NEC1_PSHV1
ID NEC1_PSHV1 Reviewed; 345 AA.
AC Q6UDK0;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 02-DEC-2020, entry version 42.
DE RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; OrderedLocusNames=UL31;
OS Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS (Pacheco's disease virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX NCBI_TaxID=670426;
OH NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA Thureen D.R., Keeler C.L. Jr.;
RT "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL J. Virol. 80:7863-7872(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_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; AY372243; AAQ73710.1; -; Genomic_DNA.
DR RefSeq; NP_944404.1; NC_005264.1.
DR SMR; Q6UDK0; -.
DR GeneID; 2656985; -.
DR KEGG; vg:2656985; -.
DR Proteomes; UP000006840; 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 3: Inferred from homology;
KW Host membrane; Host nucleus; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..345
FT /note="Nuclear egress protein 1"
FT /id="PRO_0000406849"
FT ZN_FING 115..247
FT /note="CCCH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04023"
SQ SEQUENCE 345 AA; 38521 MW; DA9CCB87377F7123 CRC64;
MSDVALKRNS SFFRAKARLT LLKRRDGGVI SRSLEHRRSS RRRSSVSAPT RRVSGTLAKL
GADDRRQFFD AFFRMTAVSP EETVSLLRSM TVPVIQQENI SLPYDINAKF APGDCISLSE
MGYTLEMGGC CSLCSYGWST TTPPELPALE LAFMHHLSSV VEFKELVTSL RVCAGNSIVG
NGAYENEGLL RMIKHLLEQS TLFYAYYTVK GGVSHDFRVL ISEDGGGDGG SPAYAMYFVF
KPGSPLHLGA KLIRQLIFNC PGYKWHADVH EGAFLLVVTR DRCSAIPEPR RVKLDPEDVY
RRYCDVLVTE EKVHDYSRLY STFSTYCPPA SRREQTAAPA TAKQV