ID   NEC1_HHV8P              Reviewed;         302 AA.
AC   F5H982;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   02-JUN-2021, entry version 28.
DE   RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN   Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; OrderedLocusNames=ORF69;
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 ORF67.
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).
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_04023,
CC       ECO:0000269|PubMed:23365436}.
CC   -!- SUBUNIT: Forms a heterohexameric complex with NEC2. Interacts with
CC       capsid vertex specific component 2/CVC2; this interaction directs the
CC       capsid to the host inner nuclear membrane to initiate budding.
CC       {ECO:0000255|HAMAP-Rule:MF_04023}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04023, ECO:0000269|PubMed:23365436}. Note=Remains attached to
CC       the nucleus inner membrane through interaction with NEC2.
CC       {ECO:0000255|HAMAP-Rule:MF_04023}.
CC   -!- PTM: Phosphorylated at serine residues in the N-terminus. This
CC       phosphorylation regulates the localization within the inner nuclear
CC       membrane. {ECO:0000255|HAMAP-Rule:MF_04023}.
CC   -!- SIMILARITY: Belongs to the herpesviridae NEC1 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04023}.
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DR   EMBL; AF148805; AAD46497.1; -; Genomic_DNA.
DR   RefSeq; YP_001129427.1; NC_009333.1.
DR   SMR; F5H982; -.
DR   BioGRID; 1776947; 16.
DR   PRIDE; F5H982; -.
DR   GeneID; 4961444; -.
DR   KEGG; vg:4961444; -.
DR   Proteomes; UP000000942; Genome.
DR   GO; GO:0044201; C:host cell nuclear inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046765; P:viral budding from nuclear membrane; IEA:InterPro.
DR   HAMAP; MF_04023; HSV_NEC1; 1.
DR   InterPro; IPR021152; Herpes_UL31.
DR   Pfam; PF02718; Herpes_UL31; 1.
PE   1: Evidence at protein level;
KW   Host membrane; Host nucleus; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..302
FT                   /note="Nuclear egress protein 1"
FT                   /id="PRO_0000423786"
FT   ZN_FING         102..227
FT                   /note="CCCH-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04023"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   302 AA;  33158 MW;  976E26C3A73AEF07 CRC64;
     MPKSVSSHIS LATSTGRSGP RDIRRCLSSR LRSVPPGARS ASVSSKHRNG LRKFISDKVF
     FSILSHRHEL GVDFLREMET PICTSKTVML PLDLSTVAPG RCVSLSPFGH SSNMGFQCAL
     CPSTENPTVA QGSRPQTMVG DALKKNNELC SVALAFYHHA DKVIQHKTFY LSLLSHSMDV
     VRQSFLQPGL LYANLVLKTF GHDPLPIFTT NNGMLTMCIL FKTRALHLGE TALRLLMDNL
     PNYKISADCC RQSYVVKFVP THPDTASIAV QVHTICEAVA ALDCTDEMRD DIQKGTALVN
     AL