NEC2_EHV2
ID NEC2_EHV2 Reviewed; 287 AA.
AC Q66669;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Nuclear egress protein 2 {ECO:0000255|HAMAP-Rule:MF_04024};
GN Name=NEC2 {ECO:0000255|HAMAP-Rule:MF_04024}; OrderedLocusNames=67;
OS Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX NCBI_TaxID=82831;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT "The DNA sequence of equine herpesvirus 2.";
RL J. Mol. Biol. 249:520-528(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; U20824; AAC13855.1; -; Genomic_DNA.
DR PIR; S55662; S55662.
DR RefSeq; NP_042664.1; NC_001650.2.
DR SMR; Q66669; -.
DR PRIDE; Q66669; -.
DR GeneID; 1461027; -.
DR KEGG; vg:1461027; -.
DR Proteomes; UP000007083; 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..287
FT /note="Nuclear egress protein 2"
FT /id="PRO_0000406065"
FT TOPO_DOM 1..264
FT /note="Perinuclear space"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT TRANSMEM 265..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT TOPO_DOM 284..287
FT /note="Nuclear"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT REGION 191..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 31241 MW; 9DF2417CB377BD56 CRC64;
MNGSKRLVAQ LCQVVRSFIC QPGTAVDLWQ CAAGPHVFAK GSTQPICIVK LVHGQIYNLE
FVYKYWCHIL QSEKFPYSPV FIISNNGLAI TLKCFLCEPM DLHSQFGRCL SMDTDVYLPK
NTSVVLSQDD FTKFKTNLVF SKDLNVFNSM VVCRTYLTDF RQALQFLVVK AKNPKRVTAI
LGTIAQTLGL TPDTRSGEGG KNSERGEDDM VRRPIRAHRA GDSGGSPGTL PAEPQGAPTP
PGGGLGLSSG LGLVRRWTRC AFQRYFTVLA VGAVAAATFL AGAKLTG