ID   HEMA_RINDL              Reviewed;         609 AA.
AC   P09460;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   23-FEB-2022, entry version 93.
DE   RecName: Full=Hemagglutinin glycoprotein;
GN   Name=H;
OS   Rinderpest virus (strain L) (RDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=11243;
OH   NCBI_TaxID=9915; Bos indicus (Zebu).
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=89462; Bubalus bubalis (Domestic water buffalo).
OH   NCBI_TaxID=9925; Capra hircus (Goat).
OH   NCBI_TaxID=9933; Gazella (gazelles).
OH   NCBI_TaxID=9894; Giraffa camelopardalis (Giraffe).
OH   NCBI_TaxID=9832; Hippopotamus.
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
OH   NCBI_TaxID=9821; Suidae (pigs).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3629979; DOI=10.1016/0042-6822(87)90042-0;
RA   Tsukiyama K., Sugiyama M., Yoshikawa Y., Yamanouchi K.;
RT   "Molecular cloning and sequence analysis of the rinderpest virus mRNA
RT   encoding the hemagglutinin protein.";
RL   Virology 160:48-54(1987).
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. Down-regulates human MCP/CD46 cell surface expression
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type
CC       II membrane protein {ECO:0000305}. Host membrane; Single-pass type II
CC       membrane protein.
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; M17434; AAA47402.1; -; Genomic_RNA.
DR   PIR; A26799; HMNZRP.
DR   SMR; P09460; -.
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   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 membrane; Host-virus interaction;
KW   Membrane; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..609
FT                   /note="Hemagglutinin glycoprotein"
FT                   /id="PRO_0000142634"
FT   TOPO_DOM        1..34
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..58
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..609
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   609 AA;  67658 MW;  849362D3B64DCAAC CRC64;
     MSSPRDRVNA FYKDNLQFKN TRVVLNKEQL LIERPYMLLA VLFVMFLSLV GLLAIAGIRL
     HRAAVNTAEI NSGLTTSIDI TKSIEYQVKD VLTPLFKIIG DEVGLRTPQR FTDLTKFISD
     KIKFLNPDKE YDFRDINWCI SPPERIKINY DQYCAHTAAE ELITMLVNSS LAGTSVLPTS
     LVNLGRSCTG STTTKGQFSN MSLALSGIYS GRGYNISSMI TITEKGMYGS TYLVGKHNQG
     ARRPSTAWQR DYRVFEVGII RELGLGTPVF HMTNYLELPR QPELEICMLA LGEFKLAALC
     LADNSVALHY GGLRDDHKIR FVKLGVWPSP ADSDTLATLS AVDPTLDGLY ITTHRGIIAA
     GKAVWVVPVT RTDDQRKMGQ CRREACREKP PPFCNSTDWE PLEAGRIPAY GILTIRLGLA
     DKLKLTIISE FGPLITHDSG MDLYTPLDGN EYWLTIPPLQ NSALGTVNTL VLEPSLKISP
     NILTLPIRSG GGDCYTPTYL SDLADDDVKL SSNLVILPSR NLQYVSATYD TSRVEHAIVY
     YIYSAGRLSS YYYPVKLPIK GDPVSLQIGC FPWGLKLWCH HFCSVIDSGT RKQVTHTGAV
     GIEITCNSR