ID Q8B079_INCM3 Unreviewed; 641 AA.
AC Q8B079;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 85.
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:BAC54290.1};
OS Influenza C virus (strain C/Miyagi/5/1991).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Gammainfluenzavirus;
OC Gammainfluenzavirus influenzae; Influenza C virus.
OX NCBI_TaxID=199345 {ECO:0000313|EMBL:BAC54290.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1] {ECO:0000313|EMBL:BAC54290.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C/Miyagi/5/91 {ECO:0000313|EMBL:BAC54290.1};
RX PubMed=12502803; DOI=10.1128/JVI.77.2.871-881.2003;
RA Matsuzaki Y., Mizuta K., Sugawara K., Tsuchiya E., Muraki Y., Hongo S.,
RA Suzuki H., Nishimura H.;
RT "Frequent reassortment among influenza C viruses.";
RL J. Virol. 77:871-881(2003).
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}.
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; AB086659; BAC54290.1; -; 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 611..638
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362095"
FT DOMAIN 25..405
FT /note="Haemagglutinin-esterase glycoprotein core"
FT /evidence="ECO:0000259|Pfam:PF03996"
FT DOMAIN 137..290
FT /note="Haemagglutinin-esterase glycoprotein haemagglutinin"
FT /evidence="ECO:0000259|Pfam:PF02710"
FT DOMAIN 433..607
FT /note="Haemagglutinin stalk influenza C"
FT /evidence="ECO:0000259|Pfam:PF08720"
FT COILED 495..522
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAC54290.1"
SQ SEQUENCE 641 AA; 70401 MW; 919220CD1C3102BD CRC64;
EKIKICLQKQ VNSSFSLHNG FGGNLYATEE KRMFELVKPK AGASVLNQST WIGFGDSRTD
KSNSAFPRSA DVSAKTANKF RSLSGGSLML SMFGPPGKVD YLYQGCGKHK VFYEGVNWSP
HAAINCYRKN WTDIKLNFQK NIYELASQSH CMSLVNALDK TIPLQVTAGT AGNCNNSFLK
NPALYTQEVK PSENKCGEEN LAFFTLPTQF GTYECKLHLV ASCYFIYDSK EVYNKRGCGN
YFQVIYDSSG KVVGGLDNRV SPYTGNSGDT PTMQCDMLQL KPGRYSVRSS PRFLLMPERS
YCFDMKEKGP VTAVQSIWGK GRESDYAVDQ ACLSTPGCML IQKQKPYIGE ADDHHGDQEM
RELLSGLEYE ARCISQSGWV NETSPFTEKY LLPPKFGRCP LAAKEESIPK IPDGLLIPTS
GTDTTVTKPK SRIFGIDDLI IGLLFVAIVE AGIGGYLLGS RKESGGGVTK ESAEKGFEKI
GNDIQILRSS TNIAIEKLND RISHDEQAIR DLTLEIENAR SEALLGELGI IRALLVGNIS
IGLQESLWEL ASEITNRAGD LAVEVSPGCW IIDNNICDQS CQNFIFKFNE TAPVPTIPPL
DTKIDLQSDP FYWGSSLGLA ITAAISLAAL VISGIAICRT K
//
