ID   TRX1_VZVD               Reviewed;         483 AA.
AC   P09276;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   07-APR-2021, entry version 70.
DE   RecName: Full=Triplex capsid protein 1 {ECO:0000255|HAMAP-Rule:MF_04018};
GN   Name=TRX1 {ECO:0000255|HAMAP-Rule:MF_04018}; OrderedLocusNames=20;
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, INTERACTION WITH HOST ZBP1 AND RIPK3, AND MUTAGENESIS OF
RP   31-ILE--GLY-34.
RX   PubMed=32649716; DOI=10.1371/journal.ppat.1008473;
RA   Steain M., Baker M.O.D.G., Pham C.L.L., Shanmugam N., Gambin Y.,
RA   Sierecki E., McSharry B.P., Avdic S., Slobedman B., Sunde M., Abendroth A.;
RT   "Varicella zoster virus encodes a viral decoy RHIM to inhibit cell death.";
RL   PLoS Pathog. 16:e1008473-e1008473(2020).
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 (By similarity). Prevents also
CC       necroptosis and extrinsic apoptosis by sequestering host ZBP1 into
CC       large, insoluble supercomplexes and impairing its ability to interact
CC       with RIPK3 (PubMed:32649716). {ECO:0000255|HAMAP-Rule:MF_04018,
CC       ECO:0000269|PubMed:32649716}.
CC   -!- SUBUNIT: Interacts with TRX2, MCP and capsid vertex component 2/CVC2
CC       (By similarity). Self-assembles into homo-oligomeric amyloid fibrils
CC       (PubMed:32649716). Interacts with host ZBP1; this interaction prevents
CC       host necroptosis and extrinsic apoptosis (PubMed:32649716). Interacts
CC       with host RIPK3 (PubMed:32649716). {ECO:0000255|HAMAP-Rule:MF_04018,
CC       ECO:0000269|PubMed:32649716}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X04370; CAA27903.1; -; Genomic_DNA.
DR   PIR; B27343; WZBE20.
DR   SMR; P09276; -.
DR   PRIDE; P09276; -.
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:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0039650; P:suppression by virus of host cysteine-type endopeptidase activity involved in apoptotic process; IEA:UniProtKB-KW.
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; Host nucleus; Host-virus interaction;
KW   Inhibition of host caspases by virus;
KW   Modulation of host cell apoptosis by virus; Reference proteome; Virion.
FT   CHAIN           1..483
FT                   /note="Triplex capsid protein 1"
FT                   /id="PRO_0000115721"
FT   MOTIF           24..40
FT                   /note="RIP homotypic interaction motif (RHIM)"
FT                   /evidence="ECO:0000269|PubMed:32649716"
FT   MUTAGEN         31..34
FT                   /note="IQIG->AAAA: Loss of ability to form a regular,
FT                   extended fibrillar structure."
FT                   /evidence="ECO:0000269|PubMed:32649716"
SQ   SEQUENCE   483 AA;  53971 MW;  A584CF73D689BF91 CRC64;
     MGSQPTNSHF TLNEQTLCGT NISLLGNNRF IQIGNGLHMT YAPGFFGNWS RDLTIGPRFG
     GLNKQPIHVP PKRTETASIQ VTPRSIVINR MNNIQINPTS IGNPQVTIRL PLNNFKSTTQ
     LIQQVSLTDF FRPDIEHAGS IVLILRHPSD MIGEANTLTQ AGRDPDVLLE GLRNLFNACT
     APWTVGEGGG LRAYVTSLSF IAACRAEEYT DKQAADANRT AIVSAYGCSR METRLIRFSE
     CLRAMVQCHV FPHRFISFFG SLLEYTIQDN LCNITAVAKG PQEAARTDKT STRRVTANIP
     ACVFWDVDKD LHLSADGLKH VFLVFVYTQR RQREGVRLHL ALSQLNEQCF GRGIGFLLGR
     IRAENAAWGT EGVANTHQPY NTRALPLVQL SNDPTSPRCS IGEITGVNWN LARQRLYQWT
     GDFRGLPTQL SCMYAAYTLI GTIPSESVRY TRRMERFGGY NVPTIWLEGV VWGGTNTWNE
     CYY