ID   HEMA_VACCC              Reviewed;         315 AA.
AC   P20978;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   29-SEP-2021, entry version 106.
DE   RecName: Full=Protein A56;
DE   AltName: Full=Hemagglutinin;
DE   Flags: Precursor;
GN   Name=HA; ORFNames=A56R;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
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 {ECO:0000250}; Single-
CC       pass type I membrane protein {ECO:0000250}. Note=Component of
CC       extracellular enveloped virus (EEV) but not intracellular mature virus
CC       (IMV). Component of the outermost 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.
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DR   EMBL; M35027; AAA48191.1; -; Genomic_DNA.
DR   PIR; D42523; HNVZ4X.
DR   SMR; P20978; -.
DR   Proteomes; UP000008269; 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; Reference proteome; Signal;
KW   Transmembrane; 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_0000040565"
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          194..213
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        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;  34778 MW;  C7EE7D5EA12134D3 CRC64;
     MTRLPILLLL ISLVYATPFP QTSKKIGDDA TLSCNRNNTN DYVVMSAWYK EPNSIILLAA
     KSDVLYFDNY TKDKISYDSP YDDLVTTITI KSLTARDAGT YVCAFFMTSP TNDTDKVDYE
     EYSTELIVNT DSESTIDIIL SGSTHSPETS SEKPDYIDNS NCSSVFEIAT PEPITDNVED
     HTDTVTYTSD SINTVSATSG ESTTDETPEP ITDKEEDHTV TDTVSYTTVS TSSGIVTTKS
     TTDDADLYDT YNDNDTVPST TVGSSTTSIS NYKTKDFVEI FGITALIILS AVAIFCITYY
     ICNKRSRKYK TENKV