TRX1_HHV11
ID TRX1_HHV11 Reviewed; 465 AA.
AC P32888; P10222;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 02-JUN-2021, entry version 78.
DE RecName: Full=Triplex capsid protein 1 {ECO:0000255|HAMAP-Rule:MF_04018};
GN Name=TRX1 {ECO:0000255|HAMAP-Rule:MF_04018}; OrderedLocusNames=UL38;
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=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 [5]
RP INTERACTION WITH CVC2.
RX PubMed=11152516; DOI=10.1128/jvi.75.3.1427-1436.2001;
RA Ogasawara M., Suzutani T., Yoshida I., Azuma M.;
RT "Role of the UL25 gene product in packaging DNA into the herpes simplex
RT virus capsid: location of UL25 product in the capsid and demonstration that
RT it binds DNA.";
RL J. Virol. 75:1427-1436(2001).
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 FUNCTION.
RX PubMed=16415029; DOI=10.1128/jvi.80.3.1537-1548.2006;
RA Adamson W.E., McNab D., Preston V.G., Rixon F.J.;
RT "Mutational analysis of the herpes simplex virus triplex protein VP19C.";
RL J. Virol. 80:1537-1548(2006).
RN [8]
RP PROTEIN SEQUENCE OF 1-16.
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_04018,
CC ECO:0000269|PubMed:10400780, ECO:0000269|PubMed:16378995,
CC ECO:0000269|PubMed:16415029, ECO:0000269|PubMed:2161052,
CC ECO:0000269|PubMed:8918600}.
CC -!- SUBUNIT: Interacts with TRX2, MCP and capsid vertex component 2/CVC2.
CC {ECO:0000255|HAMAP-Rule:MF_04018, ECO:0000269|PubMed:11152516}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04018}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04018}.
CC -!- SIMILARITY: Belongs to the herpesviridae TRX1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04018}.
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DR EMBL; X14112; CAA32313.1; -; Genomic_DNA.
DR PIR; B30088; WMBEZ8.
DR RefSeq; YP_009137113.1; NC_001806.2.
DR SMR; P32888; -.
DR BioGRID; 971404; 4.
DR DIP; DIP-2193N; -.
DR PRIDE; P32888; -.
DR DNASU; 2703359; -.
DR GeneID; 2703359; -.
DR KEGG; vg:2703359; -.
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:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019069; P:viral capsid assembly; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04018; HSV_TRX1; 1.
DR InterPro; IPR004999; Herpes_1.
DR Pfam; PF03327; Herpes_VP19C; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Direct protein sequencing; Host nucleus;
KW Reference proteome; Virion.
FT CHAIN 1..465
FT /note="Triplex capsid protein 1"
FT /id="PRO_0000436379"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 50263 MW; 5F00147AE29B3092 CRC64;
MKTNPLPATP SVWGGSTVEL PPTTRDTAGQ GLLRRVLRPP ISRRDGPGLP RGSGPRRAAS
TLWLLGLDGT DAPPGALTPN DDTEQALDKI LRGTMRGGAA LIGSPRHHLT RQVILTDLCQ
PNADRAGTLL LALRHPADLP HLAHQRAPPG RQTERLGEAW GQLMEATALG SGRAESGCTR
AGLVSFNFLV AACAASYDAR DAADAVRAHV TANYRGTRVG ARLDRFSECL RAMVHTHVFP
HEVMRFFGGL VSWVTQDELA SVTAVCAGPQ EAAHTGHPGR PRSAVILPAC AFVDLDAELG
LGGPGAAFLY LVFTYRQRRD QELCCVYVIK SQLPPRGLEP ALERLFGRLR ITNTIHGTED
MTPPAPNRNP DFPLAGLAAN PQTPRCSAGQ VTNPQFADRL YRWQPDLRGR PTARTCTYAA
FAELGMMPED SPRCLHRTER FGAVSVPVVI LEGVVWRPGE WRACA
