ID   HEMA_CDVC               Reviewed;         607 AA.
AC   Q65999;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 90.
DE   RecName: Full=Hemagglutinin glycoprotein;
GN   Name=H;
OS   Canine distemper virus (strain Convac vaccine) (CDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=82828;
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=1891961; DOI=10.1016/0168-1702(91)90048-z;
RA   Koevamees J., Blixenkrone-Moeller M., Norrby E.;
RT   "The nucleotide and predicted amino acid sequence of the attachment protein
RT   of canine distemper virus.";
RL   Virus Res. 19:223-234(1991).
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; Z35493; CAA84626.1; -; Genomic_RNA.
DR   PIR; S49017; S49017.
DR   SMR; Q65999; -.
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_0000142596"
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        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;  68198 MW;  8000979F0A62352F CRC64;
     MLSYQDKAGA FYKDNARANS TKLSLVTEEH GGRRPPYLLF VLLVLLVGIL ALLAITGVRF
     HQVSTSNMEF SRLLKEDMEK SEAVHHQVID VLTPLFKIIG DEIGSRLPQK LNEIKQFILQ
     KTNFFNPNRE FDFRDLHWCI NPPSKVKVNF TNYCESIGIR KAIASAANPI LLSALPGGRS
     DIFPPHRCSG ATTSVGKVFP LSVSLSMSLI SRTSEIINML TAISDGVYGK TYLLAPDDIE
     REFDTQEIRV FEIGFIKRWL NDMPSLQTTN YMVLPENSKA KVCTIAVGEL TLASLCVEES
     TVLLYHDSSG SQDGILVVTL GIFGTTPMDH IEEVIPVAHP SMEKIHITNH RGFIKDSIAT
     WMVPALASEK QEEQKGCLES ACQRKPYPMC NQTSWEPFGG RQLPSYGRLT LPLDASVDLQ
     LNISFTYGPV ILNGDGMDYY ESPLLNSGWL TIPPKNGTIL GLINKAGRGD QFTVIPHVLT
     FAPMESSGNC YLPIQTSQII DRDVLIESNL VVLPTQSFRY VIATYDISRS DHAIVYYVYD
     PIRTISYTHP FRLTTKGRPD FLRIECFVWD DNLWCHQFYR FEANIANSTT SVENLVRIRF
     SCNRSNP