ID   UL132_HCMVT             Reviewed;         270 AA.
AC   P69339; P16774; Q7M6R9;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Envelope glycoprotein UL132;
DE            Short=L3;
DE   Flags: Precursor;
GN   Name=UL132;
OS   Human cytomegalovirus (strain Towne) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=10363;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8109157; DOI=10.1016/0168-1702(93)90092-2;
RA   Wang J., Razzaque A.;
RT   "Mapping and DNA sequence analysis of the cytomegalovirus transforming
RT   domain III (mtrIII).";
RL   Virus Res. 30:221-238(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [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).
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
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DR   EMBL; L19942; AAA75382.1; -; Genomic_DNA.
DR   EMBL; FJ616285; AAR31454.1; -; Genomic_DNA.
DR   PIR; S09898; S09898.
DR   Proteomes; UP000006907; Genome.
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; IPR021023; UL132.
DR   Pfam; PF11359; gpUL132; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Virion.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..270
FT                   /note="Envelope glycoprotein UL132"
FT                   /id="PRO_0000037460"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          33..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   270 AA;  29972 MW;  0B641DF447C4F8E4 CRC64;
     MPAPRGLLRA TFLVLVAFGL LLHIDFSDAT NMTSSTNVPT STSSRNTVES TTSSEPTTET
     NMTTARESSV HDARNDEIMK VLAILFYIVT GTSIFSFIAV LIAVVYSSCC KHPGRFRFAD
     EEAVNLLDDT DDSGGSSPFG SGSRRGSQIP AGFCSSSPYQ RLETRDWDEE EEASAARERM
     KHDPENVIYF RKDGNLDTSF VNPNYGRGSP LTIESHLSDN EEDPIRYYVS VYDELTASEM
     EEPSNSTSWQ IPKLMKVAMQ PVSLRDPEYD