NEC2_HCMVM
ID NEC2_HCMVM Reviewed; 398 AA.
AC Q6SW81; D2K3L8;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 57.
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 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].
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 NEC1.
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_04024}.
CC -!- SUBUNIT: Forms a heterohexameric complex with NEC1. {ECO:0000255|HAMAP-
CC Rule:MF_04024, ECO:0000269|PubMed:26432641}.
CC -!- SUBCELLULAR LOCATION: Host nucleus inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04024}. Note=Localizes also at the transient membrane of
CC perinuclear virions. {ECO:0000255|HAMAP-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 (By similarity).
CC {ECO:0000250|UniProtKB:P16791, ECO:0000255|HAMAP-Rule:MF_04024}.
CC -!- SIMILARITY: Belongs to the herpesviridae NEC2 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04024}.
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DR EMBL; AY446894; AAR31616.1; -; Genomic_DNA.
DR RefSeq; YP_081509.1; NC_006273.2.
DR PDB; 5D5N; X-ray; 2.44 A; A=1-175.
DR PDBsum; 5D5N; -.
DR SMR; Q6SW81; -.
DR PRIDE; Q6SW81; -.
DR DNASU; 3077439; -.
DR GeneID; 3077439; -.
DR KEGG; vg:3077439; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019033; C:viral tegument; TAS:Reactome.
DR GO; GO:0046765; P:viral budding from nuclear membrane; IDA:UniProtKB.
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..398
FT /note="Nuclear egress protein 2"
FT /id="PRO_0000416719"
FT TOPO_DOM 1..359
FT /note="Perinuclear space"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT TRANSMEM 360..382
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT TOPO_DOM 383..398
FT /note="Nuclear"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04024"
FT REGION 202..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16791"
FT HELIX 5..19
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:5D5N"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:5D5N"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:5D5N"
SQ SEQUENCE 398 AA; 43052 MW; 367FF459968AD468 CRC64;
MEMNKVLHQD LVQATRRILK LGPSELRVTD AGLICKNPNY SVCDAMLKTD TVYCVEYLLS
YWESRTDHVP CFIFKNTGCA VSLCCFVRAP VKLVSPARHV GEFNVLKVNE SLIVTLKDIE
EIKPSAYGVL TKCVVRKSNS ASVFNIELIA FGPENEGEYE NLLRELYAKK AASTSLAVRN
HVTVSSHSGS GPSLWRARMS AALTRTAGKR SPRTASPPPP PPRHPSCSPT MVAAGGAAAG
PRPPPPPMAA GSWRLCRCEA CMGRCGCASE GDADEEEEEL LALAGEGKAA AAAAGQDIGG
SARRPLEEHV SRRRGVSTHH RHPPSPPCTP SLERTGYRWA PSSWWRARSG PSRPQSGPWL
PARFATLGPL VLALLLVLAL LWRGHGQSSS PTRSAHRD
