HEMA_INCNA
ID HEMA_INCNA Reviewed; 641 AA.
AC P17005;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Hemagglutinin-esterase-fusion glycoprotein;
DE Short=HEF;
DE EC=3.1.1.53;
DE Contains:
DE RecName: Full=Hemagglutinin-esterase-fusion glycoprotein chain 1;
DE Short=HEF1;
DE Contains:
DE RecName: Full=Hemagglutinin-esterase-fusion glycoprotein chain 2;
DE Short=HEF2;
DE Flags: Precursor; Fragment;
GN Name=HE;
OS Influenza C virus (strain C/Nara/1982).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Gammainfluenzavirus.
OX NCBI_TaxID=203232;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2773313; DOI=10.1016/0042-6822(89)90114-1;
RA Adachi K., Kitame F., Sugawara K., Nishimura H., Nakamura K.;
RT "Antigenic and genetic characterization of three influenza C strains
RT isolated in the Kinki district of Japan in 1982-1983.";
RL Virology 172:125-133(1989).
CC -!- FUNCTION: Binds to the N-acetyl-9-O-acetylneuraminic acid residues on
CC the cell surface, bringing about the attachment of the virus particle
CC to the cell. Plays a major role in the determination of host range
CC restriction and virulence. Class I viral fusion protein. Responsible
CC for penetration of the virus into the cell cytoplasm by mediating the
CC fusion of the membrane of the endocytosed virus particle with the
CC endosomal membrane. Low pH in endosomes induce an irreversible
CC conformational change in HEF2, releasing the fusion hydrophobic
CC peptide. Several trimers are required to form a competent fusion pore.
CC Displays a receptor-destroying activity which is a neuraminidate-O-
CC acetyl esterase. This activity cleaves off any receptor on the cell
CC surface, which would otherwise prevent virions release. These cleavages
CC prevent self-aggregation and ensure the efficient spread of the progeny
CC virus from cell to cell (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-9-O-acetylneuraminate = acetate + H(+) + N-
CC acetylneuraminate; Xref=Rhea:RHEA:22600, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28999, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35418; EC=3.1.1.53;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-4-O-acetylneuraminate = acetate + H(+) + N-
CC acetylneuraminate; Xref=Rhea:RHEA:25564, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29006, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35418; EC=3.1.1.53;
CC -!- SUBUNIT: Homotrimer of disulfide-linked HEF1-HEF2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Host cell membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- PTM: In natural infection, inactive HEF is matured into HEF1 and HEF2
CC outside the cell by one or more trypsin-like, arginine-specific
CC endoprotease. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses
CC hemagglutinin-esterase family. {ECO:0000305}.
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DR EMBL; M25362; AAA43790.1; -; Genomic_RNA.
DR PIR; B32665; HMIVEB.
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:0106331; F:sialate 4-O-acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; 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; IPR008980; Capsid_hemagglutn.
DR InterPro; IPR007142; Hemagglutn-estrase_core.
DR InterPro; IPR003860; Hemagglutn-estrase_hemagglutn.
DR InterPro; IPR014831; Hemagglutn_stalk_influenz-C.
DR Pfam; PF03996; Hema_esterase; 1.
DR Pfam; PF02710; Hema_HEFG; 1.
DR Pfam; PF08720; Hema_stalk; 1.
DR SUPFAM; SSF49818; SSF49818; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Hemagglutinin;
KW Host cell membrane; Host membrane; Host-virus interaction; Hydrolase;
KW Membrane; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT CHAIN 1..432
FT /note="Hemagglutinin-esterase-fusion glycoprotein chain 1"
FT /id="PRO_0000039158"
FT CHAIN 433..641
FT /note="Hemagglutinin-esterase-fusion glycoprotein chain 2"
FT /id="PRO_0000039159"
FT TOPO_DOM 1..616
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 638..641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Fusion domain-1"
FT /evidence="ECO:0000250"
FT REGION 27..137
FT /note="Esterase domain-1"
FT /evidence="ECO:0000250"
FT REGION 137..296
FT /note="N-acetyl-9-O-acetylneuraminic acid binding"
FT /evidence="ECO:0000250"
FT REGION 297..351
FT /note="Esterase domain-2"
FT /evidence="ECO:0000250"
FT REGION 352..637
FT /note="Fusion domain-2"
FT /evidence="ECO:0000250"
FT ACT_SITE 57
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 352
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 355
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 6..569
FT /note="Interchain (between HEF1 and HEF2 chains)"
FT /evidence="ECO:0000250"
FT DISULFID 106..151
FT /evidence="ECO:0000250"
FT DISULFID 126..174
FT /evidence="ECO:0000250"
FT DISULFID 196..238
FT /evidence="ECO:0000250"
FT DISULFID 215..302
FT /evidence="ECO:0000250"
FT DISULFID 223..275
FT /evidence="ECO:0000250"
FT DISULFID 332..338
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 641 AA; 70561 MW; FA2477DFF44B3319 CRC64;
EKIKICLQKQ VNSSFSLHNG FGGNLYATEE KRMFELVKPK AGASVLNQST WIGFGDSRTD
KSNPNFPRSA DVSVKTANKF RSLTGGSLML SMFGPPGKVD YLYQGCGKHK VFYEGVNWSP
HAAIDCYRKN WTDIKLNFQK NIYELASQSH CMSLVNALDK TIPLQATAGV AGNCNNSFLK
NPALYTQEVT PPXXKCGKEN LAFFTLPTQF GTYECRLHLV ASCYFIYDSK EVYNKRGCDN
YFQVIYDSSG KVVGGLDNRV SPYTGNSGDT PTMQCDMIQL KPGRYSVRSS PRFLLMPERS
YCFDMKEKGP VTAVQSIWGK DRKSDYAVDQ ACLSTPGCML IQKQKPYTGE ADDHHGDQEM
RELLSGLDYE ARCISQSGWV NETSPFTEEY LLPPKFGRCP LAAKEESIPK IPDGLLIPTS
GTDTTVTKPK SRIFGIDDLI IGLLFVAIVE AGIGGYLLGS RKESGGGVTK ESAEKGFEKI
GNDIQILRSS TNIAIEKLND RISHDEQAIR DLTLEIENAR SEALLGELGI IRALLVGNIS
IGLQESLWEL ASEITNRAGD LAVEISPGCW IIDNNICDQS CQNFIFKFNE TAPVPTIPPL
DTKIDLQSDP FYWGSSLGLA ITAAISLAAL VISGIAICRT K
