQMQSVTREA
260 270 280 290 300
AQLIHPEAPA LMQDGERRLP LYEALVAWLT HAGQLGDTLA LAPVVRVCTF
310
DGAAVVRSGD MAPVIRYP
Length:318
Mass (Da):34,271
Last modified:July 1, 1989 - v1
Checksum:i6D9925F5179B5B3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32331.1.
PIRiI30083. WMBET8.
RefSeqiNP_044619.1. NC_001806.1.

Genome annotation databases

GeneIDi2703366.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32331.1.
PIRiI30083. WMBET8.
RefSeqiNP_044619.1. NC_001806.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-1093N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703366.

Family and domain databases

InterProiIPR002690. Herpes_V23.
[Graphical view]
PfamiPF01802. Herpes_V23. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
    McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
    J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification of the genes encoding two capsid proteins of herpes simplex virus type 1 by direct amino acid sequencing."
    Rixon F.J., Davison M.D., Davison A.J.
    J. Gen. Virol. 71:1211-1214(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly."
    Trus B.L., Booy F.P., Newcomb W.W., Brown J.C., Homa F.L., Thomsen D.R., Steven A.C.
    J. Mol. Biol. 263:447-462(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "The herpes simplex virus triplex protein, VP23, exists as a molten globule."
    Kirkitadze M.D., Barlow P.N., Price N.C., Kelly S.M., Boutell C.J., Rixon F.J., McClelland D.A.
    J. Virol. 72:10066-10072(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Roles of triplex and scaffolding proteins in herpes simplex virus type 1 capsid formation suggested by structures of recombinant particles."
    Saad A., Zhou Z.H., Jakana J., Chiu W., Rixon F.J.
    J. Virol. 73:6821-6830(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Functional analysis of the triplex proteins (VP19C and VP23) of herpes simplex virus type 1."
    Okoye M.E., Sexton G.L., Huang E., McCaffery J.M., Desai P.
    J. Virol. 80:929-940(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Identification of genes encoding two capsid proteins (VP24 and VP26) of herpes simplex virus type 1."
    Davison M.D., Rixon F.J., Davison A.J.
    J. Gen. Virol. 73:2709-2713(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-13.

Entry informationi

Entry nameiVP23_HHV11
AccessioniPrimary (citable) accession number: P10202
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 7, 2015
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.