ID   NEC2_HHV6Z              Reviewed;         276 AA.
AC   Q9QJ35;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-JUN-2021, entry version 43.
DE   RecName: Full=Nuclear egress protein 2 {ECO:0000255|HAMAP-Rule:MF_04024};
GN   Name=NEC2 {ECO:0000255|HAMAP-Rule:MF_04024}; OrderedLocusNames=U34;
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].
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_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; AF157706; AAD49648.1; -; Genomic_DNA.
DR   RefSeq; NP_050215.1; NC_000898.1.
DR   SMR; Q9QJ35; -.
DR   PRIDE; Q9QJ35; -.
DR   DNASU; 1497036; -.
DR   GeneID; 1497036; -.
DR   KEGG; vg:1497036; -.
DR   Proteomes; UP000006930; 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_0000408437"
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;  31441 MW;  FA1956D7BEBBE85A CRC64;
     MANVLKEKMY DELLSATCRI LKLGSHDYRM TERNLLSKNP KFPLCDIILK LDYAYNLEYL
     LSLWEHVTKQ EPRFVFKNTG GAVSMSCYLH APVKAEGHHA VRECNILRVN ECLTVRMSDI
     VAMKPSTFAV FTKCIIRRNR DETYVVEFVA FGPENESEYI SLLKAIFLKK CSMGKQHLES
     NRFCQGLRRR SSHVLEKGQL GSSGEIANKA SAVVTSQESI NQFYEKEKSF LSGVKFSRLS
     ERHCRVAIVS ICFLLALYFC YVLLKKTPTP ASGPVV