NEC2_HHV11
ID NEC2_HHV11 Reviewed; 275 AA.
AC P10218;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 02-JUN-2021, entry version 83.
DE RecName: Full=Nuclear egress protein 2 {ECO:0000255|HAMAP-Rule:MF_04024};
GN Name=NEC2 {ECO:0000255|HAMAP-Rule:MF_04024}; OrderedLocusNames=UL34;
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 NEC1.
RX PubMed=11507225; DOI=10.1128/jvi.75.18.8803-8817.2001;
RA Reynolds A.E., Ryckman B.J., Baines J.D., Zhou Y., Liang L., Roller R.J.;
RT "U(L)31 and U(L)34 proteins of herpes simplex virus type 1 form a complex
RT that accumulates at the nuclear rim and is required for envelopment of
RT nucleocapsids.";
RL J. Virol. 75:8803-8817(2001).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=12163613; DOI=10.1128/jvi.76.17.8939-8952.2002;
RA Reynolds A.E., Wills E.G., Roller R.J., Ryckman B.J., Baines J.D.;
RT "Ultrastructural localization of the herpes simplex virus type 1 UL31,
RT UL34, and US3 proteins suggests specific roles in primary envelopment and
RT egress of nucleocapsids.";
RL J. Virol. 76:8939-8952(2002).
RN [4]
RP FUNCTION.
RX PubMed=15140953; DOI=10.1128/jvi.78.11.5564-5575.2004;
RA Reynolds A.E., Liang L., Baines J.D.;
RT "Conformational changes in the nuclear lamina induced by herpes simplex
RT virus type 1 require genes U(L)31 and U(L)34.";
RL J. Virol. 78:5564-5575(2004).
RN [5]
RP FUNCTION.
RX PubMed=12805460; DOI=10.1128/jvi.77.13.7601-7610.2003;
RA Bjerke S.L., Cowan J.M., Kerr J.K., Reynolds A.E., Baines J.D.,
RA Roller R.J.;
RT "Effects of charged cluster mutations on the function of herpes simplex
RT virus type 1 UL34 protein.";
RL J. Virol. 77:7601-7610(2003).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=14671121; DOI=10.1128/jvi.78.1.399-412.2004;
RA Ryckman B.J., Roller R.J.;
RT "Herpes simplex virus type 1 primary envelopment: UL34 protein modification
RT and the US3-UL34 catalytic relationship.";
RL J. Virol. 78:399-412(2004).
RN [7]
RP FUNCTION.
RX PubMed=15140956; DOI=10.1128/jvi.78.11.5591-5600.2004;
RA Simpson-Holley M., Baines J., Roller R., Knipe D.M.;
RT "Herpes simplex virus 1 U(L)31 and U(L)34 gene products promote the late
RT maturation of viral replication compartments to the nuclear periphery.";
RL J. Virol. 78:5591-5600(2004).
RN [8]
RP INTERACTION WITH NEC1.
RX PubMed=15731273; DOI=10.1128/jvi.79.6.3797-3806.2005;
RA Liang L., Baines J.D.;
RT "Identification of an essential domain in the herpes simplex virus 1 UL34
RT protein that is necessary and sufficient to interact with UL31 protein.";
RL J. Virol. 79:3797-3806(2005).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=16415024; DOI=10.1128/jvi.80.3.1476-1486.2006;
RA Kato A., Yamamoto M., Ohno T., Tanaka M., Sata T., Nishiyama Y.,
RA Kawaguchi Y.;
RT "Herpes simplex virus 1-encoded protein kinase UL13 phosphorylates viral
RT Us3 protein kinase and regulates nuclear localization of viral envelopment
RT factors UL34 and UL31.";
RL J. Virol. 80:1476-1486(2006).
RN [10]
RP INTERACTION WITH NEC1.
RX PubMed=17005637; DOI=10.1128/jvi.01662-06;
RA Schnee M., Ruzsics Z., Bubeck A., Koszinowski U.H.;
RT "Common and specific properties of herpesvirus UL34/UL31 protein family
RT members revealed by protein complementation assay.";
RL J. Virol. 80:11658-11666(2006).
RN [11]
RP INTERACTION WITH GLYCOPROTEIN D.
RX PubMed=19279119; DOI=10.1128/jvi.02431-08;
RA Wills E., Mou F., Baines J.D.;
RT "The U(L)31 and U(L)34 gene products of herpes simplex virus 1 are required
RT for optimal localization of viral glycoproteins D and M to the inner
RT nuclear membranes of infected cells.";
RL J. Virol. 83:4800-4809(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 15-185, AND SUBUNIT.
