NEC2_EBVB9
ID NEC2_EBVB9 Reviewed; 336 AA.
AC P03185; Q777G7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 90.
DE RecName: Full=Nuclear egress protein 2 {ECO:0000255|HAMAP-Rule:MF_04024};
GN Name=NEC2 {ECO:0000255|HAMAP-Rule:MF_04024}; ORFNames=BFRF1;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2998075; DOI=10.1016/0042-6822(85)90230-2;
RA Hudson G.S., Gibson T.J., Barrell B.G.;
RT "The BamHI F region of the B95-8 Epstein-Barr virus genome.";
RL Virology 147:99-109(1985).
RN [3]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=10708440; DOI=10.1128/jvi.74.7.3235-3244.2000;
RA Farina A., Santarelli R., Gonnella R., Bei R., Muraro R., Cardinali G.,
RA Uccini S., Ragona G., Frati L., Faggioni A., Angeloni A.;
RT "The BFRF1 gene of Epstein-Barr virus encodes a novel protein.";
RL J. Virol. 74:3235-3244(2000).
RN [4]
RP FUNCTION.
RX PubMed=15731264; DOI=10.1128/jvi.79.6.3703-3712.2005;
RA Farina A., Feederle R., Raffa S., Gonnella R., Santarelli R., Frati L.,
RA Angeloni A., Torrisi M.R., Faggioni A., Delecluse H.J.;
RT "BFRF1 of Epstein-Barr virus is essential for efficient primary viral
RT envelopment and egress.";
RL J. Virol. 79:3703-3712(2005).
RN [5]
RP INTERACTION WITH BFLF2, AND SUBCELLULAR LOCATION.
RX PubMed=15731265; DOI=10.1128/jvi.79.6.3713-3727.2005;
RA Gonnella R., Farina A., Santarelli R., Raffa S., Feederle R., Bei R.,
RA Granato M., Modesti A., Frati L., Delecluse H.J., Torrisi M.R.,
RA Angeloni A., Faggioni A.;
RT "Characterization and intracellular localization of the Epstein-Barr virus
RT protein BFLF2: interactions with BFRF1 and with the nuclear lamina.";
RL J. Virol. 79:3713-3727(2005).
RN [6]
RP INTERACTION WITH BFLF2.
RX PubMed=17005637; DOI=10.1128/jvi.01662-06;
RA Schnee M., Ruzsics Z., Bubeck A., Koszinowski U.H.;
RT "Common and specific properties of herpesvirus UL34/UL31 protein family
RT members revealed by protein complementation assay.";
RL J. Virol. 80:11658-11666(2006).
RN [7]
RP FUNCTION.
RX PubMed=16406456; DOI=10.1016/j.virol.2005.11.046;
RA Granato M., Farina A., Gonnella R., Santarelli R., Frati L., Faggioni A.,
RA Angeloni A.;
RT "Regulation of the expression of the Epstein-Barr virus early gene BFRF1.";
RL Virology 347:109-116(2006).
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:15731264, ECO:0000269|PubMed:16406456}.
CC -!- SUBUNIT: Forms a heterohexameric complex with NEC1. {ECO:0000255|HAMAP-
CC Rule:MF_04024, ECO:0000269|PubMed:15731265,
CC ECO:0000269|PubMed:17005637}.
CC -!- INTERACTION:
CC P03185; P0CK47: NEC1; NbExp=3; IntAct=EBI-2620196, EBI-2620189;
CC -!- SUBCELLULAR LOCATION: Host nucleus inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_04024, ECO:0000269|PubMed:10708440,
CC ECO:0000269|PubMed:15731265}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:10708440,
CC ECO:0000269|PubMed:15731265}. Note=Localizes also at the transient
CC membrane of 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; V01555; CAA24879.1; -; Genomic_DNA.
DR EMBL; M11923; AAA45869.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53399.1; -; Genomic_DNA.
DR PIR; F93065; QQBE7.
DR RefSeq; YP_401649.1; NC_007605.1.
DR SMR; P03185; -.
DR BioGRID; 971741; 4.
DR IntAct; P03185; 17.
DR MINT; P03185; -.
DR PRIDE; P03185; -.
DR DNASU; 3783699; -.
DR GeneID; 3783699; -.
DR KEGG; vg:3783699; -.
DR Proteomes; UP000153037; 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..336
FT /note="Nuclear egress protein 2"
FT /id="PRO_0000116033"
FT TOPO_DOM 1..315
FT /note="Perinuclear space"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT TRANSMEM 316..333
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT TOPO_DOM 334..336
FT /note="Nuclear"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT REGION 193..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 336 AA; 37632 MW; 0F2E3430DA95A944 CRC64;
MASPEERLLD ELNNVIVSFL CDSGSLEVER CSGAHVFSRG SSQPLCTVKL RHGQIYHLEF
VYKFLAFKLK NCNYPSSPVF VISNNGLATT LRCFLHEPSG LRSGQSGPCL GLSTDVDLPK
NSIIMLGQDD FIKFKSPLVF PAELDLLKSM VVCRAYITEH RTTMQFLVFQ AANAQKASRV
MDMISDMSQQ LSRSGQVEDT GARVTGGGGP RPGVTHSGCL GDSHVRGRGG WDLDNFSEAE
TEDEASYAPW RDKDSWSESE AAPWKKELVR HPIRRHRTRE TRRMRGSHSR VEHVPPETRE
TVVGGAWRYS WRATPYLARV LAVTAVALLL MFLRWT
