ID   NEC2_HHV2H              Reviewed;         276 AA.
AC   P89457;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, 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=UL34;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA   McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT   "Comparative sequence analysis of the long repeat regions and adjoining
RT   parts of the long unique regions in the genomes of herpes simplex viruses
RT   types 1 and 2.";
RL   J. Gen. Virol. 72:3057-3075(1991).
RN   [2]
RP   FUNCTION, AND TOPOLOGY.
RX   PubMed=10993927; DOI=10.1099/0022-1317-81-10-2397;
RA   Shiba C., Daikoku T., Goshima F., Takakuwa H., Yamauchi Y., Koiwai O.,
RA   Nishiyama Y.;
RT   "The UL34 gene product of herpes simplex virus type 2 is a tail-anchored
RT   type II membrane protein that is significant for virus envelopment.";
RL   J. Gen. Virol. 81:2397-2405(2000).
RN   [3]
RP   INTERACTION WITH UL31.
RX   PubMed=11369887; DOI=10.1099/0022-1317-82-6-1423;
RA   Yamauchi Y., Shiba C., Goshima F., Nawa A., Murata T., Nishiyama Y.;
RT   "Herpes simplex virus type 2 UL34 protein requires UL31 protein for its
RT   relocation to the internal nuclear membrane in transfected cells.";
RL   J. Gen. Virol. 82:1423-1428(2001).
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       ECO:0000269|PubMed:10993927}.
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; Z86099; CAB06720.1; -; Genomic_DNA.
DR   RefSeq; YP_009137186.1; NC_001798.2.
DR   SMR; P89457; -.
DR   PRIDE; P89457; -.
DR   DNASU; 1487320; -.
DR   GeneID; 1487320; -.
DR   KEGG; vg:1487320; -.
DR   Proteomes; UP000001874; 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   GO; GO:0046765; P:viral budding from nuclear membrane; IDA:UniProtKB.
DR   HAMAP; MF_04024; HSV_NEC2; 1.
DR   InterPro; IPR007626; Herpesvirus_viron_egress-type.
DR   Pfam; PF04541; Herpes_U34; 1.
PE   1: Evidence at protein level;
KW   Host membrane; Host nucleus; Late protein; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..276
FT                   /note="Nuclear egress protein 2"
FT                   /id="PRO_0000406182"
FT   TOPO_DOM        1..253
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   TOPO_DOM        275..276
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   REGION          212..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  29524 MW;  EA9CDB114245094E CRC64;
     MAGMGKPYGG RPGDAFEGLV QRIRLIVPAT LRGGGGESGP YSPSNPPSRC AFQFHGQDGS
     DEAFPIEYVL RLMNDWADVP CNPYLRVQNT GVSVLFQGFF NRPHGAPGGA ITAEQTNVIL
     HSTETTGLSL GDLDDVKGRL GLDARPMMAS MWISCFVRMP RVQLAFRFMG PEDAVRTRRI
     LCRAAEQALA RRRRSRRSQD DYGAVVVAAA HHSSGAPGPG VAASGPPAPP GRGPARPWHQ
     AVQLFRAPRP GPPALLLLAA GLFLGAAIWW AVGARL