CVC2_HHV11
ID CVC2_HHV11 Reviewed; 580 AA.
AC P10209;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 02-JUN-2021, entry version 105.
DE RecName: Full=Capsid vertex component 2 {ECO:0000255|HAMAP-Rule:MF_04025};
GN Name=CVC2 {ECO:0000255|HAMAP-Rule:MF_04025}; OrderedLocusNames=UL25;
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 INTERACTION WITH VP5 AND VP19C.
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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=16775316; DOI=10.1128/jvi.02648-05;
RA Newcomb W.W., Homa F.L., Brown J.C.;
RT "Herpes simplex virus capsid structure: DNA packaging protein UL25 is
RT located on the external surface of the capsid near the vertices.";
RL J. Virol. 80:6286-6294(2006).
RN [4]
RP INTERACTION WITH UL17.
RX PubMed=17531807; DOI=10.1016/j.molcel.2007.04.010;
RA Trus B.L., Newcomb W.W., Cheng N., Cardone G., Marekov L., Homa F.L.,
RA Brown J.C., Steven A.C.;
RT "Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17
RT heterodimers to DNA-Filled HSV-1 capsids.";
RL Mol. Cell 26:479-489(2007).
RN [5]
RP INTERACTION WITH UL36.
RX PubMed=17715218; DOI=10.1128/jvi.01113-07;
RA Coller K.E., Lee J.I., Ueda A., Smith G.A.;
RT "The capsid and tegument of the alphaherpesviruses are linked by an
RT interaction between the UL25 and VP1/2 proteins.";
RL J. Virol. 81:11790-11797(2007).
RN [6]
RP FUNCTION.
RX PubMed=18448531; DOI=10.1128/jvi.00257-08;
RA Preston V.G., Murray J., Preston C.M., McDougall I.M., Stow N.D.;
RT "The UL25 gene product of herpes simplex virus type 1 is involved in
RT uncoating of the viral genome.";
RL J. Virol. 82:6654-6666(2008).
RN [7]
RP FUNCTION.
RX PubMed=18945788; DOI=10.1128/jvi.01889-08;
RA Cockrell S.K., Sanchez M.E., Erazo A., Homa F.L.;
RT "Role of the UL25 protein in herpes simplex virus DNA encapsidation.";
RL J. Virol. 83:47-57(2009).
RN [8]
RP INTERACTION WITH HUMAN NUP214.
RX PubMed=19386703; DOI=10.1128/jvi.02655-08;
RA Pasdeloup D., Blondel D., Isidro A.L., Rixon F.J.;
RT "Herpesvirus capsid association with the nuclear pore complex and viral DNA
RT release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25.";
RL J. Virol. 83:6610-6623(2009).
RN [9]
RP INTERACTION WITH HUMAN TMEM250.
RX PubMed=21667337; DOI=10.1007/s12250-011-3179-8;
RA Zhang Y., Li Y.M., Liu L.D., Jiang L., Ji M., Jiang R.J., Guo L., Liao Y.,
RA Li Q.H.;
RT "Host cell protein C9orf69 promotes viral proliferation via interaction
RT with HSV-1 UL25 protein.";
RL Zhongguo Bing Du Xue 26:171-180(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-580.
RX PubMed=16474137; DOI=10.1128/jvi.80.5.2309-2317.2006;
RA Bowman B.R., Welschhans R.L., Jayaram H., Stow N.D., Preston V.G.,
RA Quiocho F.A.;
RT "Structural characterization of the UL25 DNA-packaging protein from herpes
RT simplex virus type 1.";
RL J. Virol. 80:2309-2317(2006).
CC -!- FUNCTION: Capsid vertex-specific component that plays a role during
CC viral DNA encapsidation, assuring correct genome cleavage and
CC presumably stabilizing capsids that contain full-length viral genomes.
CC Participates in the interaction between the capsid and the tegument
CC through interaction with the large tegument protein/LTP. May mediate
CC the capsid docking to the nuclear pore allowing entry of the viral
CC genome into the host nucleus through binding to host nucleoporins
CC NUP214. {ECO:0000255|HAMAP-Rule:MF_04025, ECO:0000269|PubMed:18448531,
CC ECO:0000269|PubMed:18945788}.
