ID   SCP_HHV11               Reviewed;         112 AA.
AC   P10219;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-JUN-2021, entry version 84.
DE   RecName: Full=Small capsomere-interacting protein {ECO:0000255|HAMAP-Rule:MF_04020};
GN   Name=SCP {ECO:0000255|HAMAP-Rule:MF_04020}; OrderedLocusNames=UL35;
OS   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA   Perry L.J., Scott J.E., Taylor P.;
RT   "The complete DNA sequence of the long unique region in the genome of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:1531-1574(1988).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8811025; DOI=10.1099/0022-1317-77-9-2251;
RA   Rixon F.J., Addison C., McGregor A., Macnab S.J., Nicholson P.,
RA   Preston V.G., Tatman J.D.;
RT   "Multiple interactions control the intracellular localization of the herpes
RT   simplex virus type 1 capsid proteins.";
RL   J. Gen. Virol. 77:2251-2260(1996).
RN   [3]
RP   INTERACTION WITH MCP.
RC   STRAIN=KOS;
RX   PubMed=12477844; DOI=10.1128/jvi.77.1.391-404.2003;
RA   Desai P., Akpa J.C., Person S.;
RT   "Residues of VP26 of herpes simplex virus type 1 that are required for its
RT   interaction with capsids.";
RL   J. Virol. 77:391-404(2003).
RN   [4]
RP   INTERACTION WITH HOST MAPRE3 AND DYNLT1, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15117959; DOI=10.1074/jbc.m311671200;
RA   Douglas M.W., Diefenbach R.J., Homa F.L., Miranda-Saksena M., Rixon F.J.,
RA   Vittone V., Byth K., Cunningham A.L.;
RT   "Herpes simplex virus type 1 capsid protein VP26 interacts with dynein
RT   light chains RP3 and Tctex1 and plays a role in retrograde cellular
RT   transport.";
RL   J. Biol. Chem. 279:28522-28530(2004).
RN   [5]
RP   INTERACTION WITH HOST TSPAN7.
RX   PubMed=20630051; DOI=10.1186/1743-422x-7-156;
RA   Wang L., Liu L., Che Y., Wang L., Jiang L., Dong C., Zhang Y., Li Q.;
RT   "Egress of HSV-1 capsid requires the interaction of VP26 and a cellular
RT   tetraspanin membrane protein.";
RL   Virol. J. 7:156-156(2010).
RN   [6]
RP   PROTEIN SEQUENCE OF 23-33 AND 37-47.
RX   PubMed=1328483; DOI=10.1099/0022-1317-73-10-2709;
RA   Davison M.D., Rixon F.J., Davison A.J.;
RT   "Identification of genes encoding two capsid proteins (VP24 and VP26) of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 73:2709-2713(1992).
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 (By
CC       similarity). Interaction with host dynein light chains suggests a
CC       possible function in the retrogarde transport of incoming viral
CC       capsids. {ECO:0000255|HAMAP-Rule:MF_04020,
CC       ECO:0000269|PubMed:15117959}.
CC   -!- SUBUNIT: Interacts with the major capsid protein/MCP. Interacts with
CC       host TSPAN7; this interaction may be responsible for the presence of
CC       TSPAN7 in extracellular virions. Interacts with host MAPRE3 and DYNLT1;
CC       these interactions mediate retrograde transport of viral capsids.
CC       {ECO:0000255|HAMAP-Rule:MF_04020, ECO:0000269|PubMed:12477844,
CC       ECO:0000269|PubMed:20630051}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04020}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04020, ECO:0000269|PubMed:15117959,
CC       ECO:0000269|PubMed:8811025}.
CC   -!- SIMILARITY: Belongs to the herpesviridae small capsomere-interacting
CC       protein family. {ECO:0000255|HAMAP-Rule:MF_04020}.
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DR   EMBL; X14112; CAA32310.1; -; Genomic_DNA.
DR   PIR; H30085; WMBEH5.
DR   RefSeq; YP_009137110.1; NC_001806.2.
DR   SMR; P10219; -.
DR   IntAct; P10219; 1.
DR   MINT; P10219; -.
DR   PRIDE; P10219; -.
DR   DNASU; 2703356; -.
DR   GeneID; 2703356; -.
DR   KEGG; vg:2703356; -.
DR   Proteomes; UP000009294; 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   1: Evidence at protein level;
KW   Capsid protein; Direct protein sequencing; Host nucleus;
KW   Host-virus interaction; Reference proteome; Virion.
FT   CHAIN           1..112
FT                   /note="Small capsomere-interacting protein"
FT                   /id="PRO_0000115734"
SQ   SEQUENCE   112 AA;  12096 MW;  ACC56F7EA0BA7384 CRC64;
     MAVPQFHRPS TVTTDSVRAL GMRGLVLATN NSQFIMDNNH PHPQGTQGAV REFLRGQAAA
     LTDLGLAHAN NTFTPQPMFA GDAPAAWLRP AFGLRRTYSP FVVREPSTPG TP