ID PG143_VACCW Reviewed; 377 AA. AC P16710; Q80HV5; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 24-JUL-2024, entry version 90. DE RecName: Full=Virion membrane protein OPG143; GN Name=OPG143; OrderedLocusNames=VACWR136; ORFNames=A16L; OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain OS WR)). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus. OX NCBI_TaxID=10254; OH NCBI_TaxID=9913; Bos taurus (Bovine). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., RA Wohlhueter R.; RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold RT redundancy and an error rate of 0.16/10kb."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-275. RX PubMed=2370683; DOI=10.1128/jvi.64.8.3853-3863.1990; RA Pacha R.F., Meis R.J., Condit R.C.; RT "Structure and expression of the vaccinia virus gene which prevents virus- RT induced breakdown of RNA."; RL J. Virol. 64:3853-3863(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). RN [4] RP IDENTIFICATION IN A COMPLEX WITH OPG147; OPG155; OPG086; OPG094; OPG107; RP OPG104 AND OPG099. RX PubMed=16339313; DOI=10.1073/pnas.0509239102; RA Senkevich T.G., Ojeda S., Townsley A., Nelson G.E., Moss B.; RT "Poxvirus multiprotein entry-fusion complex."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18572-18577(2005). RN [5] RP FUNCTION, DISULFIDE BONDS, INDUCTION, AND TOPOLOGY. RX PubMed=16352530; DOI=10.1128/jvi.80.1.51-61.2006; RA Ojeda S., Senkevich T.G., Moss B.; RT "Entry of vaccinia virus and cell-cell fusion require a highly conserved RT cysteine-rich membrane protein encoded by the A16L gene."; RL J. Virol. 80:51-61(2006). RN [6] RP INTERACTION WITH OPG094. RX PubMed=18353946; DOI=10.1128/jvi.00162-08; RA Wagenaar T.R., Ojeda S., Moss B.; RT "Vaccinia virus A56/K2 fusion regulatory protein interacts with the A16 and RT G9 subunits of the entry fusion complex."; RL J. Virol. 82:5153-5160(2008). RN [7] RP FUNCTION, AND INTERACTION WITH OPG153. RX PubMed=22278246; DOI=10.1128/jvi.06081-11; RA Chang S.J., Shih A.C., Tang Y.L., Chang W.; RT "Vaccinia mature virus fusion regulator A26 protein binds to A16 and G9 RT proteins of the viral entry fusion complex and dissociates from mature RT virions at low pH."; RL J. Virol. 86:3809-3818(2012). 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:0000269|PubMed:16352530, ECO:0000269|PubMed:22278246}. 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 (PubMed:22278246). {ECO:0000269|PubMed:16339313, CC ECO:0000269|PubMed:18353946}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type CC II membrane protein {ECO:0000305}. Note=Component of the mature virion CC (MV) membrane (Probable). The mature virion is located in the cytoplasm CC of infected cells and is probably released by cell lysis. CC {ECO:0000269|PubMed:9188589, ECO:0000305}. CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle. CC {ECO:0000269|PubMed:16352530}. 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 -!- 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; AY243312; AAO89415.1; -; Genomic_DNA. DR EMBL; M32064; AAA48348.2; -; Genomic_DNA. DR PIR; A36415; A36415. DR RefSeq; YP_233018.1; NC_006998.1. DR PDB; 8GP6; X-ray; 2.70 A; A=1-342. DR PDBsum; 8GP6; -. DR SMR; P16710; -. DR IntAct; P16710; 1. DR MINT; P16710; -. DR iPTMnet; P16710; -. DR DNASU; 3707666; -. DR GeneID; 3707666; -. DR KEGG; vg:3707666; -. DR Proteomes; UP000000344; 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 3D-structure; 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..377 FT /note="Virion membrane protein OPG143" FT /id="PRO_0000099253" 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..377 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" FT STRAND 8..14 FT /evidence="ECO:0007829|PDB:8GP6" FT STRAND 19..27 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 31..33 FT /evidence="ECO:0007829|PDB:8GP6" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:8GP6" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:8GP6" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 68..71 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 76..79 FT /evidence="ECO:0007829|PDB:8GP6" FT STRAND 82..85 FT /evidence="ECO:0007829|PDB:8GP6" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:8GP6" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 109..118 FT /evidence="ECO:0007829|PDB:8GP6" FT STRAND 123..127 FT /evidence="ECO:0007829|PDB:8GP6" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 140..148 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:8GP6" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 169..178 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 183..189 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 194..207 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 211..220 FT /evidence="ECO:0007829|PDB:8GP6" FT TURN 221..225 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 226..238 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 243..245 FT /evidence="ECO:0007829|PDB:8GP6" FT TURN 246..248 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 261..266 FT /evidence="ECO:0007829|PDB:8GP6" FT TURN 268..270 FT /evidence="ECO:0007829|PDB:8GP6" FT STRAND 271..274 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 277..279 FT /evidence="ECO:0007829|PDB:8GP6" FT HELIX 282..290 FT /evidence="ECO:0007829|PDB:8GP6" SQ SEQUENCE 377 AA; 43425 MW; EE79C44446B542FA 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 SAVGDVHPGE PVVKDKIKLP TWLGAAITLV VISVIFYFIS IYSRPKIKTN DINVRRR //