HEMA_MEASH
ID HEMA_MEASH Reviewed; 617 AA.
AC P06830;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 02-DEC-2020, entry version 98.
DE RecName: Full=Hemagglutinin glycoprotein;
GN Name=H;
OS Measles virus (strain Halle) (MeV) (Subacute sclerose panencephalitis
OS virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11236;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3794664; DOI=10.1099/0022-1317-67-12-2695;
RA Gerald C., Buckland R., Barker R., Freeman G., Wild T.F.;
RT "Measles virus haemagglutinin gene: cloning, complete nucleotide sequence
RT analysis and expression in COS cells.";
RL J. Gen. Virol. 67:2695-2703(1986).
RN [2]
RP MUTAGENESIS OF TYR-481.
RX PubMed=8676439; DOI=10.1128/jvi.70.7.4200-4204.1996;
RA Lecouturier V., Fayolle J., Caballero M., Carabana J., Celma M.L.,
RA Fernandez-Munoz R., Wild T.F., Buckland R.;
RT "Identification of two amino acids in the hemagglutinin glycoprotein of
RT measles virus (MV) that govern hemadsorption, HeLa cell fusion, and CD46
RT downregulation: phenotypic markers that differentiate vaccine and wild-type
RT MV strains.";
RL J. Virol. 70:4200-4204(1996).
RN [3]
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; X04720; CAA28427.1; -; Genomic_RNA.
DR PIR; A27007; HMNZHA.
DR SMR; P06830; -.
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_0000142600"
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"
FT MUTAGEN 481
FT /note="Y->N: Severely reduces hemadsorption and abrogates
FT both fusion and CD46 down-regulation in HeLa cells."
FT /evidence="ECO:0000269|PubMed:8676439"
SQ SEQUENCE 617 AA; 69078 MW; 39240D495A525C72 CRC64;
MSPQRDRINA FYKDNPHPKG SRIVINREHL MIDRPYVLLA VLFVMFLSLI GLLAIAGIRL
HRAAIYTAEI HKSLSTNLDV TNSIEHQVKD VLTPLFKIIG DEVGLRTPQR FTDLVKFISD
KIKFLNPDRE YDFRDLTWCI NPPERIKLDY DQYCADVAAE ELMNALVNST LLETRTTNQF
LAVSKGNCSG PTTIRGQFSN MSLSLLDLYL GRGYNVSSIV TMTSQGMYGG TYPVEKPNLS
SKRSELSQLS MYRVFEVSVI RNPGLGAPVF HMTNYLEQPV SNDLSNCMVA LGELKLAALC
HGEDSITIPY QGSGKGVSFQ LVKLGVWKSP TGMQSWVPLS TDDPVIDRLY LSSHRGVIAD
NQAKWAVPTT RTDDKLRMET CFQQACKGKI QALCENPECV PLKDNRIPSY GVLSVDLSLT
VELKIKIASG FGPLITHGSG MDLYKSNHNN VYWLTIPPMK NLALGVINTL EWIPRFKVSP
YLFTVPIKEA GEDCHAPTYL PAEVDGDVKL SSNLVILPGQ DLQYVLATYD TSRVEHAVVY
YVYSPGRSFS YFYPFRLPIK GVPIELQVEC FTWDQKLWCR HFCVLADSES GGHITHSGMV
GMGVSCTVTR EDGTNRR
