ID NEC1_ALHV1 Reviewed; 280 AA.
AC O36420;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; OrderedLocusNames=69;
OS Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Macavirus;
OC Macavirus alcelaphinegamma1.
OX NCBI_TaxID=654901;
OH NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997;
RA Ensser A., Pflanz R., Fleckenstein B.;
RT "Primary structure of the alcelaphine herpesvirus 1 genome.";
RL J. Virol. 71:6517-6525(1997).
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}. Note=Remains attached to the nucleus inner membrane
CC through interaction with NEC2. {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; AF005370; AAC58117.1; -; Genomic_DNA.
DR PIR; T03165; T03165.
DR RefSeq; NP_065569.1; NC_002531.1.
DR SMR; O36420; -.
DR GeneID; 911772; -.
DR KEGG; vg:911772; -.
DR Proteomes; UP000000941; Segment.
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 3: Inferred from homology;
KW Host membrane; Host nucleus; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..280
FT /note="Nuclear egress protein 1"
FT /id="PRO_0000405765"
FT ZN_FING 86..203
FT /note="CCCH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04023"
SQ SEQUENCE 280 AA; 31415 MW; 401D13C92D1D57D9 CRC64;
MHKIQKMSCT PSVRSRYTLK RKRLNSAKSA TLKKKKVFLS NSEFFAGVST NYELGKDFLR
EMDTPICTSN TVFLPVKFSD VAPGRCLTLS PYGHSSVLGF HCQECKPDSS SGFTQAQQSA
ESNELLSVNL CFLNNVEKVV QHKAFYLSLL GHSMNTVKQS LGQPSLLYCY TVLKKFYPQI
FPIFTANGPM LTMYIIFTSL TLHVSEAVLR ILTDNVENHN LSADCYKGHY ILSIEPQALE
ESNLNVCVTK ICDLVAQLDF SDELKQEYVN GSTLIANFLN
//
