ID A1Z0P5_HHV1 Unreviewed; 904 AA. AC A1Z0P5; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 33. DE SubName: Full=Glycoprotein B {ECO:0000313|EMBL:ABM52970.1}; GN Name=UL27 {ECO:0000313|EMBL:ABM52970.1}; OS Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus; OC Simplexvirus humanalpha1. OX NCBI_TaxID=10298 {ECO:0000313|EMBL:ABM52970.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:ABM52970.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KOSc {ECO:0000313|EMBL:ABM52970.1}; RX PubMed=17604805; DOI=10.1016/j.virol.2007.05.040; RA Ekblad M., Adamiak B., Bergefall K., Nenonen H., Roth A., Bergstrom T., RA Ferro V., Trybala E.; RT "Molecular basis for resistance of herpes simplex virus type 1 mutants to RT the sulfated oligosaccharide inhibitor PI-88."; RL Virology 367:244-252(2007). 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; EF157309; ABM52970.1; -; Genomic_DNA. DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule. DR Gene3D; 1.20.5.1890; -; 1. DR Gene3D; 2.30.29.100; -; 1. DR Gene3D; 2.30.30.1230; -; 1. DR Gene3D; 6.10.250.3280; -; 1. DR HAMAP; MF_04032; HSV_GB; 1. DR InterPro; IPR035377; Glycoprot_B_PH1. DR InterPro; IPR035381; Glycoprot_B_PH2. DR InterPro; IPR038631; Glycoprot_B_PH2_sf. DR InterPro; IPR000234; Herpes_Glycoprot_B. DR Pfam; PF17416; Glycoprot_B_PH1; 1. DR Pfam; PF17417; Glycoprot_B_PH2; 1. DR Pfam; PF00606; Glycoprotein_B; 1. DR SUPFAM; SSF161008; Viral glycoprotein ectodomain-like; 1. PE 3: Inferred from homology; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511}; KW Host endosome {ECO:0000256|ARBA:ARBA00023046}; KW Host Golgi apparatus {ECO:0000256|ARBA:ARBA00022812}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804}; KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879}; KW Virion {ECO:0000256|ARBA:ARBA00022844}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}. FT TRANSMEM 752..771 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 777..798 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 153..364 FT /note="Herpesvirus Glycoprotein B PH-like" FT /evidence="ECO:0000259|Pfam:PF17416" FT DOMAIN 366..463 FT /note="Herpesvirus Glycoprotein B PH-like" FT /evidence="ECO:0000259|Pfam:PF17417" FT REGION 31..88 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 470..492 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 883..904 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 904 AA; 100311 MW; B8FF576DF106A380 CRC64; MHQGAPSWGR RWFVVWALLG LTLGVLVASA APSSPGTPGV AAATQAANGG PANPAPPALG AAPTGDPKPK KNKKPKNPTP PRPAGDNATV AAGHATLREH LRDIKAENTD ANFYVCPPPT GATVVQFEQP RRCPTRPEGQ NYTEGIAVVF KENIAPYKFK ATMYYKDVTV SQVWFGHRYS QFMGIFEDRA PVPFEEVIDK INAKGVCRST AKYVRNNLET TAFHRDDHET DMELKPANAA TRTSRGWHTT DLKYNPSRVE AFHRYGTTVN CIVKEVDARS VYPYDEFVLA TGDFVYMSPF YGYREGSHTE HTSYAADRFK QVDGFYARDL TTKARATAPT TRNLLTTPKF TVAWDWVPKR PSVCTMTKWQ EVDEMLRSEY GGSFRFSSDA ISTTFTTNLT EYPLSRVDLG DCIGKDARDA MDRIFARRYN ATHIKVGQPQ YYLANGGFLI AYQPLLSNTL AELYVREHLR EQSRKPPNPT PPPPGASANA SVERIKTTSS IEFARLQFTY NHIQRHVNDM LGRVAIAWCE LQNHELTLWN EARKLNPNAI ASVTVGRRVS ARMLGDVMAV STCVPVAADN VIVQNSMRIS SRPGACYSRP LVSFRYEDQG PLVEGQLGEN NELRLTRDAI EPCTVGHRRY FTFGGGYVYF EEYAYSHQLS RADITTVSTF IDLNITMLED HEFVPLEVYT RHEIKDSGLL DYTEVQRRNQ LHDLRFADID TVIHADANAA MFAGLGAFFE GMGDLGRAVG KVVMGIVGGV VSAVSGVSSF MSNPFGALAV GLLVLAGLAA AFFAFRYVMR LQSNPMKALY PLTTKELKNP TNPDASGEGE EGGDFDEAKL AEAREMIRYM ALVSAMERTE HKAKKKGTSA LLSAKVTDMV MRKRRNTNYT QVPNKDGDAD EDDL //