HEMA_MEASC
ID HEMA_MEASC Reviewed; 617 AA.
AC Q786F2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 02-JUN-2021, entry version 54.
DE RecName: Full=Hemagglutinin glycoprotein;
GN Name=H;
OS Measles virus (strain Ichinose-B95a) (MeV) (Subacute sclerose
OS panencephalitis virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=645098;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10949953; DOI=10.1023/a:1008196729676;
RA Takeuchi K., Miyajima N., Kobune F., Tashiro M.;
RT "Comparative nucleotide sequence analyses of the entire genomes of B95a
RT cell-isolated and vero cell-isolated measles viruses from the same
RT patient.";
RL Virus Genes 20:253-257(2000).
RN [2]
RP INTERACTION WITH HUMAN NECTIN4.
RX PubMed=22048310; DOI=10.1038/nature10639;
RA Muhlebach M.D., Mateo M., Sinn P.L., Prufer S., Uhlig K.M., Leonard V.H.,
RA Navaratnarajah C.K., Frenzke M., Wong X.X., Sawatsky B., Ramachandran S.,
RA McCray P.B. Jr., Cichutek K., von Messling V., Lopez M., Cattaneo R.;
RT "Adherens junction protein nectin-4 is the epithelial receptor for measles
RT virus.";
RL Nature 480:530-533(2011).
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 MCP/CD46 antigen and SLAMF1 (By
CC similarity). Interacts with human NECTIN4; this interaction allows
CC virus infection of the respiratory epithelium. {ECO:0000250,
CC ECO:0000269|PubMed:22048310}.
CC -!- INTERACTION:
CC Q786F2; Q96NY8: NECTIN4; Xeno; NbExp=4; IntAct=EBI-5323300, EBI-4314784;
CC Q786F2; Q13291: SLAMF1; Xeno; NbExp=2; IntAct=EBI-5323300, EBI-4315002;
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; AB016162; BAA34982.1; -; Genomic_RNA.
DR PIR; PQ0377; PQ0377.
DR PIR; PQ0381; PQ0381.
DR RefSeq; NP_056923.1; NC_001498.1.
DR PDB; 4GJT; X-ray; 3.10 A; A=156-617.
DR PDBsum; 4GJT; -.
DR SMR; Q786F2; -.
DR DIP; DIP-59438N; -.
DR IntAct; Q786F2; 2.
DR GeneID; 1489801; -.
DR KEGG; vg:1489801; -.
DR Proteomes; UP000008699; 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_0000394712"
FT TOPO_DOM 1..37
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Note=Membrane anchor"
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 CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4GJT"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:4GJT"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 249..261
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 269..279
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 362..372
FT /evidence="ECO:0007829|PDB:4GJT"
FT HELIX 374..384
FT /evidence="ECO:0007829|PDB:4GJT"
FT TURN 389..393
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4GJT"
FT HELIX 400..403
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 408..416
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:4GJT"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 523..531
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 537..543
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 568..573
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 576..585
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:4GJT"
FT STRAND 594..604
FT /evidence="ECO:0007829|PDB:4GJT"
SQ SEQUENCE 617 AA; 69174 MW; 7E877598258DEC5E CRC64;
MSPQRDRINA FYKDNPHPKG SRIVINREHL MIDRPYVLLA VLFVMFLSLI GLLAIAGIRL
HRAAIYTAEI HKSLSTNLDV TNSIEHQVKD VLTPLFKIIG DEVGLRTPQR FTDLVKFISD
KIKFLNPDRE YDFRDLTWCI NPPERIKLDY DQYCADVAAE ELMNALVNST LLEARATNQF
LAVSKGNCSG PTTIRGQFSN MSLSLLDLYL SRGYNVSSIV TMTSQGMYGG TYLVGKPNLS
SKGSELSQLS MHRVFEVGVI RNPGLGAPVF HMTNYFEQPV SNDFSNCMVA LGELKFAALC
HREDSITIPY QGSGKGVSFQ LVKLGVWKSP TDMRSWVPLS TDDPVIDRLY LSSHRGVIAD
NQAKWAVPTT RTDDKLRMET CFQQACKGKN QALCENPEWA PLKDNRIPSY GVLSVNLSLT
VELKIKIASG FGPLITHGSG MDLYKTNHNN VYWLTIPPMK NLALGVINTL EWIPRFKVSP
NLFTVPIKEA GEDCHAPTYL PAEVDGDVKL SSNLVILPGQ DLQYVLATYD TSRVEHAVVY
YVYSPSRSFS YFYPFRLPIK GVPIELQVEC FTWDKKLWCR HFCVLADSES GGHITHSGMV
GMGVSCTVTR EDGTNRR
