ID PG143_VACCC Reviewed; 378 AA. AC P20993; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-NOV-2024, entry version 87. DE RecName: Full=Virion membrane protein OPG143; GN Name=OPG143; ORFNames=A16L; OS Vaccinia virus (strain Copenhagen) (VACV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus. OX NCBI_TaxID=10249; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2; RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., RA Paoletti E.; RT "The complete DNA sequence of vaccinia virus."; RL Virology 179:247-266(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., RA Paoletti E.; RT "Appendix to 'The complete DNA sequence of vaccinia virus'."; RL Virology 179:517-563(1990). RN [3] RP MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-2. RX PubMed=9188589; DOI=10.1128/jvi.71.7.5218-5226.1997; RA Martin K.H., Grosenbach D.W., Franke C.A., Hruby D.E.; RT "Identification and analysis of three myristylated vaccinia virus late RT proteins."; RL J. Virol. 71:5218-5226(1997). CC -!- FUNCTION: Envelope protein part of the entry-fusion complex responsible CC for the virus membrane fusion with host cell membrane during virus CC entry. Also plays a role in cell-cell fusion (syncytium formation). CC {ECO:0000250|UniProtKB:P16710}. CC -!- SUBUNIT: Part of a stable entry-fusion complex (EFC) which is at least CC composed of proteins OPG143, OPG147, OPG155, OPG086, OPG094, OPG107, CC OPG104, and OPG099. Formation of the viral membrane is necessary for CC the assembly of the complex. Interacts with OPG094. Interacts with CC OPG153. {ECO:0000250|UniProtKB:P16710}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P16710}; CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:P16710}. CC Note=Component of the mature virion (MV) membrane. The mature virion is CC located in the cytoplasm of infected cells and is probably released by CC cell lysis. {ECO:0000250|UniProtKB:P16710}. CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle. CC -!- PTM: Most cysteines are linked by disulfide bonds. They are created by CC the viral disulfide bond formation pathway, a poxvirus-specific redox CC pathway that operates on the cytoplasmic side of the MV membranes. CC {ECO:0000250|UniProtKB:P16710}. CC -!- SIMILARITY: Belongs to the orthopoxvirus OPG143 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; M35027; AAA48138.1; -; Genomic_DNA. DR PIR; I42518; I42518. DR SMR; P20993; -. DR iPTMnet; P20993; -. DR Proteomes; UP000008269; Genome. DR GO; GO:0016020; C: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 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-KW. DR GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW. DR InterPro; IPR004251; Pox_virus_G9/A16. DR Pfam; PF03003; Pox_G9-A16; 1. PE 1: Evidence at protein level; KW ATP-binding; Disulfide bond; DNA-binding; KW Fusion of virus membrane with host membrane; Helicase; Hydrolase; KW Late protein; Lipoprotein; Membrane; Myristate; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Signal-anchor; Transcription; KW Transcription regulation; Transcription termination; Transmembrane; KW Transmembrane helix; Viral envelope protein; KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell. FT INIT_MET 1 FT /note="Removed; by host" FT CHAIN 2..378 FT /note="Virion membrane protein OPG143" FT /id="PRO_0000099251" FT TOPO_DOM 2..342 FT /note="Virion surface" FT /evidence="ECO:0000255" FT TRANSMEM 343..363 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 364..378 FT /note="Intravirion" FT /evidence="ECO:0000255" FT LIPID 2 FT /note="N-myristoyl glycine; by host" FT /evidence="ECO:0000269|PubMed:9188589" FT MUTAGEN 2 FT /note="G->A: Complete loss of myristoylation." FT /evidence="ECO:0000269|PubMed:9188589" SQ SEQUENCE 378 AA; 43562 MW; 05ED614AA1D11A19 CRC64; MGAAVTLNRI KIAPGIADIR DKYMELGFNY PEYNRAVKFA EESYTYYYET SPGEIKPKFC LIDGMSIDHC SSFIVPEFAK QYVLIHGEPC SSFKFRPGSL IYYQNEVTPE YIKDLKHATD YIASGQRCHF IKKDYLLGDS DSVAKCCSKT NTKHCPKIFN NNYKTEHCDD FMTGFCRNDP GNPNCLEWLR AKRKPAMSTY SDICSKHMDA RYCSEFIRII RPDYFTFGDT ALYVFCNDHK GNRNCWCANY PKSNSGDKYL GPRVCWLHEC TDESRDRKWL YYNQDVQRTR CKYVGCTINV NSLALKNSQA ELTSNCTRTT SAVGDVHHPG EPVVKDKIKL PTWLGAAITL VVISVIFYFI SIYSRPKIKT NDINVRRR //