AC   MF_04016;
DC   Protein; auto
TR   HAMAP; MF_04016; -; 1; level=0
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Names: HSV_MCP
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ID   MCP
DE   RecName: Full=Major capsid protein;
DE            Short=MCP;
GN   Name=MCP;
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CC   -!- FUNCTION: Self-assembles to form an icosahedral capsid with a T=16
CC       symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12
CC       pentons (total of 162 capsomers). Hexons form the edges and faces of
CC       the capsid and are each composed of six MCP molecules. In contrast, one
CC       penton is found at each of the 12 vertices. Eleven of the pentons are
CC       MCP pentamers, while the last vertex is occupied by the portal complex.
CC       The capsid is surrounded by a layer of proteinaceous material
CC       designated the tegument which, in turn, is enclosed in an envelope of
CC       host cell-derived lipids containing virus-encoded glycoproteins.
CC   -!- SUBUNIT: Homomultimer. Makes the hexons and eleven out of twelve
CC       pentons. Interacts with triplex proteins 1/TRX1 and 2/TRX2; adjacent
CC       capsomers are linked together in groups of three by triplexes,
CC       heterotrimeric complexes composed of one molecule of TRX1 and two
CC       molecules of TRX2. Interacts with scaffold protein; this interaction
CC       allows efficient MCP transport to the host nucleus. Interacts with
CC       capsid vertex component 2/CVC2. Interacts with the small capsomere-
CC       interacting protein/SCP.
CC   -!- SUBCELLULAR LOCATION: Virion. Host nucleus.
CC   -!- SIMILARITY: Belongs to the herpesviridae major capsid protein family.
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DR   Pfam; PF03122; Herpes_MCP; 1; trigger=no
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KW   Capsid protein
KW   Host nucleus
KW   Virion
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GO   GO:0042025; C:host cell nucleus
GO   GO:0039622; C:T=16 icosahedral viral capsid
GO   GO:0005198; F:structural molecule activity
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Size: 1330-1413;
Related: None;
Template: P06491;
Scope:
 Viruses; Herpesviridae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.3 2019/11/20
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