ID UL56_HHV11 Reviewed; 234 AA. AC P10240; O09801; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 16-OCT-2019, sequence version 2. DT 24-JAN-2024, entry version 72. DE RecName: Full=Protein UL56; GN Name=UL56; 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]. RX PubMed=2846760; DOI=10.1099/0022-1317-69-11-2831; RA Perry L.J., McGeoch D.J.; RT "The DNA sequences of the long repeat region and adjoining parts of the RT long unique region in the genome of herpes simplex virus type 1."; RL J. Gen. Virol. 69:2831-2846(1988). RN [3] RP SEQUENCE REVISION. RX PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057; RA McGeoch D.J., Cunningham C., McIntyre G., Dolan A.; RT "Comparative sequence analysis of the long repeat regions and adjoining RT parts of the long unique regions in the genomes of herpes simplex viruses RT types 1 and 2."; RL J. Gen. Virol. 72:3057-3075(1991). RN [4] RP INTERACTION WITH HOST ITCH, DOMAIN, AND MUTAGENESIS OF TYR-26; TYR-52 AND RP TYR-147. RX PubMed=29535361; DOI=10.1038/s41598-018-22682-2; RA Koshizuka T., Kobayashi T., Ishioka K., Suzutani T.; RT "Herpesviruses possess conserved proteins for interaction with Nedd4 family RT ubiquitin E3 ligases."; RL Sci. Rep. 8:4447-4447(2018). CC -!- FUNCTION: Plays a role in the transport and release of virions form the CC host cytoplasm to the extracellular space. Relocalizes host NEDD4, a CC cytosolic E3 ligase, to cytoplasmic vesicles. CC {ECO:0000250|UniProtKB:P28282}. CC -!- SUBUNIT: Interacts with host ITCH; this interaction induces CC ubiquitination and probably degradation of ITCH (PubMed:29535361). CC Interacts with host NEDD4; this interaction increases NEDD4 CC ubiquitination (By similarity). Interacts with UL11 (By similarity). CC {ECO:0000250|UniProtKB:P28282, ECO:0000269|PubMed:29535361}. CC -!- SUBCELLULAR LOCATION: Host Golgi apparatus membrane CC {ECO:0000250|UniProtKB:P28282}; Single-pass membrane protein CC {ECO:0000255}. CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs CC essential for viral particle budding. They recruit proteins of the host CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or CC ESCRT-associated proteins. UL56 contains three L domains: the PPXY CC motifs which are involved in the interaction with ITCH, a member of the CC NEDD4 family. {ECO:0000269|PubMed:29535361}. CC -!- SIMILARITY: Belongs to the herpesviridae UL56 family. {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; X14112; CAA32292.1; -; Genomic_DNA. DR PIR; B30090; WMBEY6. DR RefSeq; YP_009137132.1; NC_001806.2. DR SMR; P10240; -. DR BioGRID; 971453; 2. DR DNASU; 2703428; -. DR GeneID; 2703428; -. DR KEGG; vg:2703428; -. DR Proteomes; UP000009294; Genome. DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR InterPro; IPR007620; Herpes_UL56. DR Pfam; PF04534; Herpes_UL56; 1. PE 1: Evidence at protein level; KW Host Golgi apparatus; Host membrane; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1..234 FT /note="Protein UL56" FT /id="PRO_0000116123" FT TRANSMEM 211..231 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..104 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 158..182 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 23..26 FT /note="PPXY motif" FT /evidence="ECO:0000269|PubMed:29535361" FT MOTIF 49..52 FT /note="PPXY motif" FT /evidence="ECO:0000269|PubMed:29535361" FT MOTIF 144..147 FT /note="PPXY motif" FT /evidence="ECO:0000269|PubMed:29535361" FT COMPBIAS 43..58 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 82..97 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 158..179 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MUTAGEN 26 FT /note="Y->A: Complete loss of interaction with host ITCH; FT when associated with A-52 and A-147." FT /evidence="ECO:0000269|PubMed:29535361" FT MUTAGEN 52 FT /note="Y->A: Complete loss of interaction with host ITCH; FT when associated with A-26 and A-147." FT /evidence="ECO:0000269|PubMed:29535361" FT MUTAGEN 147 FT /note="Y->A: Complete loss of interaction with host ITCH; FT when associated with A-26 and A-52." FT /evidence="ECO:0000269|PubMed:29535361" SQ SEQUENCE 234 AA; 25321 MW; 9F58D7D18ABFA5A7 CRC64; MASEAAQPDA GLWSAGNAFA DPPPPYDSLS GRNEGPFVVI DLDTPTDPPP PYSAGPLLSV PIPPTSSGEG EASERGRSRQ AAQRAARRAR RRAERRAQRR SFGPGGLLAT PLFLPETRLV APPDITRDLL SGLPTYAEAM SDHPPTYATV VAVRSTEQPS GALAPDDQRR TQNSGAWRPP RVNSRELYRA QRAARGSSDH APYRRQGCCG VVWRHAVFGV VAIVVVIILV FLWR //