ID Q998N5_9MONO Unreviewed; 621 AA. AC Q998N5; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 29-MAY-2024, entry version 102. DE RecName: Full=Hemagglutinin glycoprotein {ECO:0000256|ARBA:ARBA00020483}; GN Name=H {ECO:0000313|EMBL:BAB39847.1}; OS Measles morbillivirus. OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae; OC Morbillivirus; Morbillivirus hominis. OX NCBI_TaxID=11234 {ECO:0000313|EMBL:BAB39847.1}; RN [1] {ECO:0000313|EMBL:BAB39847.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Osaka-3 {ECO:0000313|EMBL:BAB39847.1}; RX PubMed=11270608; RA Furukawa K., Ayata M., Kimura M., Seto T., Matsunaga I., Murata R., RA Yamano T., Ogura H.; RT "Hemadsorption expressed by cloned H genes from subacute sclerosing RT panencephalitis (SSPE) viruses and their possible progenitor measles RT viruses isolated in Osaka, Japan."; RL Microbiol. Immunol. 45:59-68(2001). 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. {ECO:0000256|ARBA:ARBA00037156}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single- CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Virion CC membrane {ECO:0000256|ARBA:ARBA00004208}; Single-pass type II membrane CC protein {ECO:0000256|ARBA:ARBA00004208}. CC -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase CC family. Non-sialidase subfamily. {ECO:0000256|ARBA:ARBA00006578}. 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; AB045307; BAB39847.1; -; Genomic_RNA. DR PIR; PQ0377; PQ0377. DR PIR; PQ0381; PQ0381. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. 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:symbiont 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; IPR049617; MV-h_C. DR InterPro; IPR036278; Sialidase_sf. DR Pfam; PF00423; HN; 1. DR SUPFAM; SSF50939; Sialidases; 1. PE 3: Inferred from homology; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Hemagglutinin {ECO:0000256|ARBA:ARBA00022546, KW ECO:0000256|RuleBase:RU004216}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804}; KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879, KW ECO:0000256|RuleBase:RU004216}; KW Virion {ECO:0000256|ARBA:ARBA00022879, ECO:0000256|RuleBase:RU004216}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}. FT TRANSMEM 36..62 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 621 AA; 69657 MW; 0D49717D1D630F11 CRC64; MSPQRDRTNA FHKDNPHPKG SRIVINREHL MIDRPYVLLA VLFVMFLSLI GLLAIAGIRL HWAAIYTAEI HKSLSTNLDV TNSIEHQVKD VLTPLFKIIG DEVGLRIPQR FTDLVKFISD KIKFLNLDRE YNFRDLTWCI NPPERIKLDY DQYCADVAAE ELMNALVNST LLETRTTNQF LAVSKGNCSG PTTIRGQLSN MSLSLLDLYL SRGYNVSSII TMTSQGMYGG TYLVEKPNLS SKGSELSQLS IYRVFEVGVI RNPGLGAPVF HMTNYFEQPV SNDLSNCMVA LGELKLAALC HGEDSITIPY QGSGKGVSFQ LVKLGVWKSP TDMQSWVPLS TDDPVIDRLY LSSHRGVIAD NQAKWAVPTT RTDDKLRMET CFQQACKGKI QALCENPEWA PLKDNRIPSY GVLSVNLSLT VELKIKIASG FGPLITHGSG MDLYKSNHNN VYWLTIPPMK NLALGVINTL EWIPRFKVSP NFFTVPIKEA GEDCHAPTYL PAEVDGDVNL SSNLVILPGQ DLQYVLATYD TSRVEHAVVY YVYSPSRSFS YFYPFRLPIK GVPIELQVEC FTWDQKLWCR HFCVLADSES GGHITHSGMV GMGVSCTVTR EDGTNRRYSR Q //