ID   PORTL_HHV11             Reviewed;         676 AA.
AC   P10190;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04012};
GN   Name=UL6;
OS   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1; Human herpesvirus 1.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RX   PubMed=2826807; DOI=10.1128/jvi.62.2.444-453.1988;
RA   McGeoch D.J., Dalrymple M.A., Dolan A., McNab D., Perry L.J., Taylor P.,
RA   Challberg M.D.;
RT   "Structures of herpes simplex virus type 1 genes required for replication
RT   of virus DNA.";
RL   J. Virol. 62:444-453(1988).
RN   [3]
RP   FUNCTION.
RX   PubMed=11602732; DOI=10.1128/jvi.75.22.10923-10932.2001;
RA   Newcomb W.W., Juhas R.M., Thomsen D.R., Homa F.L., Burch A.D., Weller S.K.,
RA   Brown J.C.;
RT   "The UL6 gene product forms the portal for entry of DNA into the herpes
RT   simplex virus capsid.";
RL   J. Virol. 75:10923-10932(2001).
RN   [4]
RP   INTERACTION WITH UL15 AND UL28, AND SUBCELLULAR LOCATION.
RX   PubMed=12743292; DOI=10.1128/jvi.77.11.6351-6358.2003;
RA   White C.A., Stow N.D., Patel A.H., Hughes M., Preston V.G.;
RT   "Herpes simplex virus type 1 portal protein UL6 interacts with the putative
RT   terminase subunits UL15 and UL28.";
RL   J. Virol. 77:6351-6358(2003).
RN   [5]
RP   HOMODODECAMERIZATION.
RX   PubMed=15507654; DOI=10.1128/jvi.78.22.12668-12671.2004;
RA   Trus B.L., Cheng N., Newcomb W.W., Homa F.L., Brown J.C., Steven A.C.;
RT   "Structure and polymorphism of the UL6 portal protein of herpes simplex
RT   virus type 1.";
RL   J. Virol. 78:12668-12671(2004).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16920825; DOI=10.1128/jvi.01364-06;
RA   Wills E., Scholtes L., Baines J.D.;
RT   "Herpes simplex virus 1 DNA packaging proteins encoded by UL6, UL15, UL17,
RT   UL28, and UL33 are located on the external surface of the viral capsid.";
RL   J. Virol. 80:10894-10899(2006).
RN   [7]
RP   INTERACTION WITH TRM1 AND TRM3.
RX   PubMed=19224991; DOI=10.1128/jvi.00026-09;
RA   Yang K., Wills E., Baines J.D.;
RT   "The putative leucine zipper of the UL6-encoded portal protein of herpes
RT   simplex virus 1 is necessary for interaction with pUL15 and pUL28 and their
RT   association with capsids.";
RL   J. Virol. 83:4557-4564(2009).
RN   [8]
RP   MUTAGENESIS OF CYS-145; CYS-166 AND CYS-254.
RX   PubMed=21593161; DOI=10.1128/jvi.00123-11;
RA   Albright B.S., Nellissery J., Szczepaniak R., Weller S.K.;
RT   "Disulfide bond formation in the herpes simplex virus 1 UL6 protein is
RT   required for portal ring formation and genome encapsidation.";
RL   J. Virol. 85:8616-8624(2011).
CC   -!- FUNCTION: Forms a portal in the viral capsid through which viral DNA is
CC       translocated during DNA packaging. Assembles as a dodecamer at a single
CC       fivefold axe of the T=16 icosahedric capsid. Binds to the molecular
CC       motor that translocates the viral DNA, termed terminase.
CC       {ECO:0000255|HAMAP-Rule:MF_04012, ECO:0000269|PubMed:11602732}.
