A36_VACCW
ID A36_VACCW Reviewed; 221 AA.
AC P68619; P21059; Q76ZP0;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Protein A36;
GN OrderedLocusNames=VACWR159; ORFNames=A36R;
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=2045793; DOI=10.1099/0022-1317-72-6-1349;
RA Smith G.L., Chan Y.S., Howard S.T.;
RT "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the
RT right inverted terminal repeat.";
RL J. Gen. Virol. 72:1349-1376(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1856205; DOI=10.1016/s0021-9258(18)92757-2;
RA Amegadzie B.Y., Ahn B.-Y., Moss B.;
RT "Identification, sequence, and expression of the gene encoding a Mr 35,000
RT subunit of the vaccinia virus DNA-dependent RNA polymerase.";
RL J. Biol. Chem. 266:13712-13718(1991).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=9581774; DOI=10.1006/viro.1998.9103;
RA Wolffe E.J., Weisberg A.S., Moss B.;
RT "Role for the vaccinia virus A36R outer envelope protein in the formation
RT of virus-tipped actin-containing microvilli and cell-to-cell virus
RT spread.";
RL Virology 244:20-26(1998).
RN [5]
RP INTERACTION WITH HOST NCK, MUTAGENESIS OF TYR-112 AND TYR-132, AND
RP PHOSPHORYLATION AT TYR-112 AND TYR-132.
RX PubMed=10553910; DOI=10.1038/44860;
RA Frischknecht F., Moreau V., Rottger S., Gonfloni S., Reckmann I.,
RA Superti-Furga G., Way M.;
RT "Actin-based motility of vaccinia virus mimics receptor tyrosine kinase
RT signalling.";
RL Nature 401:926-929(1999).
RN [6]
RP FUNCTION.
RX PubMed=11470826; DOI=10.1083/jcb.200104124;
RA Hollinshead M., Rodger G., Van Eijl H., Law M., Hollinshead R., Vaux D.J.,
RA Smith G.L.;
RT "Vaccinia virus utilizes microtubules for movement to the cell surface.";
RL J. Cell Biol. 154:389-402(2001).
RN [7]
RP INTERACTION WITH PROTEIN A33.
RX PubMed=12634370; DOI=10.1128/jvi.77.7.4113-4126.2003;
RA Ward B.M., Weisberg A.S., Moss B.;
RT "Mapping and functional analysis of interaction sites within the
RT cytoplasmic domains of the vaccinia virus A33R and A36R envelope
RT proteins.";
RL J. Virol. 77:4113-4126(2003).
RN [8]
RP INTERACTION WITH HOST KLC1.
RX PubMed=14963148; DOI=10.1128/jvi.78.5.2486-2493.2004;
RA Ward B.M., Moss B.;
RT "Vaccinia virus A36R membrane protein provides a direct link between
RT intracellular enveloped virions and the microtubule motor kinesin.";
RL J. Virol. 78:2486-2493(2004).
RN [9]
RP FUNCTION.
RX PubMed=19052096; DOI=10.1128/jvi.01364-08;
RA Johnston S.C., Ward B.M.;
RT "Vaccinia virus protein F12 associates with intracellular enveloped virions
RT through an interaction with A36.";
RL J. Virol. 83:1708-1717(2009).
RN [10]
RP INTERACTION WITH PROTEIN F12.
RX PubMed=20195521; DOI=10.1371/journal.ppat.1000785;
RA Morgan G.W., Hollinshead M., Ferguson B.J., Murphy B.J., Carpentier D.C.,
RA Smith G.L.;
RT "Vaccinia protein F12 has structural similarity to kinesin light chain and
RT contains a motor binding motif required for virion export.";
RL PLoS Pathog. 6:E1000785-E1000785(2010).
RN [11]
RP FUNCTION, INTERACTION WITH HOST EPS15 AND ITSN1, MOTIF, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27670116; DOI=10.1038/nmicrobiol.2016.141;
RA Snetkov X., Weisswange I., Pfanzelter J., Humphries A.C., Way M.;
RT "NPF motifs in the vaccinia virus protein A36 recruit intersectin-1 to
RT promote Cdc42:N-WASP-mediated viral release from infected cells.";
RL Nat. Microbiol. 1:16141-16141(2016).
CC -!- FUNCTION: Involved in the intracellular transport of virions to the
CC host cell surface. Participates also in the formation of actin tails at
CC the plasma membrane to allow efficient actin-based motility and thus
CC cell to cell transmission of viral particles. Recruits host
CC intersectin-1/ITSN1 and activates host CDC42 to drive ARP2/3-mediated
CC actin polymerization. {ECO:0000269|PubMed:11470826,
CC ECO:0000269|PubMed:19052096, ECO:0000269|PubMed:27670116,
CC ECO:0000269|PubMed:9581774}.
