ID   HEMA_CWPXG              Reviewed;         314 AA.
AC   O72737;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   02-JUN-2021, entry version 73.
DE   RecName: Full=Protein A56;
DE   AltName: Full=Hemagglutinin;
DE   Flags: Precursor;
GN   Name=HA; ORFNames=A58R;
OS   Cowpox virus (strain GRI-90 / Grishak) (CPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=265871;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=29092; Microtus agrestis (Short-tailed field vole).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shchelkunov S.N., Safronov P.F., Totmenin A.V., Miheev M.V.,
RA   Ryazankina O.I., Petrov N.A., Gutorov V.V., Kotwal G.J., Sandakhchiev L.S.;
RT   "Structure-function and organization of cowpox virus strain GRI-90 complete
RT   genome.";
RL   Submitted (MAR-2003) 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; X94355; CAD90725.1; -; Genomic_DNA.
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..314
FT                   /note="Protein A56"
FT                   /id="PRO_0000040570"
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          192..217
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        38
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"
SQ   SEQUENCE   314 AA;  34774 MW;  A3461711524434F3 CRC64;
     MARLPILLLL ISLVYSTPSP QTSKKIGDDA TLSCNRNNTT DYVVMSAWYK EPNSIILLAA
     KSDVLYFDNY TKDKISYDSP YDDLVTTITI KSLTARDAGT YVCAFFMTST TNDTDKVDYE
     EYSTELIVNT DSESTIDIIL SGSTHSPETS SEKPDYIDNS NCSSVFEIAT PEPITDNEED
     HTDVTYTSEN INTVSTTSRE STTDETPEPI TDKEEDHTVT DTVSYTTVST SSGIVTTKST
     TDDADLYDTY NDNDTVPPTT VGGSTTSISN YKTKDFVEIF GITALIILSA VAIFCITYYI
     CNKRSRKYKT ENKV