NEC1_HCMVA
ID NEC1_HCMVA Reviewed; 376 AA.
AC P16794; Q7M6N0;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3029980; DOI=10.1016/0042-6822(87)90282-0;
RA Kouzarides T., Bankier A.T., Satchwell S.C., Weston K.M., Tomlinson P.,
RA Barrell B.G.;
RT "Large-scale rearrangement of homologous regions in the genomes of HCMV and
RT EBV.";
RL Virology 157:397-413(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [3]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11961254; DOI=10.1099/0022-1317-83-5-1005;
RA Dal Monte P., Pignatelli S., Zini N., Maraldi N.M., Perret E.,
RA Prevost M.C., Landini M.P.;
RT "Analysis of intracellular and intraviral localization of the human
RT cytomegalovirus UL53 protein.";
RL J. Gen. Virol. 83:1005-1012(2002).
RN [6]
RP INTERACTION WITH UL50.
RX PubMed=17005637; DOI=10.1128/jvi.01662-06;
RA Schnee M., Ruzsics Z., Bubeck A., Koszinowski U.H.;
RT "Common and specific properties of herpesvirus UL34/UL31 protein family
RT members revealed by protein complementation assay.";
RL J. Virol. 80:11658-11666(2006).
RN [7]
RP FUNCTION, PHOSPHORYLATION AT SER-19, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF SER-19.
RX PubMed=25339763; DOI=10.1128/jvi.02426-14;
RA Sharma M., Bender B.J., Kamil J.P., Lye M.F., Pesola J.M., Reim N.I.,
RA Hogle J.M., Coen D.M.;
RT "Human cytomegalovirus UL97 phosphorylates the viral nuclear egress
RT complex.";
RL J. Virol. 89:523-534(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 4-168, INTERACTION WITH NEC2,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-79; CYS-122; CYS-125 AND
RP HIS-211.
RX PubMed=26511021; DOI=10.15252/embj.201592651;
RA Lye M.F., Sharma M., El Omari K., Filman D.J., Schuermann J.P., Hogle J.M.,
RA Coen D.M.;
RT "Unexpected features and mechanism of heterodimer formation of a
RT herpesvirus nuclear egress complex.";
RL EMBO J. 34:2937-2952(2015).
RN [9] {ECO:0007744|PDB:6T3X}
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 1-171, INTERACTION WITH NEC2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=31980459; DOI=10.1074/jbc.ra119.011546;
RA Muller Y.A., Hage S., Alkhashrom S., Hollriegl T., Weigert S., Dolles S.,
RA Hof K., Walzer S.A., Egerer-Sieber C., Conrad M., Holst S., Losing J.,
RA Sonntag E., Sticht H., Eichler J., Marschall M.;
RT "High-resolution crystal structures of two prototypical beta- and gamma-
RT herpesviral nuclear egress complexes unravel the determinants of subfamily
RT specificity.";
RL J. Biol. Chem. 295:3189-3201(2020).
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 ECO:0000269|PubMed:25339763}.
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:26511021,
CC ECO:0000269|PubMed:31980459}.
CC -!- SUBCELLULAR LOCATION: Host nucleus inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_04023, ECO:0000269|PubMed:11961254,
CC ECO:0000269|PubMed:25339763, ECO:0000269|PubMed:26511021,
CC ECO:0000269|PubMed:31980459}. Note=Remains attached to the nucleus
CC inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-
CC Rule:MF_04023, ECO:0000269|PubMed:26511021}.
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 (PubMed:25339763). {ECO:0000255|HAMAP-Rule:MF_04023,
CC ECO:0000269|PubMed:25339763}.
CC -!- SIMILARITY: Belongs to the herpesviridae NEC1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04023}.
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DR EMBL; M17209; AAA46007.1; -; Genomic_DNA.
DR EMBL; X17403; CAA35412.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00158.1; -; Genomic_DNA.
DR PIR; S09816; QQBEW2.
DR PDB; 5DOB; X-ray; 2.47 A; A=61-289.
DR PDB; 5DOC; X-ray; 1.94 A; A/B=88-290.
DR PDB; 5DOE; X-ray; 3.00 A; B=72-290.
DR PDB; 6T3X; X-ray; 1.48 A; A/C=59-87.
DR PDBsum; 5DOB; -.
DR PDBsum; 5DOC; -.
DR PDBsum; 5DOE; -.
DR PDBsum; 6T3X; -.
DR SMR; P16794; -.
DR PRIDE; P16794; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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 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_0000116013"
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:0000269|PubMed:25339763"
FT MUTAGEN 19
FT /note="S->A: No effect on replication kinetics."
FT /evidence="ECO:0000269|PubMed:25339763"
FT MUTAGEN 79
FT /note="L->A: Loss of interaction and co-localization with
FT NEC1."
FT /evidence="ECO:0000269|PubMed:25339763"
FT MUTAGEN 122
FT /note="C->S: Partial relocalization in the host
FT nucleoplasm."
FT /evidence="ECO:0000269|PubMed:31980459"
FT MUTAGEN 125
FT /note="C->S: Partial relocalization in the host
FT nucleoplasm."
FT /evidence="ECO:0000269|PubMed:31980459"
FT MUTAGEN 211
FT /note="H->A: Partial relocalization in the host
FT nucleoplasm."
FT /evidence="ECO:0000269|PubMed:31980459"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:6T3X"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:6T3X"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5DOB"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:5DOC"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:5DOC"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:5DOC"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:5DOC"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:5DOC"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:5DOC"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5DOC"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:5DOC"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:5DOC"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:5DOC"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:5DOC"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:5DOC"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:5DOC"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:5DOC"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:5DOC"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:5DOC"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:5DOC"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:5DOC"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:5DOC"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:5DOC"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:5DOC"
FT HELIX 281..288
FT /evidence="ECO:0007829|PDB:5DOC"
SQ SEQUENCE 376 AA; 42313 MW; BF44D5F8DE2B88B9 CRC64;
MSSVSGVRTP RERRSALRSL LRKRRQRELA SKVASTVNGA TSANNHGEPP SPADARPRLT
LHDLHDIFRE HPELELKYLN MMKMAITGKE SICLPFNFHS HRQHTCLDIS PYGNEQVSRI
ACTSCEDNRI LPTASDAMVA FINQTSNIMK NRNFYYGFCK SSELLKLSTN QPPIFQIYYL
LHAANHDIVP FMHAEDGRLH MHVIFENPDV HIPCDCITQM LTAAREDYSV TLNIVRDHVV
ISVLCHAVSA SSVKIDVTIL QRKIDEMDIP NDVSESFERY KELIQELCQS SGNNLYEEAT
SSYAIRSPLT ASPLHVVSTN GCGPSSSSQS TPPHLHPPSQ ATQPHHYSHH QSQSQQHHHR
PQSPPPPLFL NSIRAP
