P10210 (SCAF_HHV11) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 94. History...
Names and origin
|Protein names||Recommended name:|
Capsid scaffolding protein
Capsid protein P40
Virion structural protein UL26
|Organism||Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]|
|Taxonomic identifier||10299 [NCBI]|
|Taxonomic lineage||Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus ›|
|Virus host||Homo sapiens (Human) [TaxID: 9606]|
|Sequence length||635 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein VP5 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as VP5 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein VP5. Cleavages products are evicted from the capsid before or during DNA packaging By similarity.
Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging By similarity.
Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein VP5. Multimerizes in the nucleus such as VP5 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging By similarity.
Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.
Capsid scaffolding protein homomultimerizes and interacts with major capsid protein VP5. Assemblin exists in a monomer-dimer equilibrium with the dimer being the active species. Assembly protein homomultimerizes and interacts with major capsid protein VP5 By similarity.
Region of interaction between pPR and pAP is called Amino conserved domain (ACD). The region of interaction with major capsid protein is called carboxyl conserved domain (CCD) By similarity.
Capsid scaffolding protein is cleaved by assemblin after completion of icosahedral capsid formation. Cleavages occur at two or more sites: release and tail site By similarity.
Assembly protein is phosphorylated.
Belongs to the herpesviridae capsid scaffolding protein family.
|Biological process||Viral capsid assembly|
Virus exit from host cell
|Cellular component||Host cytoplasm|
|Coding sequence diversity||Alternative promoter usage|
|Technical term||Complete proteome|
Direct protein sequencing
|Gene Ontology (GO)|
Inferred from electronic annotation. Source: UniProtKB-KWviral release from host cell
Inferred from electronic annotation. Source: UniProtKB-KW
|Cellular_component||host cell cytoplasm|
Inferred from electronic annotation. Source: UniProtKB-SubCellhost cell nucleus
Inferred from electronic annotation. Source: UniProtKB-SubCell
|Molecular_function||serine-type endopeptidase activity|
Inferred from electronic annotation. Source: InterPro
|Complete GO annotation...|
|This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]|
|Isoform Capsid scaffolding protein (identifier: P10210-1) |
Also known as: pPR; UL26;
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.
|Isoform pAP (identifier: P10210-2) |
Also known as: Assembly protein; UL26.5 protein;
The sequence of this isoform differs from the canonical sequence as follows:
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 635||635||Capsid scaffolding protein||PRO_0000027244|
|Chain||1 – 247||247||Assemblin||PRO_0000027245|
|Chain||248 – 635||388||Assembly protein||PRO_0000027246|
|Region||324 – 343||20||Interaction with pAP|
|Region||618 – 635||18||Interaction with major capsid protein|
|Motif||426 – 429||4||Nuclear localization signal Potential|
|Compositional bias||514 – 590||77||Pro-rich|
|Active site||61||1||Charge relay system By similarity|
|Active site||129||1||Charge relay system By similarity|
|Active site||148||1||Charge relay system By similarity|
|Site||247 – 248||2||Cleavage; by assemblin; Release site By similarity|
|Site||610 – 611||2||Cleavage; by assemblin; Tail site By similarity|
|Alternative sequence||1 – 306||306||Missing in isoform pAP.||VSP_037414|
|||"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].
|||"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 11-29; 77-91 AND 223-241.
|+||Additional computationally mapped references.|
|X14112 Genomic DNA. Translation: CAA32318.1.|
X14112 Genomic DNA. Translation: CAA32319.1.
|PIR||WMBEW6. H30084. |
|RefSeq||NP_044627.1. NC_001806.1. |
3D structure databases
|SMR||P10210. Positions 17-247. |
Protein-protein interaction databases
|IntAct||P10210. 1 interaction.|
Protein family/group databases
Protocols and materials databases
Genome annotation databases
Family and domain databases
|Gene3D||22.214.171.124. 1 hit. |
|InterPro||IPR001847. Peptidase_S21. |
|Pfam||PF00716. Peptidase_S21. 1 hit. |
|PRINTS||PR00236. HSVCAPSIDP40. |
|SUPFAM||SSF50789. SSF50789. 1 hit. |
|Accession||Primary (citable) accession number: P10210|
Secondary accession number(s): O09798
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families