ID VA16_VACCC Reviewed; 378 AA. AC P20993; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 03-MAY-2011, entry version 48. DE RecName: Full=Protein A16; GN ORFNames=A16L; OS Vaccinia virus (strain Copenhagen) (VACV). OC Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae; OC Orthopoxvirus; Vaccinia virus. OX NCBI_TaxID=10249; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=91021027; 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 COMPLETE GENOME. 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 RP GLY-2. RX MEDLINE=97332355; PubMed=9188589; 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: Required for virus entry into host cell and for cell- CC cell fusion (syncytium formation) (By similarity). CC -!- SUBUNIT: Part of a stable entry-fusion complex (EFC) which is at CC least composed of proteins A16, A21, A28, G3, G9, H2, J5, and L5. CC Formation of the viral membrane is necessary for the assembly of CC the complex (By similarity). CC -!- SUBCELLULAR LOCATION: Virion membrane; Single-pass type II CC membrane protein (Potential). Note=Component of the intracellular CC mature virion (IMV) outer membrane (By similarity). CC -!- PTM: Most cysteines are linked by disulfide bonds. They are CC created by the viral disulfide bond formation pathway, a poxvirus- CC specific redox pathway that operates on the cytoplasmic side of CC the IMV membranes (By similarity). CC -!- SIMILARITY: Belongs to the poxviruses A16/G9/J5 family. 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 GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004251; DUF230_poxv. DR Pfam; PF03003; DUF230; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; KW Fusion of virus membrane with host membrane; KW Initiation of viral infection; Lipoprotein; Membrane; Myristate; KW Signal-anchor; Transmembrane; Transmembrane helix; KW Viral penetration into host cytoplasm; Virion. FT INIT_MET 1 1 Removed; by host. FT CHAIN 2 378 Protein A16. FT /FTId=PRO_0000099251. FT TOPO_DOM 2 342 Cytoplasmic (Potential). FT TRANSMEM 343 363 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 364 378 Lumenal (Potential). FT LIPID 2 2 N-myristoyl glycine; by host. FT MUTAGEN 2 2 G->A: Complete loss of myristoylation. 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 //