A17_VACCW
ID A17_VACCW Reviewed; 203 AA.
AC P68593; P16711; Q76ZQ1;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 02-JUN-2021, entry version 54.
DE RecName: Full=Virion membrane protein A17 precursor;
DE AltName: Full=23 kDa late protein;
DE Contains:
DE RecName: Full=Mature 21 kDa protein A17;
GN OrderedLocusNames=VACWR137; ORFNames=A17L;
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 [GENOMIC DNA].
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 [2]
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 [3]
RP INTERACTION WITH A27.
RX PubMed=9811753; DOI=10.1128/jvi.72.12.10126-10137.1998;
RA Vazquez M.I., Rivas G., Cregut D., Serrano L., Esteban M.;
RT "The vaccinia virus 14-kilodalton (A27L) fusion protein forms a triple
RT coiled-coil structure and interacts with the 21-kilodalton (A17L) virus
RT membrane protein through a C-terminal alpha-helix.";
RL J. Virol. 72:10126-10137(1998).
RN [4]
RP INTERACTION WITH A14, PROTEOLYTIC CLEAVAGE AT GLY-185, AND PHOSPHORYLATION
RP BY F10 KINASE.
RX PubMed=10196242; DOI=10.1128/jvi.73.5.3534-3543.1999;
RA Betakova T., Wolffe E.J., Moss B.;
RT "Regulation of vaccinia virus morphogenesis: phosphorylation of the A14L
RT and A17L membrane proteins and C-terminal truncation of the A17L protein
RT are dependent on the F10L kinase.";
RL J. Virol. 73:3534-3543(1999).
RN [5]
RP PHOSPHORYLATION AT TYR-203.
RX PubMed=10438817; DOI=10.1128/jvi.73.9.7287-7296.1999;
RA Derrien M., Punjabi A., Khanna M., Grubisha O., Traktman P.;
RT "Tyrosine phosphorylation of A17 during vaccinia virus infection:
RT involvement of the H1 phosphatase and the F10 kinase.";
RL J. Virol. 73:7287-7296(1999).
RN [6]
RP TOPOLOGY, AND LACK OF GLYCOSYLATION.
RX PubMed=10497120; DOI=10.1006/viro.1999.9870;
RA Betakova T., Wolffe E.J., Moss B.;
RT "Membrane topology of the vaccinia virus A17L envelope protein.";
RL Virology 261:347-356(1999).
RN [7]
RP DISULFIDE BONDS.
RX PubMed=10666276; DOI=10.1128/jvi.74.5.2438-2442.2000;
RA Betakova T., Moss B.;
RT "Disulfide bonds and membrane topology of the vaccinia virus A17L envelope
RT protein.";
RL J. Virol. 74:2438-2442(2000).
RN [8]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11882999; DOI=10.1006/viro.2001.1131;
RA Wallengren K., Risco C., Krijnse-Locker J., Esteban M., Rodriguez D.;
RT "The A17L gene product of vaccinia virus is exposed on the surface of
RT IMV.";
RL Virology 290:143-152(2001).
RN [9]
RP POST-TRANSLATIONAL MODIFICATIONS, MUTAGENESIS OF GLY-16; GLY-18 AND
RP GLY-185, AND PROTEOLYTIC CLEAVAGE AT GLY-16 AND GLY-185.
RX PubMed=15163727; DOI=10.1128/jvi.78.12.6335-6343.2004;
RA Ansarah-Sobrinho C., Moss B.;
RT "Role of the I7 protein in proteolytic processing of vaccinia virus
RT membrane and core components.";
RL J. Virol. 78:6335-6343(2004).
RN [10]
RP PHOSPHORYLATION AT TYR-203, AND MUTAGENESIS OF TYR-203.
RX PubMed=14671108; DOI=10.1128/jvi.78.1.266-274.2004;
RA Szajner P., Weisberg A.S., Moss B.;
RT "Physical and functional interactions between vaccinia virus F10 protein
RT kinase and virion assembly proteins A30 and G7.";
RL J. Virol. 78:266-274(2004).
RN [11]
RP FUNCTION.
RX PubMed=17708756; DOI=10.1111/j.1462-5822.2007.01026.x;
RA Kochan G., Escors D., Gonzalez J.M., Casasnovas J.M., Esteban M.;
RT "Membrane cell fusion activity of the vaccinia virus A17-A27 protein
RT complex.";
RL Cell. Microbiol. 10:149-164(2008).
RN [12]
RP IDENTIFICATION IN A COMPLEX WITH A25; A26 AND A27.
RX PubMed=18842719; DOI=10.1128/jvi.01524-08;
RA Howard A.R., Senkevich T.G., Moss B.;
RT "Vaccinia virus A26 and A27 proteins form a stable complex tethered to
RT mature virions by association with the A17 transmembrane protein.";
RL J. Virol. 82:12384-12391(2008).
RN [13]
RP INTERACTION WITH D13.
