ID   TRX2_HHV11              Reviewed;         318 AA.
AC   P10202;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-JUN-2021, entry version 81.
DE   RecName: Full=Triplex capsid protein 2 {ECO:0000255|HAMAP-Rule:MF_04019};
GN   Name=TRX2 {ECO:0000255|HAMAP-Rule:MF_04019}; OrderedLocusNames=UL18;
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   FUNCTION.
RX   PubMed=2161052; DOI=10.1099/0022-1317-71-5-1211;
RA   Rixon F.J., Davison M.D., Davison A.J.;
RT   "Identification of the genes encoding two capsid proteins of herpes simplex
RT   virus type 1 by direct amino acid sequencing.";
RL   J. Gen. Virol. 71:1211-1214(1990).
RN   [3]
RP   FUNCTION.
RX   PubMed=8918600; DOI=10.1016/s0022-2836(96)80018-0;
RA   Trus B.L., Booy F.P., Newcomb W.W., Brown J.C., Homa F.L., Thomsen D.R.,
RA   Steven A.C.;
RT   "The herpes simplex virus procapsid: structure, conformational changes upon
RT   maturation, and roles of the triplex proteins VP19c and VP23 in assembly.";
RL   J. Mol. Biol. 263:447-462(1996).
RN   [4]
RP   FUNCTION.
RX   PubMed=9811746; DOI=10.1128/jvi.72.12.10066-10072.1998;
RA   Kirkitadze M.D., Barlow P.N., Price N.C., Kelly S.M., Boutell C.J.,
RA   Rixon F.J., McClelland D.A.;
RT   "The herpes simplex virus triplex protein, VP23, exists as a molten
RT   globule.";
RL   J. Virol. 72:10066-10072(1998).
RN   [5]
RP   FUNCTION.
RX   PubMed=10400780; DOI=10.1128/jvi.73.8.6821-6830.1999;
RA   Saad A., Zhou Z.H., Jakana J., Chiu W., Rixon F.J.;
RT   "Roles of triplex and scaffolding proteins in herpes simplex virus type 1
RT   capsid formation suggested by structures of recombinant particles.";
RL   J. Virol. 73:6821-6830(1999).
RN   [6]
RP   FUNCTION.
RX   PubMed=16378995; DOI=10.1128/jvi.80.2.929-940.2006;
RA   Okoye M.E., Sexton G.L., Huang E., McCaffery J.M., Desai P.;
RT   "Functional analysis of the triplex proteins (VP19C and VP23) of herpes
RT   simplex virus type 1.";
RL   J. Virol. 80:929-940(2006).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-13.
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: Structural component of the T=16 icosahedral capsid. The
CC       capsid is composed of pentamers and hexamers of major capsid
CC       protein/MCP, which are linked together by heterotrimers called
CC       triplexes. These triplexes are formed by a single molecule of triplex
CC       protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally,
CC       TRX1 is required for efficient transport of TRX2 to the nucleus, which
CC       is the site of capsid assembly. {ECO:0000255|HAMAP-Rule:MF_04019,
CC       ECO:0000269|PubMed:10400780, ECO:0000269|PubMed:16378995,
CC       ECO:0000269|PubMed:2161052, ECO:0000269|PubMed:8918600,
CC       ECO:0000269|PubMed:9811746}.
CC   -!- SUBUNIT: Interacts with TRX1 and major capisd protein/MCP.
CC       {ECO:0000255|HAMAP-Rule:MF_04019}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04019}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04019}.
CC   -!- SIMILARITY: Belongs to the herpesviridae TRX2 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04019}.
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DR   EMBL; X14112; CAA32331.1; -; Genomic_DNA.
DR   PIR; I30083; WMBET8.
DR   RefSeq; YP_009137092.1; NC_001806.2.
DR   SMR; P10202; -.
DR   BioGRID; 971409; 1.
DR   DIP; DIP-1093N; -.
DR   PRIDE; P10202; -.
DR   DNASU; 2703366; -.
DR   GeneID; 2703366; -.
DR   KEGG; vg:2703366; -.
DR   Proteomes; UP000009294; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IDA:CACAO.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0019069; P:viral capsid assembly; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04019; HSV_TRX2; 1.
DR   InterPro; IPR002690; Herpes_capsid_2.
DR   Pfam; PF01802; Herpes_V23; 1.
PE   1: Evidence at protein level;
KW   Capsid protein; Direct protein sequencing; Host nucleus;
KW   Reference proteome; Virion.
FT   CHAIN           1..318
FT                   /note="Triplex capsid protein 2"
FT                   /id="PRO_0000436336"
SQ   SEQUENCE   318 AA;  34271 MW;  6D9925F5179B5B3A CRC64;
     MLADGFETDI AIPSGISRPD AAALQRCEGR VVFLPTIRRQ LTLADVAHES FVSGGVSPDT
     LGLLLAYRRR FPAVITRVLP TRIVACPLDV GLTHAGTVNL RNTSPVDLCN GDPISLVPPV
     FEGQATDVRL DSLDLTLRFP VPLPSPLARE IVARLVARGI RDLNPSPRNP GGLPDLNVLY
     YNGSRLSLLA DVQQLGPVNA ELRSLVLNMV YSITEGTTII LTLIPRLFAL SAQDGYVNAL
     LQMQSVTREA AQLIHPEAPA LMQDGERRLP LYEALVAWLT HAGQLGDTLA LAPVVRVCTF
     DGAAVVRSGD MAPVIRYP