HEMA_VACCW
ID HEMA_VACCW Reviewed; 314 AA.
AC Q01218; Q76ZM3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 02-JUN-2021, entry version 105.
DE RecName: Full=Protein A56;
DE AltName: Full=Hemagglutinin;
DE Flags: Precursor;
GN Name=HA; OrderedLocusNames=VACWR181; ORFNames=A56R;
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=1529542; DOI=10.1016/0042-6822(92)91229-n;
RA Cavallaro K.F., Esposito J.J.;
RT "Sequences of the raccoon poxvirus hemagglutinin protein.";
RL Virology 190:434-439(1992).
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 SUBCELLULAR LOCATION.
RX PubMed=9636186; DOI=10.1073/pnas.95.13.7544;
RA Vanderplasschen A., Mathew E., Hollinshead M., Sim R.B., Smith G.L.;
RT "Extracellular enveloped vaccinia virus is resistant to complement because
RT of incorporation of host complement control proteins into its envelope.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7544-7549(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16509968; DOI=10.1186/1743-422x-3-10;
RA Yoder J.D., Chen T.S., Gagnier C.R., Vemulapalli S., Maier C.S.,
RA Hruby D.E.;
RT "Pox proteomics: mass spectrometry analysis and identification of Vaccinia
RT virion proteins.";
RL Virol. J. 3:10-10(2006).
RN [6]
RP INTERACTION WITH A16 AND G9.
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.
RX PubMed=18760436; DOI=10.1016/j.virol.2008.07.020;
RA Turner P.C., Moyer R.W.;
RT "The vaccinia virus fusion inhibitor proteins SPI-3 (K2) and HA (A56)
RT expressed by infected cells reduce the entry of superinfecting virus.";
RL Virology 380:226-233(2008).
RN [8]
RP FUNCTION.
RX PubMed=19036815; DOI=10.1128/jvi.01684-08;
RA Wagenaar T.R., Moss B.;
RT "Expression of the A56 and K2 proteins is sufficient to inhibit vaccinia
RT virus entry and cell fusion.";
RL J. Virol. 83:1546-1554(2009).
RN [9]
RP INTERMOLECULAR DISULFIDE BOND.
RX PubMed=20719953; DOI=10.1128/jvi.00372-10;
RA DeHaven B.C., Girgis N.M., Xiao Y., Hudson P.N., Olson V.A., Damon I.K.,
RA Isaacs S.N.;
RT "Poxvirus complement control proteins are expressed on the cell surface
RT through an intermolecular disulfide bridge with the viral A56 protein.";
RL J. Virol. 84:11245-11254(2010).
RN [10]
RP INTERACTION WITH K2 AND C3, AND SUBCELLULAR LOCATION.
RX PubMed=21715594; DOI=10.1099/vir.0.030460-0;
RA Dehaven B.C., Gupta K., Isaacs S.N.;
RT "The vaccinia virus A56 protein: a multifunctional transmembrane
RT glycoprotein that anchors two secreted viral proteins.";
RL J. Gen. Virol. 92:1971-1980(2011).
CC -!- FUNCTION: Prevents cell to cell fusion by interacting with and
CC directing the viral K2 protein on the host plasma membrane. The A56-K2
CC complex associates with components of the entry fusion complex (EFC)
CC presumably to avoid superinfection and syncytium formation. Via its
CC interaction with C3/VCP protein, protects the infected cell and
CC probably also the extracellular enveloped virus from complement attack.
CC {ECO:0000269|PubMed:18760436, ECO:0000269|PubMed:19036815}.
CC -!- SUBUNIT: Heterodimerizes with K2. The heterodimer A56/K2 interacts with
CC components of the entry fusion complex A16 and G9. Interacts with K2
CC protein. Heterodimer with C3/VPC protein; disulfide-linked.
CC {ECO:0000269|PubMed:18353946, ECO:0000269|PubMed:21715594}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Host membrane; Single-pass type I
CC membrane protein. Note=Component of extracellular enveloped virus (EEV)
CC but not intracellular mature virus (IMV). Component of the outermost
CC membrane of EEV.
CC -!- PTM: Glycosylated; contains phosphate and sulfate-substituted glycans.
CC O-glycosylation is required for hemagglutination and hemadsorption
CC activities of infected cell membranes.
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; D11079; BAA01829.1; -; Genomic_DNA.
DR EMBL; M93956; AAA48252.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89460.1; -; Genomic_DNA.
DR PIR; JQ1793; JQ1793.
DR RefSeq; YP_233063.1; NC_006998.1.
DR SMR; Q01218; -.
DR IntAct; Q01218; 6.
DR MINT; Q01218; -.
DR TCDB; 1.G.11.1.1; the poxvirus cell entry protein complex (pep-c) family.
DR DNASU; 3707652; -.
DR GeneID; 3707652; -.
DR KEGG; vg:3707652; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hemagglutinin; Host membrane;
KW Immunoglobulin domain; Late protein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..314
FT /note="Protein A56"
FT /id="PRO_0000040568"
FT TOPO_DOM 17..278
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..314
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT DOMAIN 17..121
FT /note="Ig-like V-type"
FT REGION 193..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 34..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 162
FT /note="Interchain (with C-20 in complement control protein
FT C3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 314 AA; 34678 MW; 6F4322853244707F CRC64;
MTRLPILLLL ISLVYATPFP QTSKKIGDDA TLSCNRNNTN DYVVMSAWYK EPNSIILLAA
KSDVLYFDNY TKDKISYDSP YDDLVTTITI KSLTARDAGT YVCAFFMTST TNDTDKVDYE
EYSTELIVNT DSESTIDIIL SGSTHSPETS SKKPDYIDNS NCSSVFEIAT PEPITDNVED
HTDTVTYTSD SINTVSASSG ESTTDETPEP ITDKEDHTVT DTVSYTTVST SSGIVTTKST
TDDADLYDTY NDNDTVPPTT VGGSTTSISN YKTKDFVEIF GITALIILSA VAIFCITYYI
YNKRSRKYKT ENKV
