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 24-JAN-2024, entry version 108. 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; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus; OC Simplexvirus humanalpha1; Human herpesvirus 1. 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 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 //