NEC1_HCMVM
ID NEC1_HCMVM Reviewed; 376 AA.
AC F5HFZ4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 23-FEB-2022, entry version 34.
DE RecName: Full=Nuclear egress protein 1 {ECO:0000255|HAMAP-Rule:MF_04023};
GN Name=NEC1 {ECO:0000255|HAMAP-Rule:MF_04023}; OrderedLocusNames=UL53;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Merlin;
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
RN [2] {ECO:0007744|PDB:5D5N}
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 1-175, AND INTERACTION WITH NEC2.
RX PubMed=26432641; DOI=10.1074/jbc.c115.686527;
RA Walzer S.A., Egerer-Sieber C., Sticht H., Sevvana M., Hohl K., Milbradt J.,
RA Muller Y.A., Marschall M.;
RT "Crystal Structure of the Human Cytomegalovirus pUL50-pUL53 Core Nuclear
RT Egress Complex Provides Insight into a Unique Assembly Scaffold for Virus-
RT Host Protein Interactions.";
RL J. Biol. Chem. 290:27452-27458(2015).
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, ECO:0000269|PubMed:26432641}.
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 (By similarity). Phosphorylation by viral kinase UL97 at Ser-
CC 19 plays an important role for correct viral nuclear egress complex
CC (NEC) localization (By similarity). {ECO:0000250|UniProtKB:P16794,
CC 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; AY446894; AAR31617.1; -; Genomic_DNA.
DR RefSeq; YP_081512.1; NC_006273.2.
DR PDB; 5D5N; X-ray; 2.44 A; B=50-292.
DR PDBsum; 5D5N; -.
DR SMR; F5HFZ4; -.
DR PRIDE; F5HFZ4; -.
DR DNASU; 3077575; -.
DR GeneID; 3077575; -.
DR KEGG; vg:3077575; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; 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 1: Evidence at protein level;
KW 3D-structure; Host membrane; Host nucleus; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..376
FT /note="Nuclear egress protein 1"
FT /id="PRO_0000416452"
FT ZN_FING 106..211
FT /note="CCCH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04023"
FT REGION 22..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16794"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5D5N"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:5D5N"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:5D5N"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:5D5N"
SQ SEQUENCE 376 AA; 42302 MW; 07A2E48A86AFE140 CRC64;
MSSVSGVRTP RERRSALRSL LRKRRQRELA SKVASTVNGA TSANNHGEPP SPADARPRLT
LHDLHDIFRE HPELELKYLN MMKMAITGKE SICLPFNFHS HRQHTCLDIS PYGNEQVSRI
ACTSCEDNRI LPTASDAMVA FINQTSNIMK NRNFYYGFCK SSELLKLSTN QPPIFQIYYL
LHAANHDIVP FMHAENGRLH MHVIFENSDV HIPCDCITQM LTAAREDYSV TLNIVRDHVV
ISVLCHAVSA SSVKIDVTIL QRKIDEMDIP NDVSESFERY KELIQELCQS SGNNLYEEAT
SSYAIRSPLT ASPLHVVSTN GCGPSSSSQS TPPHLHPPSQ ATQPHHYSHH QSQSQQHHHR
PQSPPPPLFL NSIRAP
