ID   NEC1_HHV6Z              Reviewed;         264 AA.
AC   Q9WT27; Q77PU8;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   02-JUN-2021, entry version 52.
DE   RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN   Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; OrderedLocusNames=U37;
OS   Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=36351;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HST;
RX   PubMed=10482554; DOI=10.1128/jvi.73.10.8053-8063.1999;
RA   Isegawa Y., Mukai T., Nakano K., Kagawa M., Chen J., Mori Y., Sunagawa T.,
RA   Kawanishi K., Sashihara J., Hata A., Zou P., Kosuge H., Yamanishi K.;
RT   "Comparison of the complete DNA sequences of human herpesvirus 6 variants A
RT   and B.";
RL   J. Virol. 73:8053-8063(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA   Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA   Pellett P.E.;
RT   "Human herpesvirus 6B genome sequence: coding content and comparison with
RT   human herpesvirus 6A.";
RL   J. Virol. 73:8040-8052(1999).
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; AF157706; AAD49651.1; -; Genomic_DNA.
DR   EMBL; AB021506; BAA78258.1; -; Genomic_DNA.
DR   PIR; T43997; T43997.
DR   RefSeq; NP_050218.1; NC_000898.1.
DR   SMR; Q9WT27; -.
DR   PRIDE; Q9WT27; -.
DR   DNASU; 1497039; -.
DR   GeneID; 1497039; -.
DR   KEGG; vg:1497039; -.
DR   Proteomes; UP000006930; Genome.
DR   Proteomes; UP000142685; 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..264
FT                   /note="Nuclear egress protein 1"
FT                   /id="PRO_0000408435"
FT   ZN_FING         83..187
FT                   /note="CCCH-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04023"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   264 AA;  30869 MW;  80377776C12A0223 CRC64;
     MTVHKNRFRR SRSLSVTHRI QKRPDHREKT KLYLQLKLHD LHAVFNLFPE YEQKFLAIIK
     LPITGKEPID VPFSLSNHHQ HTCLEFSPYA NEQISKSACL HCESVSVPTS SDAMVAHLNQ
     VTNVMQNRFY FYGFRKDMEL IRMSAKQPTI FQIFYIVHNT INNIFPIMFE KKQKLGMHIV
     FQSRTLHIPC ECIKQIIAVS SGYNVYLDIL QDSVILTVLC ETLDTNTNIH IDIGMLQKKL
     EEMDIPNEIS DRLEKYKGHL IGFH