RX PubMed=26511020; DOI=10.15252/embj.201592359;
RA Bigalke J.M., Heldwein E.E.;
RT "Structural basis of membrane budding by the nuclear egress complex of
RT herpesviruses.";
RL EMBO J. 34:2921-2936(2015).
CC -!- FUNCTION: Plays an essential role in virion nuclear egress, the first
CC step of virion release from infected cell. Within the host nucleus,
CC NEC1 interacts with the newly formed capsid through the vertexes and
CC directs it to the inner nuclear membrane by associating with NEC2.
CC Induces the budding of the capsid at the inner nuclear membrane as well
CC as its envelopment into the perinuclear space. There, the NEC1/NEC2
CC complex promotes the fusion of the enveloped capsid with the outer
CC nuclear membrane and the subsequent release of the viral capsid into
CC the cytoplasm where it will reach the secondary budding sites in the
CC host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024,
CC ECO:0000269|PubMed:12805460, ECO:0000269|PubMed:15140953,
CC ECO:0000269|PubMed:15140956}.
CC -!- SUBUNIT: Forms a heterohexameric complex with NEC1. Interacts with
CC glycoprotein D; this interaction recruits glycoprotein D and
CC glycoprotein M to the inner nuclear membrane.
CC {ECO:0000269|PubMed:11507225, ECO:0000269|PubMed:15731273,
CC ECO:0000269|PubMed:17005637, ECO:0000269|PubMed:19279119,
CC ECO:0000269|PubMed:26511020}.
CC -!- INTERACTION:
CC P10218; P02545: LMNA; Xeno; NbExp=2; IntAct=EBI-7183680, EBI-351935;
CC -!- SUBCELLULAR LOCATION: Host nucleus inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_04024, ECO:0000269|PubMed:12163613,
CC ECO:0000269|PubMed:16415024}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:12163613,
CC ECO:0000269|PubMed:16415024}. Note=Localizes also at the transient
CC membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
CC -!- PTM: Phosphorylated by viral kinase US3. {ECO:0000269|PubMed:14671121}.
CC -!- SIMILARITY: Belongs to the herpesviridae NEC2 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04024}.
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DR EMBL; X14112; CAA32309.1; -; Genomic_DNA.
DR PIR; G30085; WMBEH4.
DR RefSeq; YP_009137109.1; NC_001806.2.
DR PDB; 4ZXS; X-ray; 2.77 A; A/C=15-185.
DR PDBsum; 4ZXS; -.
DR SMR; P10218; -.
DR IntAct; P10218; 1.
DR MINT; P10218; -.
DR PRIDE; P10218; -.
DR DNASU; 2703355; -.
DR GeneID; 2703355; -.
DR KEGG; vg:2703355; -.
DR Proteomes; UP000009294; Genome.
DR GO; GO:0044201; C:host cell nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046802; P:exit of virus from host cell nucleus by nuclear egress; IDA:UniProtKB.
DR GO; GO:0046765; P:viral budding from nuclear membrane; IDA:UniProtKB.
DR HAMAP; MF_04024; HSV_NEC2; 1.
DR InterPro; IPR007626; Herpesvirus_viron_egress-type.
DR Pfam; PF04541; Herpes_U34; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host membrane; Host nucleus; Late protein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..275
FT /note="Nuclear egress protein 2"
FT /id="PRO_0000116026"
FT TOPO_DOM 1..251
FT /note="Perinuclear space"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT TOPO_DOM 273..275
FT /note="Nuclear"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT REGION 137..181
FT /note="Interaction with NEC1"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 161..170
FT /evidence="ECO:0007829|PDB:4ZXS"
SQ SEQUENCE 275 AA; 29790 MW; BA45B62F68838EC3 CRC64;
MAGLGKPYTG HPGDAFEGLV QRIRLIVPST LRGGDGEAGP YSPSSLPSRC AFQFHGHDGS
DESFPIEYVL RLMNDWAEVP CNPYLRIQNT GVSVLFQGFF HRPHNAPGGA ITPERTNVIL
GSTETTGLSL GDLDTIKGRL GLDARPMMAS MWISCFVRMP RVQLAFRFMG PEDAGRTRRI
LCRAAEQAIT RRRRTRRSRE AYGAEAGLGV AGTGFRARGD GFGPLPLLTQ GPSRPWHQAL
RGLKHLRIGP PALVLAAGLV LGAAIWWVVG AGARL
