ID   HEMA_MEASI              Reviewed;         617 AA.
AC   P26028;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   02-JUN-2021, entry version 92.
DE   RecName: Full=Hemagglutinin glycoprotein;
GN   Name=H;
OS   Measles virus (strain IP-3-Ca) (MeV) (Subacute sclerose panencephalitis
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=11237;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1585658; DOI=10.1016/0042-6822(92)90552-z;
RA   Schmid A., Spielhofer P., Cattaneo R., Baczko K., Ter Meulen V.,
RA   Billeter M.A.;
RT   "Subacute sclerosing panencephalitis is typically characterized by
RT   alterations in the fusion protein cytoplasmic domain of the persisting
RT   measles virus.";
RL   Virology 188:910-915(1992).
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. May use human CD46 and/or SLAMF1 as receptors for
CC       viral entry into the cell. The high degree of interaction between H and
CC       MCP/CD46 results in down-regulation of the latter from the surface of
CC       infected cells, rendering them more sensitive to c3b-mediated
CC       complement lysis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with human NECTIN4; this interaction allows virus
CC       infection of the respiratory epithelium. Interacts with human MCP/CD46
CC       antigen and SLAMF1 (By similarity). {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X16566; CAA34569.1; -; Genomic_RNA.
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..617
FT                   /note="Hemagglutinin glycoprotein"
FT                   /id="PRO_0000142601"
FT   TOPO_DOM        1..37
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..617
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        238
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   617 AA;  68626 MW;  8FF518CE4A4CB4F3 CRC64;
     MSPQRDRINA FDKDNPHPXX XXXXXXXXXX XXXRPYVLLA VLFVMFLSLI GLLAIAGIRF
     HRAAIYTAEI HKSLSTNLDV TNSIEHQVKD VLTPLFKIIG DEVGLRTPQR FTDLVKFISD
     KIKFLNPDRE YDFRDLTWCI NPPERIKLDY DQYCADVAAE ELMNALVNST LLETRTTNQF
     LAVSKGNCSG PTTIRGQFSN MSLSLLDLYL SRSYNVSSIV TMTSQGMHGG TYLVGKPNLS
     NKGSELSQLS MYRVFEVGVI RNPGLGAPVF HMTNYFEQPV SNDLSNCMVA LGELKLAALC
     HGEDSITIPY QGSGKGVSIQ LVKLGVWKSP TDMQSWVPLS TDDPVIDRLY LSSHRGVIAD
     NQAKWAVPTT RTDDKLRMET CFQQACRGEV QALCEDPEWA PLKDGRIPSY GVLSVDLSLT
     VELKIKIASG FGPLITRGSG MDLYRSNHNN VCWLAVPPMK SLALGVVNTL EWMPGFKVGP
     YLFTVPIKEA GEDCHAPAYL PAEVDGDVKL SSNLVILPGQ DLQYVLATYD TSRVEHAVVY
     YVYSPGRSFS YFYPFRLPIK GVPIELQVEC FTWDQKLWCR HFCVLADSES GGHITHSGMV
     GMGVSCTVTR EDGTNCR