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Q67387 (HEMA_INCNB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemagglutinin-esterase-fusion glycoprotein

Short name=HEF
EC=3.1.1.53
Gene names
Name:HE
OrganismInfluenza C virus (strain C/Nara/2/1985)
Taxonomic identifier127957 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus C
Virus hostHomo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length648 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Binds to the N-acetyl-9-O-acetylneuraminic acid residues on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HEF2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Displays a receptor-destroying activity which is a neuraminidate-O-acetyl esterase. This activity cleaves off any receptor on the cell surface, which would otherwise prevent virions release. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell By similarity.

Catalytic activity

N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate.

Subunit structure

Homotrimer of disulfide-linked HEF1-HEF2 By similarity.

Subcellular location

Virion membrane; Single-pass type I membrane protein Potential. Host cell membrane; Single-pass type I membrane protein By similarity.

Post-translational modification

In natural infection, inactive HEF is matured into HEF1 and HEF2 outside the cell by one or more trypsin-like, arginine-specific endoprotease By similarity.

Sequence similarities

Belongs to the influenza type C/coronaviruses hemagglutinin-esterase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 77 By similarity
Chain8 – 439432Hemagglutinin-esterase-fusion glycoprotein chain 1
PRO_0000039160
Chain440 – 648209Hemagglutinin-esterase-fusion glycoprotein chain 2
PRO_0000039161

Regions

Topological domain8 – 623616Extracellular Potential
Transmembrane624 – 64421Helical; Potential
Topological domain645 – 6484Cytoplasmic Potential
Region8 – 3326Fusion domain-1 By similarity
Region34 – 144111Esterase domain-1 By similarity
Region144 – 303160N-acetyl-9-O-acetylneuraminic acid binding By similarity
Region304 – 35855Esterase domain-2 By similarity
Region359 – 644286Fusion domain-2 By similarity

Sites

Active site641Nucleophile By similarity
Active site3591Charge relay system By similarity
Active site3621Charge relay system By similarity

Amino acid modifications

Glycosylation191N-linked (GlcNAc...); by host Potential
Glycosylation541N-linked (GlcNAc...); by host Potential
Glycosylation1371N-linked (GlcNAc...); by host Potential
Glycosylation3881N-linked (GlcNAc...); by host Potential
Disulfide bond13 ↔ 576Interchain (between HEF1 and HEF2 chains) By similarity
Disulfide bond113 ↔ 158 By similarity
Disulfide bond133 ↔ 181 By similarity
Disulfide bond203 ↔ 245 By similarity
Disulfide bond222 ↔ 309 By similarity
Disulfide bond230 ↔ 282 By similarity
Disulfide bond339 ↔ 345 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q67387 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D6736996092E5DB9

FASTA64871,229
        10         20         30         40         50         60 
MLGLTEAEKI KICLQKQVNS SFSLHNGFGG NLYATEEKRM FELVKPKAGA SVLNQSTWIG 

        70         80         90        100        110        120 
FGDSRTDQSN SAFPRSADVS AKTADKFRSL SGGSLMLSMF GPPGKVDYLY QGCGKHKVFY 

       130        140        150        160        170        180 
EGVNWSPHAA IDCYRKNWTD IKLNFQKSIY ELASQSHCMS LVNALDKTIP LQVTKGVAKN 

       190        200        210        220        230        240 
CNNSFLKNPA LYTQEVKPLE QICGKENLAF FTLPTQFGTY ECKLHLVASC YFIYDSKEVY 

       250        260        270        280        290        300 
NKRGCGNYFQ VIYDSSGKVV GGLDNRVSPY TGNSGDTPTM QCDMLQLKPG RYSVRSSPRF 

       310        320        330        340        350        360 
LLMPERSYCF DMKEKGPVTA VQSIWGKGRE SDYAVDQACL STPGCMLIQK QKPYIGEADD 

       370        380        390        400        410        420 
HHGDQEMREL LSGLDYEARC ISQSGWVNET SPFTEEYLLP PKFGRCPLAA KEESIPKIPD 

       430        440        450        460        470        480 
GLLIPTSGTD TTVTKPKSRI FGIDDLIIGL LFVAIVEAGI GGYLLGSRKE SGGGVTKESA 

       490        500        510        520        530        540 
EKGFEKIGND IQILRSSTNI AIEKLNDRIS HDEQAIRDLT LEIENARSEA LLGELGIIRA 

       550        560        570        580        590        600 
LLVGNISIGL QESLWELASE ITNRAGDLAV EVSPGCWIID NNICDQSCQN FIFKFNETAP 

       610        620        630        640 
VPTIPPLDTK IDLQSDPFYW GSSLGLAITA AISLAALVIS GIAICRTK 

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References

[1]"Genetic reassortment of influenza C viruses in man."
Peng G., Hongo S., Muraki Y., Sugawara K., Nishimura H., Kitame F., Nakamura K.
J. Gen. Virol. 75:3619-3622(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30697 Genomic RNA. Translation: BAA06368.1.

3D structure databases

ProteinModelPortalQ67387.
SMRQ67387. Positions 8-434, 443-604.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.20.10. 1 hit.
InterProIPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
IPR013829. Hemagglutn_stalk.
IPR014831. Hemagglutn_stalk_influenz-C.
[Graphical view]
PfamPF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
PF08720. Hema_stalk. 1 hit.
[Graphical view]
SUPFAMSSF49818. SSF49818. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEMA_INCNB
AccessionPrimary (citable) accession number: Q67387
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families