ID   CEP1_HHV11              Reviewed;         296 AA.
AC   P10191;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-JUN-2021, entry version 66.
DE   RecName: Full=Cytoplasmic envelopment protein 1 {ECO:0000255|HAMAP-Rule:MF_04038};
GN   Name=UL7;
OS   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA   Perry L.J., Scott J.E., Taylor P.;
RT   "The complete DNA sequence of the long unique region in the genome of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:1531-1574(1988).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22158881; DOI=10.1099/vir.0.039776-0;
RA   Loret S., Lippe R.;
RT   "Biochemical analysis of infected cell polypeptide (ICP)0, ICP4, UL7 and
RT   UL23 incorporated into extracellular herpes simplex virus type 1 virions.";
RL   J. Gen. Virol. 93:624-634(2012).
RN   [3]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=25552711; DOI=10.1128/jvi.02799-14;
RA   Roller R.J., Fetters R.;
RT   "The HSV-1 UL51 protein interacts with the UL7 protein and plays a role in
RT   its recruitment into the virion.";
RL   J. Virol. 89:3112-3122(2015).
CC   -!- FUNCTION: Plays a critical role in cytoplasmic virus egress.
CC       Participates in the final step of tegumentation and envelope
CC       acquisition within the host cytoplasm. {ECO:0000255|HAMAP-
CC       Rule:MF_04038}.
CC   -!- SUBUNIT: Interacts with UL51; this interaction allows incorporation of
CC       UL7 within the virion. {ECO:0000269|PubMed:25552711}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04038,
CC       ECO:0000269|PubMed:22158881, ECO:0000269|PubMed:25552711}. Virion
CC       tegument {ECO:0000255|HAMAP-Rule:MF_04038,
CC       ECO:0000269|PubMed:22158881}. Host cytoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_04038, ECO:0000269|PubMed:25552711}. Host Golgi apparatus
CC       {ECO:0000255|HAMAP-Rule:MF_04038}.
CC   -!- SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment
CC       protein 1 family. {ECO:0000255|HAMAP-Rule:MF_04038}.
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DR   EMBL; X14112; CAA32343.1; -; Genomic_DNA.
DR   PIR; G28133; WMBEX7.
DR   PDB; 6T5A; X-ray; 1.83 A; E/F/G/H=1-296.
DR   PDBsum; 6T5A; -.
DR   SMR; P10191; -.
DR   BioGRID; 971455; 1.
DR   PRIDE; P10191; -.
DR   Proteomes; UP000009294; Genome.
DR   GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   HAMAP; MF_04038; HSV_CEP1; 1.
DR   InterPro; IPR002600; Herpes_UL7.
DR   Pfam; PF01677; Herpes_UL7; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Host cytoplasm; Host Golgi apparatus; Reference proteome;
KW   Virion; Virion tegument.
FT   CHAIN           1..296
FT                   /note="Cytoplasmic envelopment protein 1"
FT                   /id="PRO_0000115914"
FT   HELIX           12..22
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           26..34
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   STRAND          37..46
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   STRAND          59..65
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           86..94
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   STRAND          99..108
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   STRAND          114..119
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           121..124
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           136..150
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           158..174
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           180..199
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           212..220
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   STRAND          222..224
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           227..230
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   TURN            231..233
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           261..267
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           269..280
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   HELIX           288..290
FT                   /evidence="ECO:0007829|PDB:6T5A"
FT   STRAND          294..296
FT                   /evidence="ECO:0007829|PDB:6T5A"
SQ   SEQUENCE   296 AA;  33059 MW;  3A32E059B7DA3E92 CRC64;
     MAAATADDEG SAATILKQAI AGDRSLVEAA EAISQQTLLR LACEVRQVGD RQPRFTATSI
     ARVDVAPGCR LRFVLDGSPE DAYVTSEDYF KRCCGQSSYR GFAVAVLTAN EDHVHSLAVP
     PLVLLHRFSL FNPRDLLDFE LACLLMYLEN CPRSHATPST FAKVLAWLGV AGRRTSPFER
     VRCLFLRSCH WVLNTLMFMV YVKPFDDEFV LPHWYMARYL LANNPPPVLS ALFCATPTSS
     SFRLPGPPPR SDCVAYNPAG IMGSCWASEE VRAPLVYWWL SETPKRQTSS LFYQFC