CEP2_HHV11
ID CEP2_HHV11 Reviewed; 373 AA.
AC P10200;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 02-JUN-2021, entry version 72.
DE RecName: Full=Cytoplasmic envelopment protein 2 {ECO:0000255|HAMAP-Rule:MF_04039};
GN Name=UL16;
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 CYTOPLASMIC ENVELOPMENT PROTEIN 3.
RC STRAIN=KOS;
RX PubMed=14557627; DOI=10.1128/jvi.77.21.11417-11424.2003;
RA Loomis J.S., Courtney R.J., Wills J.W.;
RT "Binding partners for the UL11 tegument protein of herpes simplex virus
RT type 1.";
RL J. Virol. 77:11417-11424(2003).
RN [3]
RP INTERACTION WITH CAPSID, AND SUBCELLULAR LOCATION.
RC STRAIN=KOS;
RX PubMed=17855514; DOI=10.1128/jvi.01306-07;
RA Meckes D.G. Jr., Wills J.W.;
RT "Dynamic interactions of the UL16 tegument protein with the capsid of
RT herpes simplex virus.";
RL J. Virol. 81:13028-13036(2007).
RN [4]
RP FUNCTION.
RC STRAIN=KOS;
RX PubMed=18715922; DOI=10.1128/jvi.01223-08;
RA Meckes D.G. Jr., Wills J.W.;
RT "Structural rearrangement within an enveloped virus upon binding to the
RT host cell.";
RL J. Virol. 82:10429-10435(2008).
RN [5]
RP INTERACTION WITH CYTOPLASMIC ENVELOPMENT PROTEIN 3, AND MUTAGENESIS OF
RP CYS-221; CYS-244; CYS-247; CYS-269; CYS-271 AND CYS-275.
RC STRAIN=KOS;
RX PubMed=18715918; DOI=10.1128/jvi.01230-08;
RA Yeh P.-C., Meckes D.G. Jr., Wills J.W.;
RT "Analysis of the interaction between the UL11 and UL16 tegument proteins of
RT herpes simplex virus.";
RL J. Virol. 82:10693-10700(2008).
CC -!- FUNCTION: Plays a critical role in cytoplasmic virus egress.
CC Participates in the final step of tegumentation and envelope
CC acquisition within the host cytoplasm by directly interacting with the
CC capsid. Upon virion binding to target cell, a signaling cascade is
CC triggered to disrupt the interaction with the capsid, thereby preparing
CC capsid uncoating. {ECO:0000255|HAMAP-Rule:MF_04039,
CC ECO:0000269|PubMed:18715922}.
CC -!- SUBUNIT: Interacts with cytoplasmic envelopment protein 3 and with the
CC capsid. {ECO:0000255|HAMAP-Rule:MF_04039, ECO:0000269|PubMed:14557627,
CC ECO:0000269|PubMed:17855514, ECO:0000269|PubMed:18715918}.
CC -!- INTERACTION:
CC P10200; P04289: UL11; NbExp=3; IntAct=EBI-7044955, EBI-7044930;
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04039,
CC ECO:0000269|PubMed:17855514}. Host cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_04039, ECO:0000269|PubMed:17855514}. Host nucleus
CC {ECO:0000255|HAMAP-Rule:MF_04039, ECO:0000269|PubMed:17855514}.
CC Note=Localizes in the host nucleus up to 18 hours postinfection, but at
CC later times localizes to punctate, cytoplasmic structures.
CC {ECO:0000255|HAMAP-Rule:MF_04039, ECO:0000269|PubMed:17855514}.
CC -!- SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment
CC protein 2 family. {ECO:0000255|HAMAP-Rule:MF_04039}.
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DR EMBL; X14112; CAA32328.1; -; Genomic_DNA.
DR PIR; G30083; WMBET6.
DR RefSeq; YP_009137090.1; NC_001806.2.
DR IntAct; P10200; 2.
DR MINT; P10200; -.
DR PRIDE; P10200; -.
DR GeneID; 24271465; -.
DR KEGG; vg:24271465; -.
DR Proteomes; UP000009294; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR HAMAP; MF_04039; HSV_CEP2; 1.
DR InterPro; IPR004286; Herpes_UL16/UL94.
DR Pfam; PF03044; Herpes_UL16; 1.
PE 1: Evidence at protein level;
KW Host cytoplasm; Host nucleus; Late protein; Reference proteome; Virion;
KW Virion tegument.
FT CHAIN 1..373
FT /note="Cytoplasmic envelopment protein 2"
FT /id="PRO_0000115949"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 221
FT /note="C->S: No effect on the interaction with UL11."
FT /evidence="ECO:0000269|PubMed:18715918"
FT MUTAGEN 244
FT /note="C->S: No effect on the interaction with UL11."
FT /evidence="ECO:0000269|PubMed:18715918"
FT MUTAGEN 247
FT /note="C->S: Complete loss of interaction with UL11."
FT /evidence="ECO:0000269|PubMed:18715918"
FT MUTAGEN 269
FT /note="C->S: Complete loss of interaction with UL11."
FT /evidence="ECO:0000269|PubMed:18715918"
FT MUTAGEN 271
FT /note="C->S: Complete loss of interaction with UL11."
FT /evidence="ECO:0000269|PubMed:18715918"
FT MUTAGEN 275
FT /note="C->S: Complete loss of interaction with UL11."
FT /evidence="ECO:0000269|PubMed:18715918"
SQ SEQUENCE 373 AA; 40443 MW; 85D9914C533FE34B CRC64;
MAQLGPRRPL APPGPPGTLP RPDSRAGARG TRDRVDDLGT DVDSIARIVN SVFVWRVVRA
DERLKIFRCL TVLTEPLCQV ALPNPDPGRA LFCEIFLYLT RPKALRLPPN TFFALFFFNR
ERRYCAIVHL RSVTHPLTPL LCTLTFARIR AATPPEETPD PTTEQLAEEP VVGELDGAYL
VPAKTPPEPG ACCALGPGAW WHLPSGQIYC WAMDSDLGSL CPPGSRARHL GWLLARITNH
PGGCESCAPP PHIDSANALW LSSVVTESCP CVAPCLWAKM AQCTLAVQGD ASLCPLLFGH
PVDTVTLLQA PRRPCITDRL QEVVGGRCGA DNIPPTSAGW RLCVFSSYIS RLFATSCPTV
ARAVARASSS DPE