RX PubMed=19570860; DOI=10.1128/jvi.00875-09;
RA Bisht H., Weisberg A.S., Szajner P., Moss B.;
RT "Assembly and disassembly of the capsid-like external scaffold of immature
RT virions during vaccinia virus morphogenesis.";
RL J. Virol. 83:9140-9150(2009).
CC -!- FUNCTION: Envelope protein which participates in virus morphogenesis.
CC Needed for an early step in viral crescent membrane formation by
CC interacting with D13 scaffold protein. Its interaction with D13
CC scaffold protein leads to the formation of rigid, crescent-shaped
CC membranes that assemble around the cytoplasmic virus factory. Membrane
CC anchor for the protein A27. A17-A27 virus envelope protein might be
CC involved in fusion or attachment, and can further associate to A26.
CC {ECO:0000269|PubMed:17708756}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (Probable). Interacts (via N-
CC terminus) with D13 scaffold; this interaction helps D13 to associate
CC with membranes. Interacts with A14. Interacts with A27; this
CC interaction allows A27 to be anchored in the mature virion (MV)
CC membrane. Part of a complex composed of A17, A25, A26 and A27.
CC {ECO:0000269|PubMed:10196242, ECO:0000269|PubMed:10666276,
CC ECO:0000269|PubMed:18842719, ECO:0000269|PubMed:19570860,
CC ECO:0000269|PubMed:9811753, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Note=The 23 kDa precursor is associated
CC with immature virions (IV) and the final 21 kDa form is present in
CC mature virions (MV). {ECO:0000269|PubMed:11882999}.
CC -!- PTM: The 23 kDa precursor is cleaved into a final 21 kDa form by the I7
CC protease during virus maturation. {ECO:0000269|PubMed:10196242}.
CC -!- PTM: Phosphorylated on tyrosine and threonine. Its phosphorylation
CC state is regulated by the F10 kinase and the H1 phosphatase (Probable).
CC Phosphorylation by F10 kinase seems to be required to form the
CC membranes associated with IV. {ECO:0000269|PubMed:10196242,
CC ECO:0000269|PubMed:10438817, ECO:0000269|PubMed:14671108, ECO:0000305}.
CC -!- PTM: Not glycosylated.
CC -!- SIMILARITY: Belongs to the chordopoxvirinae A17 family. {ECO:0000305}.
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DR EMBL; M32064; AAA48349.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89416.1; -; Genomic_DNA.
DR PIR; A42519; A42519.
DR RefSeq; YP_233019.1; NC_006998.1.
DR iPTMnet; P68593; -.
DR DNASU; 3707667; -.
DR GeneID; 3707667; -.
DR KEGG; vg:3707667; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0016021; C:integral component of 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 InterPro; IPR007977; Poxvirus_P21.
DR Pfam; PF05313; Pox_P21; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT CHAIN 1..203
FT /note="Virion membrane protein A17 precursor"
FT /id="PRO_0000099258"
FT PROPEP 1..16
FT /id="PRO_0000413883"
FT CHAIN 17..185
FT /note="Mature 21 kDa protein A17"
FT /id="PRO_0000413884"
FT PROPEP 185..203
FT /id="PRO_0000413885"
FT TOPO_DOM 1..65
FT /note="Virion surface"
FT /evidence="ECO:0000305"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..138
FT /note="Intravirion"
FT /evidence="ECO:0000305"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..203
FT /note="Virion surface"
FT /evidence="ECO:0000305"
FT REGION 1..38
FT /note="Binding to D13 scaffold protein"
FT SITE 16..17
FT /note="Cleavage; by I7 protease"
FT /evidence="ECO:0000305|PubMed:15163727"
FT SITE 185..186
FT /note="Cleavage; by I7 protease"
FT /evidence="ECO:0000269|PubMed:10196242,
FT ECO:0000305|PubMed:15163727"
FT MOD_RES 203
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10438817,
FT ECO:0000269|PubMed:14671108"
FT DISULFID 101..121
FT /evidence="ECO:0000269|PubMed:10666276"
FT DISULFID 178
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:10666276"
FT MUTAGEN 16
FT /note="G->A: No cleavage by I7 protease in N-terminus."
FT /evidence="ECO:0000269|PubMed:15163727"
FT MUTAGEN 18
FT /note="G->A: No cleavage by I7 protease in N-terminus."
FT /evidence="ECO:0000269|PubMed:15163727"
FT MUTAGEN 185
FT /note="G->A: No cleavage by I7 protease in C-terminus."
FT /evidence="ECO:0000269|PubMed:15163727"
FT MUTAGEN 203
FT /note="Y->F: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:14671108"
SQ SEQUENCE 203 AA; 22999 MW; 24759AF6FC18D431 CRC64;
MSYLRYYNML DDFSAGAGVL DKDLFTEEQQ QSFMPKDGGM MQNDYGGMND YLGIFKNNDV
RTLLGLILFV LALYSPPLIS ILMIFISSFL LPLTSLVITY CLVTQMYRGG NGNTVGMSIV
CIVAAVIIMA INVFTNSQIF NIISYIILFI LFFAYVMNIE RQDYRRSINV TIPEQYTCNK
PYTAGNKVDV DIPTFNSLNT DDY
