ID   NEC2_EHV1V              Reviewed;         275 AA.
AC   P84406; Q6S6P5;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   02-JUN-2021, entry version 44.
DE   RecName: Full=Nuclear egress protein 2 {ECO:0000255|HAMAP-Rule:MF_04024};
GN   Name=NEC2 {ECO:0000255|HAMAP-Rule:MF_04024}; OrderedLocusNames=26;
OS   Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=310273;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAS45910.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AY464052; AAS45910.1; -; Genomic_DNA.
DR   RefSeq; YP_053071.1; NC_001491.2.
DR   SMR; P84406; -.
DR   GeneID; 1487492; -.
DR   KEGG; vg:1487492; -.
DR   Proteomes; UP000008296; 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   Transmembrane; Transmembrane helix.
FT   CHAIN           1..275
FT                   /note="Nuclear egress protein 2"
FT                   /id="PRO_0000116028"
FT   TOPO_DOM        1..251
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   TOPO_DOM        273..275
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   REGION          197..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   275 AA;  30680 MW;  283A6F8395AB86A5 CRC64;
     MDSYNYRDFA VGGGLLQRIR LVVSGSLHCG ESDATLNDPK HLPARCVFQF SGPDNNSVTF
     PIEYVLRLMK NWARSQCDPY IRIQNTGVSV LFQGFFFAPP NAPMASITSE HNNVILKSTH
     TTGLALSGIE RVKRGGGLDL RPLQAMMQIS CFTRMPVVQL SFRFMGPEDA SRTQRLLERA
     TSFGAMELHQ KRTVDSCDRS NGIVSPREHR ECRERQKRRP TPKRCASEVF ASLASISSAF
     ASERVKRRPV RIAAAILAFV FVAVILAIAT KGRLF