ID   SCP_VZVD                Reviewed;         235 AA.
AC   P09279;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-JUN-2021, entry version 69.
DE   RecName: Full=Small capsomere-interacting protein {ECO:0000255|HAMAP-Rule:MF_04020};
GN   Name=SCP {ECO:0000255|HAMAP-Rule:MF_04020}; OrderedLocusNames=23;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18684828; DOI=10.1128/jvi.01890-07;
RA   Chaudhuri V., Sommer M., Rajamani J., Zerboni L., Arvin A.M.;
RT   "Functions of Varicella-zoster virus ORF23 capsid protein in viral
RT   replication and the pathogenesis of skin infection.";
RL   J. Virol. 82:10231-10246(2008).
CC   -!- FUNCTION: Participates in the assembly of the infectious particles by
CC       decorating the outer surface of the capsid shell and thus forming a
CC       layer between the capsid and the tegument. Complexes composed of the
CC       capsid protein VP5 and VP26 assemble together in the host cytoplasm and
CC       are translocated to the nucleus, where they accumulate and participate
CC       in capsid assembly (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:18684828}.
CC   -!- FUNCTION: Participates in the assembly of the infectious particles by
CC       decorating the outer surface of the capsid shell and thus forming a
CC       layer between the capsid and the tegument. Complexes composed of the
CC       major capsid protein and small capsomere-interacting protein/SCP
CC       assemble together in the host cytoplasm and are translocated to the
CC       nucleus, where they accumulate and participate in capsid assembly.
CC       {ECO:0000255|HAMAP-Rule:MF_04020}.
CC   -!- SUBUNIT: Interacts with the major capsid protein/MCP.
CC       {ECO:0000255|HAMAP-Rule:MF_04020}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04020}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04020, ECO:0000269|PubMed:18684828}.
CC   -!- SIMILARITY: Belongs to the herpesviridae small capsomere-interacting
CC       protein family. {ECO:0000255|HAMAP-Rule:MF_04020}.
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DR   EMBL; X04370; CAA27906.1; -; Genomic_DNA.
DR   PIR; E27343; WZBE23.
DR   SMR; P09279; -.
DR   PRIDE; P09279; -.
DR   Proteomes; UP000002602; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04020; HSV_SCP_alphahv; 1.
DR   InterPro; IPR007584; Herpes_UL35.
DR   Pfam; PF04496; Herpes_UL35; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host nucleus; Reference proteome; Virion.
FT   CHAIN           1..235
FT                   /note="Small capsomere-interacting protein"
FT                   /id="PRO_0000115737"
FT   REGION          104..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   235 AA;  24417 MW;  6BC37A7BEE06F30A CRC64;
     MTQPASSRVV FDPSNPTTFS VEAIAAYTPV ALIRLLNASG PLQPGHRVDI ADARSIYTVG
     AAASAARARA NHNANTIRRT AMFAETDPMT WLRPTVGLKR TFNPRIIRPQ PPNPSMSLGI
     SGPTILPQKT QSADQSALQQ PAALAFSGSS PQHPPPQTTS ASVGQQQHVV SGSSGQQPQQ
     GAQSSTVQPT TGSPPAAQGV PQSTPPPTQN TPQGGKGQTL SHTGQSGNAS RSRRV