ID   NEC1_HHV2H              Reviewed;         305 AA.
AC   P89454;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-JUN-2021, entry version 64.
DE   RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN   Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; Synonyms=UL31;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA   McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT   "Comparative sequence analysis of the long repeat regions and adjoining
RT   parts of the long unique regions in the genomes of herpes simplex viruses
RT   types 1 and 2.";
RL   J. Gen. Virol. 72:3057-3075(1991).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10550666; DOI=10.1007/s007050050715;
RA   Zhu H.Y., Yamada H., Jiang Y.M., Yamada M., Nishiyama Y.;
RT   "Intracellular localization of the UL31 protein of herpes simplex virus
RT   type 2.";
RL   Arch. Virol. 144:1923-1935(1999).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11369887; DOI=10.1099/0022-1317-82-6-1423;
RA   Yamauchi Y., Shiba C., Goshima F., Nawa A., Murata T., Nishiyama Y.;
RT   "Herpes simplex virus type 2 UL34 protein requires UL31 protein for its
RT   relocation to the internal nuclear membrane in transfected cells.";
RL   J. Gen. Virol. 82:1423-1428(2001).
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   -!- 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:10550666,
CC       ECO:0000269|PubMed:11369887}. Note=Remains attached to the nucleus
CC       inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-
CC       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; Z86099; CAB06756.1; -; Genomic_DNA.
DR   RefSeq; YP_009137183.1; NC_001798.2.
DR   SMR; P89454; -.
DR   PRIDE; P89454; -.
DR   DNASU; 1487317; -.
DR   GeneID; 1487317; -.
DR   KEGG; vg:1487317; -.
DR   Proteomes; UP000001874; 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; IDA:UniProtKB.
DR   HAMAP; MF_04023; HSV_NEC1; 1.
DR   InterPro; IPR021152; Herpes_UL31.
DR   Pfam; PF02718; Herpes_UL31; 1.
PE   3: Inferred from homology;
KW   Host membrane; Host nucleus; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..305
FT                   /note="Nuclear egress protein 1"
FT                   /id="PRO_0000406179"
FT   ZN_FING         105..224
FT                   /note="CCCH-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04023"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  33915 MW;  9DC2D2CAF21B5A60 CRC64;
     MYDIAPRRSG SRPGPGRDKT RRRSRFSAAG NPGVERRASR KSLPSHARRL ELCLHERRRY
     RGFFAALAQT PSEEIAIVRS LSVPLVKTTP VSLPFSLDQT VADNCLTLSG MGYYLGIGGC
     CPACSAGDGR LATVSREALI LAFVQQINTI FEHRTFLASL VVLADRHSTP LQDLLADTLG
     QPELFFVHTI LRGGGACDPR FLFYPDPTYG GHMLYVIFPG TSAHLHYRLI DRMLTACPGY
     RFAAHVWQST FVLVVRRNAE KPADAEIPTV SAADIYCKMR DISFDGGLML EYQRLYATFD
     EFPPP