HEMA_VACCT
ID HEMA_VACCT Reviewed; 315 AA.
AC P16561; Q89120; Q9JF47;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein A56;
DE AltName: Full=Hemagglutinin;
DE Flags: Precursor;
GN Name=HA; ORFNames=TA66R;
OS Vaccinia virus (strain Tian Tan) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10253;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2754392; DOI=10.1084/jem.170.2.571;
RA Dongyan J., Zhiliang L., Qi J., Hao Y., Yunde H.;
RT "Vaccinia virus hemagglutinin. A novel member of the immunoglobulin
RT superfamily.";
RL J. Exp. Med. 170:571-576(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Li Z., Jin Q., Yu W., Jin T., Hou Y.;
RT "Complete nucleotide sequence of the hemagglutinin gene of Tian Tan strain
RT of vaccinia virus.";
RL Ping Tu Hsueh Pao 5:1-9(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jin Q., Hou Y.D., Cheng N.H., Yao E.M., Cheng S.X., Yang X.K., Jing D.Y.,
RA Yu W.H., Yuan J.S., Ma X.J.;
RT "Complete genomic sequence of vaccinia virus (Tian Tan strain).";
RL Submitted (SEP-1998) 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.
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DR EMBL; X15709; CAA33740.1; -; Genomic_DNA.
DR EMBL; U25662; AAA74188.1; -; Genomic_DNA.
DR EMBL; AF095689; AAF34065.1; -; Genomic_DNA.
DR PIR; JL0108; HNVZVT.
DR SMR; P16561; -.
DR Proteomes; UP000163220; 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:0000255"
FT CHAIN 17..315
FT /note="Protein A56"
FT /id="PRO_0000040567"
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 192..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..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"
FT CONFLICT 132
FT /note="S -> T (in Ref. 2; AAA74188)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="S -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="A -> G (in Ref. 2; AAA74188)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 34758 MW; E04944814085CAA4 CRC64;
MARLPILLLL ISLVYSTPSP QTSKKIGDDA TLSCNRNNTN DYVVMSAWYK EPNSIILLAA
KSDVLYFDNY TKDKISYDSP YDDLVTTITI KSLTARDAGT YVCAFFMTSP TNDTDKVDYE
EYSTELIVNT DSESTIDIIL SGSTHSPETS SEKPEDIDNL NCSSVFEIAT PEPITDNVED
HTDTVTYTSD SINTVSASSG ESTTDETPEP ITDKEEDHTV TDTVSYTTVS TSSGIVTTKS
TTDDADLYDT YNDNDTVPST TVGCSTTSIS NYKTKDFVEI FGITALIILS AVAIFCITYY
IYNKRSRKYK TENKV
