ID   EV45_HHV23              Reviewed;         172 AA.
AC   P06483;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   02-JUN-2021, entry version 68.
DE   RecName: Full=Envelope protein UL45;
DE   AltName: Full=18 kDa protein;
GN   ORFNames=UL45;
OS   Human herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10313;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2982036; DOI=10.1128/jvi.53.2.561-569.1985;
RA   Swain M.A., Peet R.W., Galloway D.A.;
RT   "Characterization of the gene encoding herpes simplex virus type 2
RT   glycoprotein C and comparison with the type 1 counterpart.";
RL   J. Virol. 53:561-569(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-144.
RX   PubMed=6090692; DOI=10.1128/jvi.52.1.154-163.1984;
RA   Dowbenko D.J., Lasky L.A.;
RT   "Extensive homology between the herpes simplex virus type 2 glycoprotein F
RT   gene and the herpes simplex virus type 1 glycoprotein C gene.";
RL   J. Virol. 52:154-163(1984).
RN   [3]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=9557736; DOI=10.1128/jvi.72.5.4430-4433.1998;
RA   Cockrell A.S., Muggeridge M.I.;
RT   "Herpes simplex virus 2 UL45 is a type II membrane protein.";
RL   J. Virol. 72:4430-4433(1998).
CC   -!- FUNCTION: Important virulence factor of HSV neurotropism. Seems to be
CC       required for glycoprotein B-induced fusion. Dispensable for growth in
CC       vitro (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:9557736};
CC       Single-pass type II membrane protein {ECO:0000269|PubMed:9557736}.
CC       Note=In transfected cells, it is retained within the ER. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the herpesviridae HHV-1 UL45 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X01996; CAA26026.1; -; Genomic_DNA.
DR   EMBL; X01456; CAA25688.1; -; Genomic_DNA.
DR   EMBL; M10053; AAA66444.1; -; Genomic_DNA.
DR   RefSeq; YP_009137197.1; NC_001798.2.
DR   DNASU; 1487332; -.
DR   GeneID; 1487332; -.
DR   KEGG; vg:1487332; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR018002; Herpes_UL45.
DR   PIRSF; PIRSF003509; Herpes_UL45; 1.
PE   1: Evidence at protein level;
KW   Membrane; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Virion.
FT   CHAIN           1..172
FT                   /note="Envelope protein UL45"
FT                   /id="PRO_0000116089"
FT   TOPO_DOM        1..27
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..172
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        16..18
FT                   /note="AAS -> RPP (in Ref. 2; CAA25688)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="S -> C (in Ref. 2; CAA25688)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   172 AA;  18148 MW;  8EAACA9FE5D6F8C0 CRC64;
     MAFRASGPAY QPLAPAASPA RARVPAVAWI GVGAIVGAFA LVAALVLVPP RSSWGLSPCD
     SGWQEFNAGC VAWDPTPVEH EQAVGGCSAP ATLIPRAAAK HLAALTRVQA ERSSGYWWVN
     GDGIRTCLRL VDSVSGIDEF CEELAIRICY YPRSPGGFVR FVTSIRNALG LP