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 22-JUL-2008, entry version 38. 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. 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 complex which is at least composed of CC proteins A16, A21, A28, G3, G9, H2, J5, and L5. Formation of the CC viral membrane is necessary for the assembly of the complex (By CC similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein (Potential). Note=Component of the intracellular mature CC 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 InterPro; IPR004251; DUF230_poxv. DR Pfam; PF03003; DUF230; 1. PE 1: Evidence at protein level; KW Complete proteome; Lipoprotein; Membrane; Myristate; Signal-anchor; KW Transmembrane; 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 Signal-anchor for type II membrane FT 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 //