CC   -!- SUBUNIT: Homododecamerizes. Interacts with terminase subunits TRM1 and
CC       TRM3. {ECO:0000255|HAMAP-Rule:MF_04012, ECO:0000269|PubMed:12743292,
CC       ECO:0000269|PubMed:19224991}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04012,
CC       ECO:0000269|PubMed:16920825}. Host nucleus {ECO:0000255|HAMAP-
CC       Rule:MF_04012, ECO:0000269|PubMed:12743292}.
CC   -!- SIMILARITY: Belongs to the herpesviridae portal protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04012}.
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DR   EMBL; X14112; CAA32342.1; -; Genomic_DNA.
DR   EMBL; AH002360; AAA45818.2; -; Genomic_DNA.
DR   PIR; F28133; WMBEX6.
DR   SMR; P10190; -.
DR   BioGRID; 971454; 1.
DR   IntAct; P10190; 2.
DR   MINT; P10190; -.
DR   TCDB; 1.W.4.1.1; the viral portal protein 4 (ppp4) family.
DR   Proteomes; UP000009294; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR   GO; GO:0051276; P:chromosome organization; IEA:UniProtKB-UniRule.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04012; HSV_PORTL; 1.
DR   InterPro; IPR002660; Herpes_Portal.
DR   Pfam; PF01763; Herpes_UL6; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Host nucleus; Reference proteome; Viral genome packaging;
KW   Viral release from host cell; Virion.
FT   CHAIN           1..676
FT                   /note="Portal protein"
FT                   /id="PRO_0000115903"
FT   REGION          383..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..443
FT                   /note="Putative leucine zipper motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04012,
FT                   ECO:0000305|PubMed:19224991"
FT   REGION          627..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        166
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04012,
FT                   ECO:0000269|PubMed:21593161"
FT   DISULFID        254
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04012,
FT                   ECO:0000269|PubMed:21593161"
FT   MUTAGEN         145
FT                   /note="C->A: Complete loss of nuclear localization."
FT                   /evidence="ECO:0000269|PubMed:21593161"
FT   MUTAGEN         166
FT                   /note="C->A: Complete loss of portal ring formation."
FT                   /evidence="ECO:0000269|PubMed:21593161"
FT   MUTAGEN         254
FT                   /note="C->A: Complete loss of portal ring formation."
FT                   /evidence="ECO:0000269|PubMed:21593161"
SQ   SEQUENCE   676 AA;  74092 MW;  8CF9D73C6313FAE9 CRC64;
     MTAPRSRAPT TRARGDTEAL CSPEDGWVKV HPSPGTMLFR EILHGQLGYT EGQGVYNVVR
     SSEATTRQLQ AAIFHALLNA TTYRDLEADW LGHVAARGLQ PQRLVRRYRN AREADIAGVA
     ERVFDTWRNT LRTTLLDFAH GLVACFAPGG PSGPSSFPKY IDWLTCLGLV PILRKRQEGG
     VTQGLRAFLK QHPLTRQLAT VAEAAERAGP GFFELALAFD STRVADYDRV YIYYNHRRGD
     WLVRDPISGQ RGECLVLWPP LWTGDRLVFD SPVQRLFPEI VACHSLREHA HVCRLRNTAS
     VKVLLGRKSD SERGVAGAAR VVNKVLGEDD ETKAGSAASR LVRLIINMKG MRHVGDINDT
     VRSYLDEAGG HLIDAPAVDG TLPGFGKGGN SRGSAGQDQG GRAPQLRQAF RTAVVNNING
     VLEGYINNLF GTIERLRETN AGLATQLQER DRELRRATAG ALERQQRAAD LAAESVTGGC
     GSRPAGADLL RADYDIIDVS KSMDDDTYVA NSFQHPYIPS YAQDLERLSR LWEHELVRCF
     KILCHRNNQG QETSISYSSG AIAAFVAPYF ESVLRAPRVG APITGSDVIL GEEELWDAVF
     KKTRLQTYLT DIAALFVADV QHAALPPPPS PVGADFRPGA SPRGRSRSRS PGRTARGAPD
     QGGGIGHRDG RRDGRR
//