ID   NEC1_EBVA8              Reviewed;         318 AA.
AC   P0CK48; P03183; Q777G9;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   23-FEB-2022, entry version 25.
DE   RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN   Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; ORFNames=BFLF2;
OS   Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=82830;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA   Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT   "The genome of Epstein-Barr virus type 2 strain AG876.";
RL   Virology 350:164-170(2006).
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   -!- 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}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane
CC       through interaction with NEC2. {ECO:0000255|HAMAP-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   -!- SIMILARITY: Belongs to the herpesviridae NEC1 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04023}.
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; DQ279927; ABB89218.1; -; Genomic_DNA.
DR   RefSeq; YP_001129443.1; NC_009334.1.
DR   RefSeq; YP_401647.1; NC_007605.1.
DR   SMR; P0CK48; -.
DR   IntAct; P0CK48; 11.
DR   MINT; P0CK48; -.
DR   PRIDE; P0CK48; -.
DR   DNASU; 3783698; -.
DR   GeneID; 3783698; -.
DR   GeneID; 5176194; -.
DR   KEGG; vg:3783698; -.
DR   KEGG; vg:5176194; -.
DR   Proteomes; UP000007639; 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:0046765; P:viral budding from nuclear membrane; IEA:InterPro.
DR   HAMAP; MF_04023; HSV_NEC1; 1.
DR   InterPro; IPR021152; Herpes_UL31.
DR   Pfam; PF02718; Herpes_UL31; 1.
PE   3: Inferred from homology;
KW   Host membrane; Host nucleus; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..318
FT                   /note="Nuclear egress protein 1"
FT                   /id="PRO_0000415966"
FT   ZN_FING         129..239
FT                   /note="CCCH-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04023"
SQ   SEQUENCE   318 AA;  35361 MW;  E69F1357D72E94F4 CRC64;
     MAPVTPDAVN ARQQRPADPA LRRLMHPHHR NYTASKASAH SVKSVSRCGK SRSELGRMER
     VGSVARSICS RHTRHGVDRS HFSLRDFFRG ISANFELGKD FLREMNTPIH VSEAVFLPLS
     LCTLSPGRCL RLSPFGHSLT LGSHCEICIN RSQVHVPQEF SSTQLSFFNN VHKIIPNKTF
     YVSLLSSSPS AVKAGLSQPS LLYAYLVTGH FCGTICPIFS TNGKGRLIMH LLLQGTSLHI
     PETCLKLLCE NIGPTYELAV DLVGDAFCIK VSPRDTVYEK AVNVDEDAIY EAIKDLECGD
     ELRLQIINYT QLILENKQ