ID Q9Q206_9ORTO Unreviewed; 640 AA.
AC Q9Q206;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Hemagglutinin-esterase-fusion glycoprotein {ECO:0000256|ARBA:ARBA00022176, ECO:0000256|RuleBase:RU362095};
DE EC=3.1.1.53 {ECO:0000256|ARBA:ARBA00013141, ECO:0000256|RuleBase:RU362095};
DE Flags: Fragment;
GN Name=HE {ECO:0000256|RuleBase:RU362095, ECO:0000313|EMBL:BAA88402.1};
OS Influenza C virus (C/Yamagata/5/92).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Gammainfluenzavirus;
OC Gammainfluenzavirus influenzae; Influenza C virus.
OX NCBI_TaxID=224310 {ECO:0000313|EMBL:BAA88402.1};
RN [1] {ECO:0000313|EMBL:BAA88402.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C/Yamagata/5/92 {ECO:0000313|EMBL:BAA88402.1};
RA Gao P.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAA88402.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C/Yamagata/5/92 {ECO:0000313|EMBL:BAA88402.1};
RX PubMed=8757991;
RA Peng G., Hongo S., Kimura H., Muraki Y., Sugawara K., Kitame F.,
RA Numazaki Y., Suzuki H., Nakamura K.;
RT "Frequent occurrence of genetic reassortment between influenza C virus
RT srains in nature.";
RL J. Gen. Virol. 77:1489-1492(1996).
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. {ECO:0000256|ARBA:ARBA00024709,
CC ECO:0000256|RuleBase:RU362095}.
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 Evidence={ECO:0000256|ARBA:ARBA00000954,
CC ECO:0000256|RuleBase:RU362095};
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 Evidence={ECO:0000256|ARBA:ARBA00001221};
CC -!- SUBUNIT: Homotrimer of disulfide-linked HEF1-HEF2.
CC {ECO:0000256|ARBA:ARBA00011223, ECO:0000256|RuleBase:RU362095}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}. Virion membrane
CC {ECO:0000256|RuleBase:RU362095}; Single-pass type I membrane protein
CC {ECO:0000256|RuleBase:RU362095}. Host cell membrane
CC {ECO:0000256|RuleBase:RU362095}; Single-pass type I membrane protein
CC {ECO:0000256|RuleBase:RU362095}.
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:0000256|RuleBase:RU362095}.
CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses
CC hemagglutinin-esterase family. {ECO:0000256|ARBA:ARBA00010920,
CC ECO:0000256|RuleBase:RU362095}.
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DR EMBL; D78433; BAA88402.1; -; Genomic_RNA.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma 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:0106331; F:sialate 4-O-acetylesterase activity; IEA:RHEA.
DR GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:RHEA.
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 Gene3D; 2.20.70.20; -; 2.
DR Gene3D; 3.90.20.10; -; 1.
DR HAMAP; MF_04072; INFV_HEMA; 1.
DR InterPro; IPR008980; Capsid_hemagglutn.
DR InterPro; IPR007142; Hemagglutn-estrase_core.
DR InterPro; IPR003860; Hemagglutn-estrase_hemagglutn.
DR InterPro; IPR001364; Hemagglutn_influenz_A/B.
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; SSF58064; Influenza hemagglutinin (stalk); 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR SUPFAM; SSF49818; Viral protein domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU362095};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510};
KW Fusion of virus membrane with host membrane
KW {ECO:0000256|ARBA:ARBA00022506};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hemagglutinin {ECO:0000256|ARBA:ARBA00022546,
KW ECO:0000256|RuleBase:RU362095};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511,
KW ECO:0000256|RuleBase:RU362095};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870,
KW ECO:0000256|RuleBase:RU362095};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362095};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362095};
KW Transmembrane {ECO:0000256|RuleBase:RU362095};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362095};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|RuleBase:RU362095};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT TRANSMEM 610..637
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362095"
FT DOMAIN 25..404
FT /note="Haemagglutinin-esterase glycoprotein core"
FT /evidence="ECO:0000259|Pfam:PF03996"
FT DOMAIN 137..289
FT /note="Haemagglutinin-esterase glycoprotein haemagglutinin"
FT /evidence="ECO:0000259|Pfam:PF02710"
FT DOMAIN 432..606
FT /note="Haemagglutinin stalk influenza C"
FT /evidence="ECO:0000259|Pfam:PF08720"
FT COILED 494..521
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAA88402.1"
SQ SEQUENCE 640 AA; 70455 MW; 899EB87E3DD55F07 CRC64;
EKIKICLQKQ VNSSFSLHNG FGGNLYATEE KRMFELVKPK AGASVLNQST WIGFGDSRTD
KSNPNFPRSA DVSVKTANKF RSSTGGSLML SMFGPPGKVD YLYQGCGKHK VFYEGVNWSP
HAAIDCYRKN WTDIKLNFQK NIYELASQSH CMSLVNALDK TIPLQATAGV AGNCNNSFLK
NPALYTQEVT PPEKCGKENL AFFTLPTQFG TYECRLHLVA SCYFIYDSKE VYNKRGCDNY
FQVIYDSSGK VVGGLDNRVS PYTGNTGDTP TMQCDMIQLK PGRYSVRSSP RFLLMPERSY
CFDMKEKGPV TAVQSIWGKD RKSDYAVDQA CLSTPGCMLI QKQKPYTGEA DDHHGDQEMR
ELLSGLDYEA RCISQSGWVN ETSPFTEEYL LPPKFGRCPL AAKEESIPKI PDGLLIPTSG
TDTTVTKPKS RIFGIDDLII GLLFVAIVEA GIGGYLLGSR KESGGGVTKE SAEKGFEKIG
NDIQILRSST NIAIEKLNDR ISHDEQAIRD LTLEIENARS EALLGELGII RALLVGNISI
GLQESLWELA SEITNRAGDL AVEISPGCWI IDNNICDQSC QNFIFKFNET APVPTIPPLD
TKIDLQSDPF YWGSSLGLAI TAAISLAALV ISGIAICRTK
//
