NEC1_HHV11
ID NEC1_HHV11 Reviewed; 306 AA.
AC P10215;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 02-JUN-2021, entry version 82.
DE RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; OrderedLocusNames=UL31;
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 NEC2.
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=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 [6]
RP INTERACTION WITH NEC2.
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 [7]
RP INTERACTION WITH NEC2.
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 [8]
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 [9]
RP PHOSPHORYLATION.
RX PubMed=19279109; DOI=10.1128/jvi.00090-09;
RA Mou F., Wills E., Baines J.D.;
RT "Phosphorylation of the UL31 protein of herpes simplex virus 1 by the US3-
RT encoded kinase regulates localization of the nuclear envelopment complex
RT and egress of nucleocapsids.";
RL J. Virol. 83:5181-5191(2009).
RN [10]
RP INTERACTION WITH NEC2.
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 [11]
RP FUNCTION, AND INTERACTION WITH CVC2.
RX PubMed=24453362; DOI=10.1128/jvi.03175-13;
RA Yang K., Wills E., Lim H.Y., Zhou Z.H., Baines J.D.;
RT "Association of herpes simplex virus pUL31 with capsid vertices and
RT components of the capsid vertex-specific complex.";
RL J. Virol. 88:3815-3825(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 51-306, 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_04023,
CC ECO:0000269|PubMed:15140953, ECO:0000269|PubMed:15140956,
CC ECO:0000269|PubMed:24453362}.
CC -!- SUBUNIT: Forms a heterohexameric complex with NEC2. Interacts with
CC capsid vertex specific component 2/CVC2; this interaction directs the
CC capsid to the host inner nuclear membrane to initiate budding.
CC {ECO:0000255|HAMAP-Rule:MF_04023, ECO:0000269|PubMed:11507225,
CC ECO:0000269|PubMed:15731273, ECO:0000269|PubMed:17005637,
CC ECO:0000269|PubMed:19279119, ECO:0000269|PubMed:26511020}.
CC -!- INTERACTION:
CC P10215; P02545: LMNA; Xeno; NbExp=2; IntAct=EBI-7183650, EBI-351935;
CC -!- SUBCELLULAR LOCATION: Host nucleus inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_04023, ECO:0000269|PubMed:12163613,
CC ECO:0000269|PubMed:16415024}. Note=Remains attached to the nucleus
CC inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-
CC Rule:MF_04023}.
CC -!- PTM: Phosphorylated at serine residues in the N-terminus. This
CC phosphorylation regulates the localization within the inner nuclear
CC membrane. {ECO:0000255|HAMAP-Rule:MF_04023,
CC ECO:0000269|PubMed:19279109}.
CC -!- SIMILARITY: Belongs to the herpesviridae NEC1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04023}.
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DR EMBL; X14112; CAA32324.1; -; Genomic_DNA.
DR PIR; D30085; WMBEH1.
DR RefSeq; YP_009137106.1; NC_001806.2.
DR PDB; 4ZXS; X-ray; 2.77 A; B/D=51-306.
DR PDBsum; 4ZXS; -.
DR SMR; P10215; -.
DR BioGRID; 971397; 1.
DR DIP; DIP-41285N; -.
DR IntAct; P10215; 3.
DR MINT; P10215; -.
DR PRIDE; P10215; -.
DR DNASU; 2703350; -.
DR GeneID; 2703350; -.
DR KEGG; vg:2703350; -.
DR Proteomes; UP000009294; Genome.
DR GO; GO:0044201; C:host cell nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; 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_04023; HSV_NEC1; 1.
DR InterPro; IPR021152; Herpes_UL31.
DR Pfam; PF02718; Herpes_UL31; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host membrane; Host nucleus; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..306
FT /note="Nuclear egress protein 1"
FT /id="PRO_0000116006"
FT ZN_FING 106..225
FT /note="CCCH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04023,
FT ECO:0000269|PubMed:26511020"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4ZXS"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:4ZXS"
FT TURN 146..150
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:4ZXS"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:4ZXS"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:4ZXS"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:4ZXS"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:4ZXS"
SQ SEQUENCE 306 AA; 33953 MW; D4FE0FD98D934C46 CRC64;
MYDTDPHRRG SRPGPYHGKE RRRSRSSAAG GTLGVVRRAS RKSLPPHARK QELCLHERQR
YRGLFAALAQ TPSEEIAIVR SLSVPLVKTT PVSLPFCLDQ TVADNCLTLS GMGYYLGIGG
CCPACNAGDG RFAATSREAL ILAFVQQINT IFEHRAFLAS LVVLADRHNA PLQDLLAGIL
GQPELFFVHT ILRGGGACDP RLLFYPDPTY GGHMLYVIFP GTSAHLHYRL IDRMLTACPG
YRFVAHVWQS TFVLVVRRNA EKPTDAEIPT VSAADIYCKM RDISFDGGLM LEYQRLYATF
DEFPPP
