ID   NEC1_EHV2               Reviewed;         305 AA.
AC   Q66672;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 56.
DE   RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN   Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; OrderedLocusNames=69;
OS   Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX   NCBI_TaxID=82831;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA   Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus 2.";
RL   J. Mol. Biol. 249:520-528(1995).
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}.
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DR   EMBL; U20824; AAC13859.1; -; Genomic_DNA.
DR   PIR; S55666; S55666.
DR   RefSeq; NP_042668.1; NC_001650.2.
DR   SMR; Q66672; -.
DR   GeneID; 1461025; -.
DR   KEGG; vg:1461025; -.
DR   Proteomes; UP000007083; 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..305
FT                   /note="Nuclear egress protein 1"
FT                   /id="PRO_0000406038"
FT   ZN_FING         104..230
FT                   /note="CCCH-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04023"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  34322 MW;  C8321C295F305C41 CRC64;
     MDRERPRKTR EPASPGSVLS KRSKLSRKSL ALRSLNKFHP YKAPSSVRSL KKAHTLVSNG
     DFFNGISLNC EFGKDFLREM DTPICTSKVI CLPLDVHEIA PGRCLVLSPL GHACNMGFYC
     EKCTQSGQNS YSQFQGRGGN AKMAAQNSKD DLHSVTLTFY NQVSKVVQNK NFYLSLLSHS
     LTTIKKSFVQ PSLLYSYTVL RALCDDVFPI FKDTENGLCM FALFKTDDLH VSETCLRHLV
     DNLIHYRVTL DCVKHTYMLK FSPIRAEANG MTIQEVEICE AITGLDFTDE IKQEIISGQE
     LVSEL