ID   HEMA_MEASA              Reviewed;         617 AA.
AC   P35971;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   29-SEP-2021, entry version 96.
DE   RecName: Full=Hemagglutinin glycoprotein;
GN   Name=H;
OS   Measles virus (strain Edmonston-AIK-C vaccine) (MeV) (Subacute sclerose
OS   panencephalitis virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=36408;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8470368; DOI=10.1007/bf01702349;
RA   Mori T., Sasaki K., Hashimoto H., Makino S.;
RT   "Molecular cloning and complete nucleotide sequence of genomic RNA of the
RT   AIK-C strain of attenuated measles virus.";
RL   Virus Genes 7:67-81(1993).
RN   [2]
RP   INTERACTION WITH HUMAN MCP/CD46 AND SLAMF1.
RX   PubMed=12029158; DOI=10.1099/0022-1317-83-6-1431;
RA   Erlenhofer C., Duprex W.P., Rima B.K., ter Meulen V.,
RA   Schneider-Schaulies J.;
RT   "Analysis of receptor (CD46, CD150) usage by measles virus.";
RL   J. Gen. Virol. 83:1431-1436(2002).
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 (By similarity). Interacts with
CC       human MCP/CD46 antigen and SLAMF1. {ECO:0000250,
CC       ECO:0000269|PubMed:12029158}.
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; S58435; AAB26146.1; -; Genomic_RNA.
DR   PIR; F48556; F48556.
DR   SMR; P35971; -.
DR   Proteomes; UP000007775; Genome.
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   1: Evidence at protein level;
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_0000142598"
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   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;  69323 MW;  F7D48744436C1CCA CRC64;
     MSPQRDRINA FYKDNPHPKG SRIVINREHL MIDRPYVLLA VLFVMFLSLI GLLAIAGIRL
     HRAAIYTAEI HKSLSTNLDV TNSIEHQVKD VLTPLFKIIG DEVGLRTPQR FTDLVKFISD
     KIKFLNPDRE YDFRDLTWCI NPPERIKLDY DQYCADVAAE ELMNALVNST LLETRTTNQF
     LAVSKGNCSG PTTIRGQFSN MSLSLLDLYL GRGYNVSSIV TMTSQGMYGG TYLVEKPNLS
     SKRSELSQLS MYRVFEVGVI RNPGLGAPVF HMTNYLEQPV SNDLSNCMVA LGELKLAALC
     HREDSITIPY QGSGKGVSFQ LVKLGVWKSP TDMQSWVTLS TDDPVIDRLY LSSHRGVIAD
     NQAKWAVPTT RTDDKLRMET CFQQACKGKI QALCENPEWA PLKDNRIPSY GVLSVDLSLT
     VELKIKIASG FGPLITHGSG MDLYKSNHNN VYWLTIPPMK NLALGVINTL EWIPRFKVSP
     YLFNVPIKEA GEDCHAPTYL PAEVDGDVKL SSNLVILPGQ DLQYVLATYD TSRVEHAVVY
     YVYSPSRSFS YFYPFRLPIK GVPIELQVEC FTWDQKLWCR HFCVLADSES GGHITHSGMV
     GMGVSCTVTR EDGTNRR