CC -!- SUBUNIT: Interacts with host NCK (PubMed:10553910). Interacts with
CC protein A33 (via C-terminus) (PubMed:12634370). Interacts with protein
CC F12 (PubMed:20195521). Interacts (via C-terminus) with host kinesin
CC light chain/KLC1 (PubMed:14963148). Interacts with host intersectin-
CC 1/ITSN1 and EPS15 (PubMed:27670116). {ECO:0000269|PubMed:10553910,
CC ECO:0000269|PubMed:12634370, ECO:0000269|PubMed:14963148,
CC ECO:0000269|PubMed:20195521, ECO:0000269|PubMed:27670116}.
CC -!- INTERACTION:
CC P68619; P68617: VACWR156; NbExp=7; IntAct=EBI-7133540, EBI-7133633;
CC P68619; P33176: KIF5B; Xeno; NbExp=3; IntAct=EBI-7133540, EBI-355878;
CC P68619; O88447: Klc1; Xeno; NbExp=2; IntAct=EBI-7133540, EBI-301550;
CC P68619; P37285: Klc1; Xeno; NbExp=4; IntAct=EBI-7133540, EBI-917396;
CC P68619; O88448: Klc2; Xeno; NbExp=3; IntAct=EBI-7133540, EBI-301558;
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000269|PubMed:27670116};
CC Single-pass membrane protein {ECO:0000305}. Note=Found exclusively on
CC the wrapped enveloped virion. Absent in the mature virion (MV) and
CC extracellular enveloped virion (EV).
CC -!- PTM: Phosphorylation of Tyr-112 and Tyr-132 of A36 Mechanistically,
CC phosphorylation of Tyr-112 and Tyr-132 of A36 activates the host ARP2-
CC ARP3 complex and leads to actin nucleation.
CC {ECO:0000269|PubMed:10553910}.
CC -!- SIMILARITY: Belongs to the orthopoxvirus A36 protein family.
CC {ECO:0000305}.
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DR EMBL; D11079; BAA01808.1; -; Genomic_DNA.
DR EMBL; M61187; AAA48332.1; -; Genomic_DNA.
DR EMBL; X57318; CAA40585.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89438.1; -; Genomic_DNA.
DR PIR; JQ1772; B42521.
DR RefSeq; YP_233041.1; NC_006998.1.
DR ELM; P68619; -.
DR IntAct; P68619; 7.
DR MINT; P68619; -.
DR iPTMnet; P68619; -.
DR DNASU; 3707689; -.
DR GeneID; 3707689; -.
DR KEGG; vg:3707689; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0075520; P:actin-dependent intracellular transport of virus; IDA:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; IDA:UniProtKB.
DR InterPro; IPR010274; Orthopox_A36R.
DR Pfam; PF05950; Orthopox_A36R; 1.
PE 1: Evidence at protein level;
KW Host cell membrane; Host membrane; Host-virus interaction; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..221
FT /note="Protein A36"
FT /id="PRO_0000040600"
FT TOPO_DOM 1
FT /note="Extracellular"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..221
FT /note="Cytoplasmic"
FT MOTIF 161..163
FT /note="NPF-motif"
FT /evidence="ECO:0000269|PubMed:27670116"
FT MOTIF 176..178
FT /note="NPF-motif"
FT /evidence="ECO:0000269|PubMed:27670116"
FT MOTIF 190..192
FT /note="NPF-motif"
FT /evidence="ECO:0000269|PubMed:27670116"
FT MOD_RES 112
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000269|PubMed:10553910"
FT MOD_RES 132
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000269|PubMed:10553910"
FT MUTAGEN 112
FT /note="Y->F: About 85% loss of virus-induced actin tail
FT formation."
FT /evidence="ECO:0000269|PubMed:10553910"
FT MUTAGEN 112
FT /note="Y->F: Complete loss of virus-induced actin tail
FT formation; when associated with Y-132."
FT /evidence="ECO:0000269|PubMed:10553910"
FT MUTAGEN 132
FT /note="Y->F: About 20% loss of virus-induced actin tail
FT formation."
FT /evidence="ECO:0000269|PubMed:10553910"
SQ SEQUENCE 221 AA; 25133 MW; 5D15758981B0E2E2 CRC64;
MMLVPLITVT VVAGTILVCY ILYICRKKIR TVYNDNKIIM TKLKKIKSSN SSKSSKSTDS
ESDWEDHCSA MEQNNDVDNI SRNEILDDDS FAGSLIWDNE SNVMAPSTEH IYDSVAGSTL
LINNDRNEQT IYQNTTVVIN ETETVEVLNE DTKQNPNYSS NPFVNYNKTS ICSKSNPFIT
ELNNKFSENN PFRRAHSDDY LNKQEQDHEH DDIESSVVSL V
