ID   HEMA_RINDR              Reviewed;         609 AA.
AC   P41355;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   23-FEB-2022, entry version 107.
DE   RecName: Full=Hemagglutinin glycoprotein;
GN   Name=H;
OS   Rinderpest virus (strain RBOK) (RDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=36409;
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=7897350; DOI=10.1099/0022-1317-76-3-593;
RA   Baron M.D., Barrett T.;
RT   "Sequencing and analysis of the nucleocapsid (N) and polymerase (L) genes
RT   and the terminal extragenic domains of the vaccine strain of rinderpest
RT   virus.";
RL   J. Gen. Virol. 76:593-602(1995).
RN   [2]
RP   FUNCTION.
RX   PubMed=9811778; DOI=10.1128/jvi.72.12.10292-10297.1998;
RA   Galbraith S.E., Tiwari A., Baron M.D., Lund B.T., Barrett T., Cosby S.L.;
RT   "Morbillivirus downregulation of CD46.";
RL   J. Virol. 72:10292-10297(1998).
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 (By similarity). Down-regulates human MCP/CD46 cell
CC       surface expression. {ECO:0000250, ECO:0000269|PubMed:9811778}.
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; Z30697; CAA83182.1; -; Genomic_RNA.
DR   PIR; S43009; S43009.
DR   PDB; 3PWU; X-ray; 1.90 A; C=407-415.
DR   PDBsum; 3PWU; -.
DR   SMR; P41355; -.
DR   Proteomes; UP000008654; Genome.
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   1: Evidence at protein level;
KW   3D-structure; Glycoprotein; Hemagglutinin; 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..609
FT                   /note="Hemagglutinin glycoprotein"
FT                   /id="PRO_0000142635"
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        187
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;  67863 MW;  0DC8E652E29DCBBE CRC64;
     MSPPRDRVDA YYKDNFQFKN TRVVLNKEQL LIERPCMLLT VLFVMFLSLV GLLAIAGIRL
     HRAAVNTAKI NNDLTTSIDI TKSIEYQVKD VLTPLFKIIG DEVGLRTPQR FTDLTKFISD
     KIKFLNPDKE YDFRDINWCI NPPERIKIDY DQYCAHTAAE DLITMLVNSS LTGTTVPRTS
     LVNLGRNCTG PTTTKGQFSN ISLTLSGIYS GRGYNISSMI TITGKGMYGS TYLVGKYNQR
     ARRPSKVWHQ DYRVFEVGII RELGVGTPGF HMTNYLELPR QPELETCMLA LGESKLAALC
     LADSPVALHY GRVGDDNKIR FVKLGVWASP ADRDTLATLS AIDPTLDGLY ITTHRGIIAA
     GTAIWAVPVT RTDDQVKMGK CRLEACRDRP PPFCNSTDWE PLEAGRIPAY GVLTIKLGLA
     DEPKVDIISE FGPLITHDSG MDLYTSFDGT KYWLTTPPLQ NSALGTVNTL VLEPSLKISP
     NILTLPIRSG GGDCYIPTYL SDRADDDVKL SSNLVILPSR DLQYVSATYD ISRVEHAIVY
     HIYSTGRLSS YYYPFKLPIK GDPVSLQIEC FPWDRKLWCH HFCSVVDSGT GEQVTHIGVV
     GIKITCNGK