ID   NEC1_GAHVM              Reviewed;         300 AA.
AC   Q9E6N8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   12-AUG-2020, entry version 55.
DE   RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN   Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; OrderedLocusNames=MDV044;
OS   Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS   disease herpesvirus type 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX   NCBI_TaxID=10389;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA   Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT   "The genome of a very virulent Marek's disease virus.";
RL   J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14224.1; -; Genomic_DNA.
DR   RefSeq; YP_001033960.1; NC_002229.3.
DR   SMR; Q9E6N8; -.
DR   GeneID; 4811505; -.
DR   KEGG; vg:4811505; -.
DR   Proteomes; UP000008072; 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..300
FT                   /note="Nuclear egress protein 1"
FT                   /id="PRO_0000406591"
FT   ZN_FING         90..217
FT                   /note="CCCH-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04023"
SQ   SEQUENCE   300 AA;  34249 MW;  1914126DEF95AC4E CRC64;
     MTGHTLVRRK SIGRDKRLVG RSRRQWRDMN LPSYGNSKGT NMDIYRAYFE FIAESPADEL
     MLVKDLVTPL IKTTSISLPF DMSEAVADNC LSLSGMGYYL GVGGCCPTCV SSGDPRLGRN
     DRAALILAYV QQINNIYHYR IFLASIIVLG DRLRGDARDK DMESILTRII AIPELFFAYY
     VLLDSGIKNV KVLFYLDREA GSSEYMMYIV FPGKALHLHY RLIDCMKSAC KSYRIIAHVW
     RTNFLLVIRK EYDRQTDSCD VPAVNAEDVY CKLCDLNIDG ELLLEYGKLY SAFDEFLPPR