ID   NEC2_VZVD               Reviewed;         269 AA.
AC   P09280;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-JUN-2021, entry version 65.
DE   RecName: Full=Nuclear egress protein 2 {ECO:0000255|HAMAP-Rule:MF_04024};
GN   Name=NEC2 {ECO:0000255|HAMAP-Rule:MF_04024}; OrderedLocusNames=24;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
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_04024}.
CC   -!- SUBUNIT: Forms a heterohexameric complex with NEC1. {ECO:0000255|HAMAP-
CC       Rule:MF_04024}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04024}. Note=Localizes also at the transient membrane of
CC       perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
CC   -!- PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04024}.
CC   -!- SIMILARITY: Belongs to the herpesviridae NEC2 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04024}.
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DR   EMBL; X04370; CAA27907.1; -; Genomic_DNA.
DR   PIR; F27343; WZBE24.
DR   SMR; P09280; -.
DR   PRIDE; P09280; -.
DR   Proteomes; UP000002602; Genome.
DR   GO; GO:0044201; C:host cell nuclear inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   HAMAP; MF_04024; HSV_NEC2; 1.
DR   InterPro; IPR007626; Herpesvirus_viron_egress-type.
DR   Pfam; PF04541; Herpes_U34; 1.
PE   3: Inferred from homology;
KW   Host membrane; Host nucleus; Late protein; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..269
FT                   /note="Nuclear egress protein 2"
FT                   /id="PRO_0000116031"
FT   TOPO_DOM        1..247
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   TOPO_DOM        269
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
SQ   SEQUENCE   269 AA;  30452 MW;  EE401F8595C169C5 CRC64;
     MSRRTYVRSE RRRGCGDNLL QRIRLVVPSA LQCCDGDLPI FDPQRPPARC VFQFNGEDNV
     SEAFPVEYIM RLMANWAQVD CDPYIKIQNT GVSVLFQGFF FRPTNAPVAE VSIDSNNVIL
     SSTLSTGINL SALESIKRGG GIDRRPLQAL MWVNCFVRMP YVQLSFRFMG PEDPSRTIKL
     MARATDAYMY KETGNNLDEY IRWRPSFRSP PENGSPNTSV QMQSDIKPAL PDTQTTRVWK
     LALPVANVTY ALFIVIVLVV VLGAVLFWK