HEMA_MEASE
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 23-FEB-2022, entry version 112.
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.
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}.
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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; 2.
DR UniLectin; P08362; -.
DR EvolutionaryTrace; P08362; -.
DR Proteomes; UP000000833; Genome.
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 3D-structure; Glycoprotein; Hemagglutinin; Host cell membrane;
KW Host membrane; Host-virus interaction; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW 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
