ID   HEMA_MEASY              Reviewed;         620 AA.
AC   P28081;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   07-OCT-2020, entry version 90.
DE   RecName: Full=Hemagglutinin glycoprotein;
GN   Name=H;
OS   Measles virus (strain Yamagata-1) (MeV) (Subacute sclerose panencephalitis
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=11239;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2402882; DOI=10.1007/bf00678407;
RA   Komase K., Haga T., Yoshikawa Y., Sato T.A., Yamanouchi K.;
RT   "Molecular analysis of structural protein genes of the Yamagata-1 strain of
RT   defective subacute sclerosing panencephalitis virus. III. Nucleotide
RT   sequence of the hemagglutinin gene.";
RL   Virus Genes 4:163-172(1990).
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}.
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DR   EMBL; D10549; BAA01406.1; -; mRNA.
DR   PIR; JU0273; JU0273.
DR   SMR; P28081; -.
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   2: Evidence at transcript 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..620
FT                   /note="Hemagglutinin glycoprotein"
FT                   /id="PRO_0000142602"
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..620
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   620 AA;  69602 MW;  30641B0DA2B48A68 CRC64;
     MSPQRDRTNA FYKDNPHPKG SRIVINREHL MIDRPYVLLA ILFVMFLSLI GLLAIAGIRL
     HQAAIHTAEI HKSLSTNLDV TNSIEHQVKD VLTPLFKIIG DEVGLRTPQR FTDLVKFISD
     KIKFLNPDRE YDFRDLNWCI NPPERIKLDY DQYCADVAAE ELMNALVNST LLETRTTNQF
     LAVSKGNCSG PTTIRGQFSN MSTSLLDLYL SRGYNVSSIV TMTSQGMYGG TYLVEKPNLS
     SKRSELSQLS MYRVFEVGVI RNPGLGAPVF HMTNYFEQPV SNDLSNCMVA LGEFKLAALC
     HREDSITIPY QGSGKGVSFQ LVNLGVWKSP TDMQSWIPLS TDDPVIDRLY LSSHRGVIAD
     NQAKWAVPTT RTDDKLRMET CFQQACKGKI QALCENPEWA PLKDNRIPSY GVLSVDLSPT
     VELKIKIASG FGPLITHGSG MDLYKSNHNN VYWLTIPPMK NLALGVINTL EWIPRFKVSP
     NLFTVPIKEA GKDCHAPTYL PAEVDGDVKL SSNLVILPGQ DLQYVLATYD TSRVEHAVVY
     YVYSPGRSFS YFYPFRLPIR GVPIELQVEC FTWDQKLWCR HFCVLANSES GGHITHSGMV
     GMGVSCTVTR EDGTNRRQSC