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 22-FEB-2023, entry version 92. 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}. 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; D10549; BAA01406.1; -; mRNA. DR PIR; JU0273; JU0273. DR SMR; P28081; -. DR GlyCosmos; P28081; 5 sites, No reported glycans. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C: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 CDD; cd15467; MV-h; 1. DR Gene3D; 2.120.10.10; -; 1. DR InterPro; IPR000665; Hemagglutn/HN. DR InterPro; IPR036278; Sialidase_sf. DR Pfam; PF00423; HN; 1. DR SUPFAM; SSF50939; Sialidases; 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 //