HEMA_VAR67
ID HEMA_VAR67 Reviewed; 313 AA.
AC P33807;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein A56;
DE AltName: Full=Hemagglutinin;
DE Flags: Precursor;
GN Name=HA; ORFNames=A56R, J9R;
OS Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=587200;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=India-1967 / Isolate Ind3;
RX PubMed=1666548;
RA Shchelkunov S.N., Marennikova S.S., Totmenin A.V., Blinov V.M.,
RA Chizhikov V.E., Gutorov V.V., Safronov P.F., Pozdnyakov S.G.,
RA Shelukhina E.M., Gashnikov P.V., Anjaparidze O.G., Sandakhchiev L.S.;
RT "Creation of a clone library of fragments from the natural variola virus
RT and study of the structural and functional organization of viral genes from
RT a circle of hosts.";
RL Dokl. Akad. Nauk SSSR 321:402-406(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=India-1967 / Isolate Ind3;
RX PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT "Genes of variola and vaccinia viruses necessary to overcome the host
RT protective mechanisms.";
RL FEBS Lett. 319:80-83(1993).
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; X69198; CAA49108.1; -; Genomic_DNA.
DR EMBL; X67118; CAA47552.1; -; Genomic_DNA.
DR PIR; H36854; H36854.
DR RefSeq; NP_042211.1; NC_001611.1.
DR SMR; P33807; -.
DR GeneID; 1486455; -.
DR KEGG; vg:1486455; -.
DR Proteomes; UP000002060; 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:0000255"
FT CHAIN 17..313
FT /note="Protein A56"
FT /id="PRO_0000040569"
FT TOPO_DOM 17..277
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..313
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT DOMAIN 18..121
FT /note="Ig-like V-type"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
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 313 AA; 34584 MW; 3A495FEF4C474A5E CRC64;
MTRLSILLLL ISLVYSTPYP QTQISKKIGD DATLSCSRNN INDYVVMSAW YKEPNSIILL
AAKSDVLYFD NYTKDKISYD SPYDDLVTTI TIKSLTAKDA GTYVCAFFMT STTNDTDKVD
YEEYSTELIV NTDSESTIDI ILSGSSHSPE TSSEKPDYIN NFNCSLVFEI ATPGPITDNV
ENHTDTVTYT SDIINTVSTS SRESTTVKTS GPITNKEDHT VTDTVSYTTV STSSEIVTTK
STANDAHNDN EPSTVSPTTV KNITKSIGKY STKDYVKVFG IAALIILSAV AIFCITYYIC
NKRSRKYKTE NKV
