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NEC2_HHV8P
ID   NEC2_HHV8P              Reviewed;         271 AA.
AC   F5HA27;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   02-JUN-2021, entry version 29.
DE   RecName: Full=Nuclear egress protein 2 {ECO:0000255|HAMAP-Rule:MF_04024};
GN   Name=NEC2 {ECO:0000255|HAMAP-Rule:MF_04024}; OrderedLocusNames=ORF67;
OS   Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS   sarcoma-associated herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=868565;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA   Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT   "Identification of a spliced gene from Kaposi's sarcoma-associated
RT   herpesvirus encoding a protein with similarities to latent membrane
RT   proteins 1 and 2A of Epstein-Barr virus.";
RL   J. Virol. 73:6953-6963(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA   Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT   "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL   J. Gen. Virol. 87:1781-1804(2006).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PROTEIN ORF69.
RX   PubMed=23365436; DOI=10.1128/jvi.03418-12;
RA   Luitweiler E.M., Henson B.W., Pryce E.N., Patel V., Coombs G.,
RA   McCaffery J.M., Desai P.J.;
RT   "Interactions of the Kaposi's Sarcoma-associated herpesvirus nuclear egress
RT   complex: ORF69 is a potent factor for remodeling cellular membranes.";
RL   J. Virol. 87:3915-3929(2013).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23623980; DOI=10.1016/j.virusres.2013.04.001;
RA   Farina A., Santarelli R., Bloise R., Gonnella R., Granato M., Bei R.,
RA   Modesti A., Cirone M., Bengtsson L., Angeloni A., Faggioni A.;
RT   "KSHV ORF67 encoded lytic protein localizes on the nuclear membrane and
RT   alters emerin distribution.";
RL   Virus Res. 175:143-150(2013).
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:23365436, ECO:0000269|PubMed:23623980}.
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, ECO:0000269|PubMed:23365436,
CC       ECO:0000269|PubMed:23623980}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:23365436,
CC       ECO:0000269|PubMed:23623980}. 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; AF148805; ABD28920.1; -; Genomic_DNA.
DR   RefSeq; YP_001129424.1; NC_009333.1.
DR   SMR; F5HA27; -.
DR   BioGRID; 1777027; 2.
DR   PRIDE; F5HA27; -.
DR   DNASU; 4961524; -.
DR   GeneID; 4961524; -.
DR   KEGG; vg:4961524; -.
DR   Proteomes; UP000000942; 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   1: Evidence at protein level;
KW   Host membrane; Host nucleus; Late protein; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..271
FT                   /note="Nuclear egress protein 2"
FT                   /id="PRO_0000423787"
FT   TOPO_DOM        1..249
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   TRANSMEM        250..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT   TOPO_DOM        268..271
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
SQ   SEQUENCE   271 AA;  29849 MW;  A9B44CDDF9E58F04 CRC64;
     MSVVGKRVVD ELCRVVSSYL GQSGQSLDLE RCIDGAPVYA KGGATAICTV RMQHGCVYHL
     EFVYKFWAHL LEEMHYPFSP CFVISNNGLS TTLKCFLCRP SDAVSQFGHV LPVESDVYLA
     KNTSVVLGQD DFTKFKASLV FSKNLGVYNS MVICRTYFTD YRQVLQFLVV TPKSHKRLKS
     LLETVYCLAA PVADSAAQGG AGFPTNGRDA RACTSDVTAV YWAGQGGRTV RILGAFQWSL
     GRAVALVRRS WPWISAGIAF LCLGLVWMRP S
 
 
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