ID HEMA_MEASE Reviewed; 617 AA. AC P08362; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 27-MAR-2024, entry version 117. DE RecName: Full=Hemagglutinin glycoprotein; GN Name=H; OS Measles virus (strain Edmonston) (MeV) (Subacute sclerose panencephalitis OS virus). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae; OC Morbillivirus; Morbillivirus hominis; Measles morbillivirus. OX NCBI_TaxID=11235; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=3008420; DOI=10.1016/0042-6822(86)90312-0; RA Alkhatib G., Briedis D.J.; RT "The predicted primary structure of the measles virus hemagglutinin."; RL Virology 150:479-490(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2596022; DOI=10.1016/0042-6822(89)90554-0; RA Cattaneo R., Schmid A., Spielhofer P., Kaelin K., Baczko K., Meulen V., RA Pardowitz J., Flanagan S., Rima B.K., Udem S.A.; RT "Mutated and hypermutated genes of persistent measles viruses which caused RT lethal human brain diseases."; RL Virology 173:415-425(1989). RN [3] RP INTERACTION WITH HUMAN MCP/CD46. RX PubMed=8402913; DOI=10.1016/0092-8674(93)80071-l; RA Doerig R.E., Marcil A., Chopra A., Richardson C.D.; RT "The human CD46 molecule is a receptor for measles virus (Edmonston RT strain)."; RL Cell 75:295-305(1993). RN [4] RP FUNCTION. RX PubMed=9811778; DOI=10.1128/jvi.72.12.10292-10297.1998; RA Galbraith S.E., Tiwari A., Baron M.D., Lund B.T., Barrett T., Cosby S.L.; RT "Morbillivirus downregulation of CD46."; RL J. Virol. 72:10292-10297(1998). RN [5] RP INTERACTION WITH HUMAN SLAMF1. RX PubMed=10972291; DOI=10.1038/35022579; RA Tatsuo H., Ono N., Tanaka K., Yanagi Y.; RT "SLAM (CDw150) is a cellular receptor for measles virus."; RL Nature 406:893-897(2000). 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:0000269|PubMed:9811778}. 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:10972291, ECO:0000269|PubMed:8402913}. 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; M14877; AAA46424.1; -; Genomic_RNA. DR EMBL; K01711; AAA75500.1; -; Genomic_RNA. DR PIR; A27006; HMNZED. DR PDB; 2RKC; X-ray; 2.70 A; A=156-617. DR PDB; 2ZB5; X-ray; 3.00 A; A=149-617. DR PDB; 2ZB6; X-ray; 2.60 A; A=149-617. DR PDB; 3ALW; X-ray; 3.55 A; A=184-607. DR PDB; 3ALX; X-ray; 3.15 A; A/B/C/D=184-607. DR PDB; 3ALZ; X-ray; 4.52 A; A=149-617. DR PDB; 3INB; X-ray; 3.10 A; A/B=179-617. DR PDBsum; 2RKC; -. DR PDBsum; 2ZB5; -. DR PDBsum; 2ZB6; -. DR PDBsum; 3ALW; -. DR PDBsum; 3ALX; -. DR PDBsum; 3ALZ; -. DR PDBsum; 3INB; -. DR SMR; P08362; -. DR DIP; DIP-59049N; -. DR IntAct; P08362; 3. DR UniLectin; P08362; -. DR GlyCosmos; P08362; 5 sites, No reported glycans. DR EvolutionaryTrace; P08362; -. DR Proteomes; UP000000833; Genome. 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; IPR049617; MV-h_C. DR InterPro; IPR036278; Sialidase_sf. DR Pfam; PF00423; HN; 1. DR SUPFAM; SSF50939; Sialidases; 1. PE 1: Evidence at protein level; KW 3D-structure; Glycoprotein; Hemagglutinin; Host cell membrane; KW Host membrane; Host-virus interaction; Membrane; Signal-anchor; KW Transmembrane; Transmembrane helix; Viral attachment to host cell; KW Viral envelope protein; Virion; Virus entry into host cell. FT CHAIN 1..617 FT /note="Hemagglutinin glycoprotein" FT /id="PRO_0000142599" 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 HELIX 159..163 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 189..198 FT /evidence="ECO:0007829|PDB:2ZB6" FT HELIX 205..211 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 215..224 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 227..236 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 250..261 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 264..267 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 269..279 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:3INB" FT STRAND 286..292 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 295..307 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 313..315 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 318..327 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 333..339 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 344..350 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 355..359 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 362..371 FT /evidence="ECO:0007829|PDB:2ZB6" FT HELIX 374..385 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 387..389 FT /evidence="ECO:0007829|PDB:2ZB5" FT HELIX 391..395 FT /evidence="ECO:0007829|PDB:2ZB6" FT HELIX 400..403 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 409..418 FT /evidence="ECO:0007829|PDB:2ZB6" FT TURN 420..422 FT /evidence="ECO:0007829|PDB:2ZB5" FT STRAND 425..430 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 442..445 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 451..456 FT /evidence="ECO:0007829|PDB:2ZB6" FT TURN 460..462 FT /evidence="ECO:0007829|PDB:3INB" FT STRAND 466..471 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 477..486 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 488..493 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 495..497 FT /evidence="ECO:0007829|PDB:2ZB6" FT TURN 504..506 FT /evidence="ECO:0007829|PDB:3INB" FT STRAND 509..511 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 519..521 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 524..530 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 531..535 FT /evidence="ECO:0007829|PDB:3INB" FT STRAND 538..543 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 548..552 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 565..572 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 574..584 FT /evidence="ECO:0007829|PDB:2ZB6" FT TURN 588..590 FT /evidence="ECO:0007829|PDB:2ZB6" FT STRAND 595..606 FT /evidence="ECO:0007829|PDB:2ZB6" SQ SEQUENCE 617 AA; 69250 MW; 0E5A05AEDA43D9C6 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 HGEDSITIPY QGSGKGVSFQ LVKLGVWKSP TDMQSWVPLS 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 GGHITHSGME GMGVSCTVTR EDGTNRR //