ID   HEMA_CDVA4              Reviewed;         607 AA.
AC   Q66001;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 83.
DE   RecName: Full=Hemagglutinin glycoprotein;
GN   Name=H;
OS   Canine distemper virus (strain A92-27/4) (CDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=82826;
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; Z54156; CAA90867.1; -; Genomic_RNA.
DR   SMR; Q66001; -.
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_0000142594"
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"
FT   CARBOHYD        603
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   607 AA;  68260 MW;  A1B711D2840B59C5 CRC64;
     MLSYQDKVGA FYKDNARANS SRLSLVTEDQ GGRRPPYLLF VLLILLVGIM ALLAITGVRF
     HQVSTSNMEF SRLLKEDMEK SEAVHHQVID VLTPLFKIIG DEIGLRLPQK LNEIKQFILQ
     KTNFFNPNRE FDFRDLHWCI NPPSKIKVNF TNYCDTIGIR KSIASAANPI LLSALSRSRG
     DIFPPYRCSG ATTSVGSVFP LSVSLSMSLI SRTSEIINML TAISDGVYGK TYLLVPDYLE
     GEFDTQKIRV FEIGFIKRWL NNMPLLQTTN YMVLPENSKA KVCTIAVGEL TLASLCVDES
     TVLLYHDSNG SQGGILVVTL GIFGATPMDQ VEEVIPVPHP SVEKIHITNH RGFIKDSIAT
     WMVPALVSEK QEEQKNCLES ACQRKSYPMC NQTSWEPFGG GQLPSYGRLT LPLDPSIDLQ
     LNISFTYGPV ILNGDGMDYY ESPLLDSGWL TIPPKNGTVL GLINKASRGD QFTVIPHVLT
     FAPRESSGNC YLPIQTSQIM DKDVLTESNL VVLPTQNFIY VIATYDISRG DHAIVYYVYD
     PIRTISYTHA FRLTTKGRPD FLRIECFVWD DDLWCHQFYR FEADSTNSTT SVENLVRIRF
     SCNRSKP