ID   NEC1_SHV21              Reviewed;         261 AA.
AC   Q01041;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-DEC-2020, entry version 58.
DE   RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN   Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; OrderedLocusNames=69, ECRF2;
OS   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1314457; DOI=10.1016/0042-6822(92)90759-i;
RA   Nicholas J., Cameron K.R., Coleman H., Newman C., Honess R.W.;
RT   "Analysis of nucleotide sequence of the rightmost 43 kbp of herpesvirus
RT   saimiri (HVS) L-DNA: general conservation of genetic organization between
RT   HVS and Epstein-Barr virus.";
RL   Virology 188:296-310(1992).
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; X64346; CAA45692.1; -; Genomic_DNA.
DR   EMBL; M86409; AAA46145.1; -; Genomic_DNA.
DR   RefSeq; NP_040271.1; NC_001350.1.
DR   SMR; Q01041; -.
DR   GeneID; 1682457; -.
DR   KEGG; vg:1682457; -.
DR   Proteomes; UP000000587; 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..261
FT                   /note="Nuclear egress protein 1"
FT                   /id="PRO_0000116011"
FT   ZN_FING         70..184
FT                   /note="CCCH-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04023"
SQ   SEQUENCE   261 AA;  29784 MW;  16623EF1B30860A8 CRC64;
     MSSRSVKSRK STKSRRHHPY VKLTDKMFFS AISSKKELGT DFLREMDAPI CTSKTILLPL
     DLNSISPGRC IYLSPFGHSS NMEFQCEKCT ESKNKGSGDV SQNHDLYSVT LVFYKNVDKV
     VKHKAFYLSL LSHSMENLKK SFTQPELLYA YVVVKEAGHN VFPIFFEKDD CLSICLTFKC
     QTLHIGESCL RMLMDNLPNY KISIDYIKDV YAMTFTQCFA IQRNISIAED TICESVSTLD
     CTDELREEIV KGINALQIKD I