ID   NEC2_HHV6U              Reviewed;         276 AA.
AC   P52465;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-JUN-2021, entry version 63.
DE   RecName: Full=Nuclear egress protein 2 {ECO:0000255|HAMAP-Rule:MF_04024};
GN   Name=NEC2 {ECO:0000255|HAMAP-Rule:MF_04024}; OrderedLocusNames=U34, XILF2;
OS   Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS   lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=10370;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA   Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA   Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT   "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT   genome evolution.";
RL   Virology 209:29-51(1995).
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; X83413; CAA58414.1; -; Genomic_DNA.
DR   RefSeq; NP_042927.1; NC_001664.2.
DR   SMR; P52465; -.
DR   PRIDE; P52465; -.
DR   DNASU; 1487911; -.
DR   GeneID; 1487911; -.
DR   KEGG; vg:1487911; -.
DR   Proteomes; UP000009295; 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..276
FT                   /note="Nuclear egress protein 2"
FT                   /id="PRO_0000116029"
FT   TOPO_DOM        1..245
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   TRANSMEM        246..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   TOPO_DOM        265..276
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
SQ   SEQUENCE   276 AA;  31671 MW;  5C5ED509CF9CE937 CRC64;
     MANVLKEKMY DELLSATCRI LKLGSHDYRI TERNLLSKNP KFPLCDIILK LDYAYNLEYL
     LSLWEHVTKQ EPRFVFKNTG GAVSMSCYLH APVKVEGHHA VRECNILRVN ECLTVRMSDI
     VAMKPSTFAV FTKCIIRRNR DDTYVVEFVA FGPENESEYI SLLKAIFLKK CSMGKQHLES
     NRFCQGLRRR SSHVLEKGRF ESSGKVVNKA SAVVTSQESI KQFYEKEKSL LSGVKFWRLS
     ERHCRFALVG ICFLLALYFC YVLLKKTPTP ASGSVV