NEC2_HCMVA
ID NEC2_HCMVA Reviewed; 397 AA.
AC P16791; Q7M6N3;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 02-JUN-2021, entry version 78.
DE RecName: Full=Nuclear egress protein 2 {ECO:0000255|HAMAP-Rule:MF_04024};
GN Name=NEC2 {ECO:0000255|HAMAP-Rule:MF_04024}; OrderedLocusNames=UL50;
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 IDENTIFICATION.
RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT HCMV proteome.";
RL J. Virol. 78:10960-10966(2004).
RN [6]
RP ERRATUM OF PUBMED:15452216.
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RL J. Virol. 78:13395-13395(2004).
RN [7]
RP INTERACTION WITH UL53.
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 [8]
RP FUNCTION, PHOSPHORYLATION AT SER-216, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF SER-216.
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 4-168, INTERACTION WITH NEC1, AND
RP SUBCELLULAR LOCATION.
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 1-171, INTERACTION WITH NEC1, 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_04024,
CC ECO:0000269|PubMed:25339763}.
CC -!- SUBUNIT: Forms a heterohexameric complex with NEC1. {ECO:0000255|HAMAP-
CC Rule:MF_04024, ECO:0000269|PubMed:26511021,
CC ECO:0000269|PubMed:31980459}.
CC -!- SUBCELLULAR LOCATION: Host nucleus inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_04024, ECO:0000269|PubMed:25339763,
CC ECO:0000269|PubMed:26511021, ECO:0000269|PubMed:31980459}; Single-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_04024}. Note=Localizes also
CC at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-
CC Rule:MF_04024}.
CC -!- PTM: Phosphorylated (By similarity). Phosphorylation by viral kinase
CC UL97 at Ser-216 plays an important role for correct viral nuclear
CC egress complex (NEC) localization (PubMed:25339763).
CC {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:25339763}.
CC -!- SIMILARITY: Belongs to the herpesviridae NEC2 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04024}.
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DR EMBL; M17209; AAA46004.1; -; Genomic_DNA.
DR EMBL; X17403; CAA35409.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00155.1; -; Genomic_DNA.
DR PIR; S09813; S09813.
DR PDB; 5DOB; X-ray; 2.47 A; B=4-168.
DR PDB; 6T3X; X-ray; 1.48 A; A/C=1-171.
DR PDBsum; 5DOB; -.
DR PDBsum; 6T3X; -.
DR SMR; P16791; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
DR GO; GO:0044201; C:host cell nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR HAMAP; MF_04024; HSV_NEC2; 1.
DR InterPro; IPR007626; Herpesvirus_viron_egress-type.
DR Pfam; PF04541; Herpes_U34; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host membrane; Host nucleus; Late protein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..397
FT /note="Nuclear egress protein 2"
FT /id="PRO_0000116034"
FT TOPO_DOM 1..358
FT /note="Perinuclear space"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT TRANSMEM 359..381
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT TOPO_DOM 382..397
FT /note="Nuclear"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT REGION 205..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25339763"
FT HELIX 1..19
FT /evidence="ECO:0007829|PDB:6T3X"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:6T3X"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:6T3X"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6T3X"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:6T3X"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6T3X"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:6T3X"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6T3X"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:6T3X"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6T3X"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:6T3X"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5DOB"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:6T3X"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:5DOB"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:6T3X"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:6T3X"
SQ SEQUENCE 397 AA; 42901 MW; 08DC5FA358E8A473 CRC64;
MEMNKVLHQD LVQATRRILK LGPSELRVTD AGLICKNPNY SVCDAMLKTD TVYCVEYLLS
YWESRTDHVP CFIFKNTGCA VSLCCFVRAP VKLVSPARHV GEFNVLKVNE SLIVTLKDIE
EIKPSAYGVL TKCVVRKSNS ASVFNIELIA FGPENEGEYE NLLRELYAKK AASTSLAVRN
HVTVSSHSGS GPSLWRARMS AALTRTAGKR SSRTASPPPP PRHPSCSPTM VAAGGAAAGP
RPPPPPMAAG SWRLCRCEAC MGRCGCASEG DADEEEEELL ALAGEGKAAA AAAGQDVGGS
ARRPLEEHVS RRRGVSTHHR HPPSPPCAPS LERTGYRWAP SSWWRARSGP SRPQSGPWLP
ARFATLGPLV LALLLVLALL WRGHGQSSSP TRSAHRD
