ID   HEMA_RACVI              Reviewed;         310 AA.
AC   Q00716;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-JUN-2021, entry version 86.
DE   RecName: Full=Protein A56;
DE   AltName: Full=Hemagglutinin;
DE   Flags: Precursor;
GN   Name=HA;
OS   Raccoon poxvirus (RCN).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10256;
OH   NCBI_TaxID=9654; Procyon lotor (Raccoon).
RN   [1]
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate rcn-84, Isolate rcn-85a, and Isolate rcn-85b;
RA   Esposito J.J., Ropp S.L., Jin Q., Cai B., Knight J.C., Yu L.,
RA   Taubenberger J.K., Tsai M.M., Nowotny N., Meyer H., Cavallaro K.F.;
RT   "Phylogenetic analysis of orthopoxviruses.";
RL   Submitted (MAY-2001) 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 {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 (By similarity). {ECO:0000250}.
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DR   EMBL; M94169; AAA47231.1; -; Genomic_DNA.
DR   EMBL; AF375115; AAN47049.1; -; Genomic_DNA.
DR   EMBL; AF375116; AAN47050.1; -; Genomic_DNA.
DR   EMBL; AF375117; AAN47051.1; -; Genomic_DNA.
DR   PIR; A43381; HNVZRA.
DR   SMR; Q00716; -.
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:0000255"
FT   CHAIN           17..310
FT                   /note="Protein A56"
FT                   /id="PRO_0000040571"
FT   TOPO_DOM        17..275
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301..310
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          19..121
FT                   /note="Ig-like V-type"
FT   REGION          153..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   310 AA;  34190 MW;  7C25F5C19C7B11B9 CRC64;
     MKQLSIVILL LSIVYTTKPH PTQISKKLGD DATLSCNRNN THGYLVMSSW YKKPDSIILL
     AAKNDVVYFD DYTADKVSYD SPYDTLATII TIKSLTSADA GTYICAFFIT STNDTDKIDY
     EEYFIDLVVN PANVSTIDAI LSGSTTQQDI ISHTEEQHDS DTTICTSEST TQISETSEST
     TSSQISETSE STSYGVEDDT QYNVTTDTTD NSDTIGTLPE EDTTTISTTI HKTTTTDDNL
     YDTYNEPISV SSSIPTTVES VTISTTKYTT SDFIEIFGIV SLILLLAVAI FCIIYYFCSG
     RSRKQETNIL