ID E0WL39_INCJJ Unreviewed; 655 AA.
AC E0WL39;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Hemagglutinin-esterase-fusion glycoprotein {ECO:0000256|HAMAP-Rule:MF_04072};
DE Short=HEF {ECO:0000256|HAMAP-Rule:MF_04072};
DE EC=3.1.1.53 {ECO:0000256|HAMAP-Rule:MF_04072};
DE Contains:
DE RecName: Full=Hemagglutinin-esterase-fusion glycoprotein chain 1 {ECO:0000256|HAMAP-Rule:MF_04072};
DE Short=HEF1 {ECO:0000256|HAMAP-Rule:MF_04072};
DE Contains:
DE RecName: Full=Hemagglutinin-esterase-fusion glycoprotein chain 2 {ECO:0000256|HAMAP-Rule:MF_04072};
DE Short=HEF2 {ECO:0000256|HAMAP-Rule:MF_04072};
GN Name=HEF {ECO:0000313|EMBL:CBW43847.1};
GN Synonyms=HE {ECO:0000256|HAMAP-Rule:MF_04072,
GN ECO:0000256|RuleBase:RU362095};
OS Influenza C virus (strain C/JJ/1950).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Gammainfluenzavirus;
OC Gammainfluenzavirus influenzae; Influenza C virus.
OX NCBI_TaxID=11560 {ECO:0000313|EMBL:CBW43847.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1] {ECO:0000313|EMBL:CBW43847.1}
RP NUCLEOTIDE SEQUENCE.
RA Pachler K., Mayr J., Vlasak R.;
RT "A seven plasmid-based system for the rescue of influenza C virus.";
RL J. Mol. Genet. Med. 4:239-246(2010).
RN [2] {ECO:0000313|EMBL:CBW43847.1}
RP NUCLEOTIDE SEQUENCE.
RA Pachler K.;
RT "Reverse genetics of influenza C viruses.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_04072, 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, ECO:0000256|HAMAP-
CC Rule:MF_04072, 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, ECO:0000256|HAMAP-
CC Rule:MF_04072};
CC -!- SUBUNIT: Homotrimer of disulfide-linked HEF1-HEF2.
CC {ECO:0000256|ARBA:ARBA00011223, ECO:0000256|HAMAP-Rule:MF_04072,
CC 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|HAMAP-Rule:MF_04072, ECO:0000256|RuleBase:RU362095};
CC Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04072,
CC ECO:0000256|RuleBase:RU362095}. Host cell membrane {ECO:0000256|HAMAP-
CC Rule:MF_04072, ECO:0000256|RuleBase:RU362095}; Single-pass type I
CC membrane protein {ECO:0000256|HAMAP-Rule:MF_04072,
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|HAMAP-Rule:MF_04072,
CC 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 -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC {ECO:0000256|HAMAP-Rule:MF_04072}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04072}.
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DR EMBL; FR671422; CBW43847.1; -; 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-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046789; F:host cell surface receptor binding; IEA:UniProtKB-UniRule.
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:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule.
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, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510, ECO:0000256|HAMAP-Rule:MF_04072};
KW Fusion of virus membrane with host membrane {ECO:0000256|ARBA:ARBA00022506,
KW ECO:0000256|HAMAP-Rule:MF_04072};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Hemagglutinin {ECO:0000256|ARBA:ARBA00022546, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04072};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04072};
KW Signal {ECO:0000256|HAMAP-Rule:MF_04072};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04072,
KW ECO:0000256|RuleBase:RU362095};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804,
KW ECO:0000256|HAMAP-Rule:MF_04072};
KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595,
KW ECO:0000256|HAMAP-Rule:MF_04072};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04072};
KW Virus endocytosis by host {ECO:0000256|HAMAP-Rule:MF_04072};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296,
KW ECO:0000256|HAMAP-Rule:MF_04072}.
FT TRANSMEM 624..652
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072,
FT ECO:0000256|RuleBase:RU362095"
FT DOMAIN 39..419
FT /note="Haemagglutinin-esterase glycoprotein core"
FT /evidence="ECO:0000259|Pfam:PF03996"
FT DOMAIN 151..304
FT /note="Haemagglutinin-esterase glycoprotein haemagglutinin"
FT /evidence="ECO:0000259|Pfam:PF02710"
FT DOMAIN 447..621
FT /note="Haemagglutinin stalk influenza C"
FT /evidence="ECO:0000259|Pfam:PF08720"
FT REGION 15..40
FT /note="Fusion domain-1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT REGION 151..311
FT /note="N-acetyl-9-O-acetylneuraminic acid binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT REGION 366..651
FT /note="Fusion domain-2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT COILED 509..536
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 71
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT ACT_SITE 370
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT DISULFID 346..352
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
SQ SEQUENCE 655 AA; 72195 MW; 240BA47C74B3A835 CRC64;
MFFSLLLMLG LTEAEKIKIC LQKQVNSSFS LHNGFGGNLY ATEEKRMFEL VKPKAGASVL
NQSAWIGFGD SRTDKSNSAF PRSADVSAKT ADKFRSLSGG SLMLSMFGPP GKVDYLYQGC
GKHKVFYEGV NWSPHAAINC YRKNWTDIKL NFQKNIYELA SQSHCMSLVN ALDKTIPLQA
TAGVAKNCNN SFLKNPALYT QEVNPSERKC GKENLAFFTL PTQFGTYECK LHLVASCYFI
YDSKEVYNKR GCDDYFQVIY DSYGKVVGGL DNRVSPYTGN SGDIPTMQCD MLQLKPGRYS
VRSSPRFLLM PERSYCFDMK EKGPVTAVQS IWGKGRESDH AVDQACLSTP GCMLIQKQKP
YIGEADDHHG DQEMRELLSG LDYEARCISQ SGWVNETSPF TEEYLLPPKF GRCPLAAKEE
SIPKIPDGLL IPTSGTDTTV TKPKSRIFGI DDLIIGLFFV SIVEAGIGGY LLGSRKQSGG
GVTKESAEKG FEKIGNDIQI LRSSTNIAIE KLNDRISHDE QAIRDLTLEI ENARSEALLG
ELGIIRALLV GNISIGLQES LWELASEITN RAGDLAVEVS PGCWVIDNNI CDQSCQNFIF
KFNETAPVPT IPPLDTKIDL QSDLFYWGSS LGLVITAAIS LAALVISGIA ICRTK
//
