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 08-NOV-2023, entry version 77.
DE RecName: Full=Protein OPG185;
DE AltName: Full=Hemagglutinin;
DE Flags: Precursor;
GN Name=OPG185; Synonyms=HA; ORFNames=A58R;
OS Cowpox virus (strain GRI-90 / Grishak) (CPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Cowpox virus.
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 OPG040 protein on the host plasma membrane. The
CC OPG185-OPG040 complex associates with components of the entry fusion
CC complex (EFC) presumably to avoid superinfection and syncytium
CC formation. Via its interaction with C3/VCP protein, protects the
CC infected cell and probably also the extracellular enveloped virus from
CC complement attack. {ECO:0000250|UniProtKB:Q01218}.
CC -!- SUBUNIT: Heterodimerizes with OPG040. The heterodimer OPG185-OPG040
CC interacts with components of the entry fusion complex OPG143 and
CC OPG094. Heterodimer with C3/VPC protein; disulfide-linked.
CC {ECO:0000250|UniProtKB:Q01218}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:Q01218};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q01218}.
CC Host membrane {ECO:0000250|UniProtKB:Q01218}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:Q01218}. Note=Component of
CC extracellular enveloped virus (EEV) but not intracellular mature virus
CC (IMV). Component of the outermost membrane of EEV.
CC {ECO:0000250|UniProtKB:Q01218}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC -!- PTM: Glycosylated; contains phosphate and sulfate-substituted glycans.
CC O-glycosylation is required for hemagglutination and hemadsorption
CC activities of infected cell membranes. {ECO:0000250|UniProtKB:Q01218}.
CC -!- SIMILARITY: Belongs to the orthopoxvirus OPG185 family. {ECO:0000305}.
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DR EMBL; X94355; CAD90725.1; -; Genomic_DNA.
DR SMR; O72737; -.
DR GlyCosmos; O72737; 6 sites, No reported glycans.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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; Immunoglobulins; 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; Immunoglobulin; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Early protein; 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 OPG185"
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
//
