NEC1_VZVD
ID NEC1_VZVD Reviewed; 333 AA.
AC P09283;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 02-JUN-2021, entry version 58.
DE RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; OrderedLocusNames=27;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
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; X04370; CAA27910.1; -; Genomic_DNA.
DR PIR; A27214; WZBE27.
DR SMR; P09283; -.
DR PRIDE; P09283; -.
DR Proteomes; UP000002602; 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..333
FT /note="Nuclear egress protein 1"
FT /id="PRO_0000116010"
FT ZN_FING 128..251
FT /note="CCCH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04023"
FT REGION 45..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 333 AA; 38236 MW; C01BC52DFA5E2E1F CRC64;
MHLKPTRFFH ANQPPMPHSY EMEDLCFDDM QYRWSPSNTP YRSMSRRYKS VSRSGPSMRV
RSRTPCRRQT IRGKLMSKER SVYRHYFNYI ARSPPEELAT VRGLIVPIIK TTPVTLPFNL
GQTVADNCLS LSGMGYHLGL GGYCPTCTAS GEPRLCRTDR AALILAYVQQ LNNIYEYRVF
LASILALSDR ANMQAASAEP LLSSVLAQPE LFFMYHIMRE GGMRDIRVLF YRDGDAGGFM
MYVIFPGKSV HLHYRLIDHI QAACRGYKIV AHVWQTTFLL SVCRNPEQQT ETVVPSIGTS
DVYCKMCDLN FDGELLLEYK RLYALFDDFV PPR