HEMA_VACCA
ID HEMA_VACCA Reviewed; 315 AA.
AC Q89182;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 89.
DE RecName: Full=Protein A56;
DE AltName: Full=Hemagglutinin;
DE Flags: Precursor;
GN Name=HA; OrderedLocusNames=MVA165R, ACAM3000_MVA_165; ORFNames=A56R;
OS Vaccinia virus (strain Ankara) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=126794;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8921843; DOI=10.1016/0378-1119(96)00267-3;
RA Antoine G., Scheiflinger F., Holzer G., Langmann T., Falkner F.G.,
RA Dorner F.;
RT "Characterization of the vaccinia MVA hemagglutinin gene locus and its
RT evaluation as an insertion site for foreign genes.";
RL Gene 177:43-46(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT "The complete genomic sequence of the modified vaccinia Ankara strain:
RT comparison with other orthopoxviruses.";
RL Virology 244:365-396(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Acambis 3000;
RA Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA Khristova M., Wohlhueter R.M.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. 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 (By similarity). {ECO:0000250}.
CC -!- PTM: Glycosylated; contains phosphate and sulfate-substituted glycans.
CC O-glycosylation is required for hemagglutination and hemadsorption
CC activities of infected cell membranes.
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DR EMBL; X91135; CAA62575.1; -; Genomic_DNA.
DR EMBL; U94848; AAB96543.1; -; Genomic_DNA.
DR EMBL; AY603355; AAT10563.1; -; Genomic_DNA.
DR PIR; T37438; T37438.
DR SMR; Q89182; -.
DR Proteomes; UP000159908; Genome.
DR Proteomes; UP000172909; 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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hemagglutinin; Host membrane;
KW Immunoglobulin domain; Late protein; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..315
FT /note="Protein A56"
FT /id="PRO_0000040564"
FT TOPO_DOM 17..279
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..315
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT DOMAIN 17..121
FT /note="Ig-like V-type"
FT REGION 191..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
FT /note="Polar residues"
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 254
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 315 AA; 34794 MW; C7EE7D42D7E4E543 CRC64;
MTRLPILLLL ISLVYATPFP QTSKKIGDDA TLSCNRNNTN DYVVMSAWYK EPNSIILLAA
KSDVLYFDNY TKDKISYDSP YDDLVTTITI KSLTARDAGT YVCAFFMTSP TNDTDKVDYE
EYSTELIVNT DSESTIDIIL SGSTHSPETS SEKPDYIDNS NCSSVFEIAT PEPITDNVED
HTDTVTYTSD SINTVSASSG ESTTDETPEP ITDKEEDHTV TDTVSYTTVS TSSGIVTTKS
TTDDADLYDT YNDNDTVPST TVGGSTTSIS NYKTKDFVEI FGITALIILS AVAIFCITYY
IYNKRSRKYK TENKV