CC -!- SUBUNIT: Heterodimerizes with CVC1. Interacts with major capsid
CC protein/MCP and triplex capsid protein 1/TRX1 at the pentamer vertices.
CC Interacts with the large tegument protein/LTP. Interacts with host
CC NUP214; this interaction might be essential to the capsid docking to
CC the host nuclear pore. Interacts with host TMEM250. {ECO:0000255|HAMAP-
CC Rule:MF_04025, ECO:0000269|PubMed:11152516,
CC ECO:0000269|PubMed:17531807, ECO:0000269|PubMed:17715218,
CC ECO:0000269|PubMed:19386703, ECO:0000269|PubMed:21667337}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04025,
CC ECO:0000269|PubMed:16775316}. Host nucleus {ECO:0000255|HAMAP-
CC Rule:MF_04025, ECO:0000269|PubMed:16775316}.
CC -!- SIMILARITY: Belongs to the herpesviridae CVC2 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04025}.
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; X14112; CAA32317.1; -; Genomic_DNA.
DR PIR; G30084; WMBEW5.
DR RefSeq; YP_009137099.1; NC_001806.2.
DR PDB; 2F5U; X-ray; 2.10 A; A=134-580.
DR PDBsum; 2F5U; -.
DR SMR; P10209; -.
DR BioGRID; 971417; 1.
DR DIP; DIP-60387N; -.
DR IntAct; P10209; 9.
DR PRIDE; P10209; -.
DR DNASU; 2703377; -.
DR GeneID; 2703377; -.
DR KEGG; vg:2703377; -.
DR EvolutionaryTrace; P10209; -.
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:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0019072; P:viral genome packaging; IEA:UniProtKB-UniRule.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04025; HSV_CVC2; 1.
DR InterPro; IPR002493; Herpes_UL25.
DR Pfam; PF01499; Herpes_UL25; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host nucleus; Host-virus interaction;
KW Reference proteome; Viral genome packaging;
KW Viral penetration into host nucleus; Viral release from host cell; Virion;
KW Virus entry into host cell.
FT CHAIN 1..580
FT /note="Capsid vertex component 2"
FT /id="PRO_0000115993"
FT REGION 1..50
FT /note="Interaction with major capsid protein/MCP"
FT REGION 1..49
FT /note="Interaction with major capsid protein/MCP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04025"
FT REGION 108..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2F5U"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2F5U"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 231..246
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:2F5U"
FT TURN 308..313
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 351..360
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 372..392
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 438..446
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 448..454
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 465..474
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 496..508
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 517..540
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 550..554
FT /evidence="ECO:0007829|PDB:2F5U"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:2F5U"
FT HELIX 561..570
FT /evidence="ECO:0007829|PDB:2F5U"
SQ SEQUENCE 580 AA; 62670 MW; 3F8F0B7C122B2E36 CRC64;
MDPYCPFDAL DVWEHRRFIV ADSRNFITPE FPRDFWMSPV FNLPRETAAE QVVVLQAQRT
AAAAALENAA MQAAELPVDI ERRLRPIERN VHEIAGALEA LETAAAAAEE ADAARGDEPA
GGGDGGAPPG LAVAEMEVQI VRNDPPLRYD TNLPVDLLHM VYAGRGATGS SGVVFGTWYR
TIQDRTITDF PLTTRSADFR DGRMSKTFMT ALVLSLQACG RLYVGQRHYS AFECAVLCLY
LLYRNTHGAA DDSDRAPVTF GDLLGRLPRY LACLAAVIGT EGGRPQYRYR DDKLPKTQFA
AGGGRYEHGA LASHIVIATL MHHGVLPAAP GDVPRDASTH VNPDGVAHHD DINRAAAAFL
SRGHNLFLWE DQTLLRATAN TITALGVIQR LLANGNVYAD RLNNRLQLGM LIPGAVPSEA
IARGASGSDS GAIKSGDNNL EALCANYVLP LYRADPAVEL TQLFPGLAAL CLDAQAGRPV
GSTRRVVDMS SGARQAALVR LTALELINRT RTNPTPVGEV IHAHDALAIQ YEQGLGLLAQ
QARIGLGSNT KRFSAFNVSS DYDMLYFLCL GFIPQYLSAV
