ID   HEMA_CDVA6              Reviewed;         607 AA.
AC   Q66000;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-DEC-2020, entry version 83.
DE   RecName: Full=Hemagglutinin glycoprotein;
GN   Name=H;
OS   Canine distemper virus (strain A92-6) (CDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=82827;
OH   NCBI_TaxID=9646; Ailuropoda melanoleuca (Giant panda).
OH   NCBI_TaxID=9649; Ailurus fulgens (Lesser panda) (Red panda).
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH   NCBI_TaxID=9665; Mustela.
OH   NCBI_TaxID=9689; Panthera leo (Lion).
OH   NCBI_TaxID=9654; Procyon lotor (Raccoon).
OH   NCBI_TaxID=9704; Zalophus californianus (California sealion).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8601773; DOI=10.1099/0022-1317-77-3-397;
RA   Harder T.C., Kenter M., Vos H., Siebelink K., Huisman W., van Amerongen G.,
RA   Orvell C., Barrett T., Appel M.J.G., Osterhaus A.D.M.E.;
RT   "Canine distemper virus from diseased large felids: biological properties
RT   and phylogenetic relationships.";
RL   J. Gen. Virol. 77:397-405(1996).
CC   -!- FUNCTION: Attaches the virus to cell receptors and thereby initiating
CC       infection. Binding of H protein to the receptor induces a
CC       conformational change that allows the F protein to trigger virion/cell
CC       membranes fusion. The cellular receptor might be SLAM, and may explain
CC       the lymphotropism of the virus (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds canine SLAMF1 at the cell surface. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type
CC       II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC       family. Non-sialidase subfamily. {ECO:0000305}.
CC   -!- CAUTION: Morbiliviruses hemagglutinins have no neuraminidase activity.
CC       {ECO:0000305}.
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DR   EMBL; Z54166; CAA90879.1; -; Genomic_RNA.
DR   SMR; Q66000; -.
DR   GO; GO:0020002; C:host cell plasma 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   GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR000665; Hemagglutn/HN.
DR   InterPro; IPR036278; Sialidase_sf.
DR   Pfam; PF00423; HN; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hemagglutinin; Host cell membrane; Host membrane;
KW   Host-virus interaction; Membrane; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Virion; Virus entry into host cell.
FT   CHAIN           1..607
FT                   /note="Hemagglutinin glycoprotein"
FT                   /id="PRO_0000142595"
FT   TOPO_DOM        1..37
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..607
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        456
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        587
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   607 AA;  68213 MW;  8ECB8ED882BF7592 CRC64;
     MLSYQDKVGA FYKDNARANS SKLSLVTEEQ GGRRPPYLLF VLLILLVGIM ALLAITGVRF
     HQVSTSNMEF SRLLKEDMEK SEAVHHQVID VLTPLFKIIG DEVGLRLPQK LNEIKQFILQ
     KTNFFNPNRE FDFRDLHWCI NPPSKIKVNF TNYCDTIGIR KSIASAANPI LLSAHTGGRG
     DIFPPYRCSG ATTSVGRVFP LSVSLSMSLI SRTSEIINML TAISDGVYGK TYLLVPDYIE
     GEFDTQKIRV FEIGFIKRWL NDMPLLQTTN YMVLPENSKA KVCTIAVGEL TLASLCVDES
     TILLYHDSNG SQDGILVVTL GIFGATPMDQ VEEVIPVAHP SVEKIHITNH RGFIKDSIAT
     WMVPALVSEK QEEQKSCLES ACQRKSYPMC NQTSWEPFGG GQLPSYGRLT LPLDPSIDLQ
     LNISFTYGPV ILNGNGMDYY ESPLLGSGWL TIPPKNGTVL GLINKAGRGD QFTVIPHVLT
     FAPRESSGNC YLPIQTSQIM DKDVLTESNL VVLPTQNFRY VIATYDISRG DHAIVYYVYD
     PIRTISYTHP FRLTTKGRPD FLRIECFVWD DDLWCHQFYR FETDSTNSTT SVENLVRIRF
     SCSRSKP