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P03465 (HEMA_INCCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. 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/California/1978)
Taxonomic identifier203224 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus C
Virus hostHomo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length654 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 – 1414 By similarity
Chain15 – 444430Hemagglutinin-esterase-fusion glycoprotein chain 1
PRO_0000039144
Chain446 – 654209Hemagglutinin-esterase-fusion glycoprotein chain 2
PRO_0000039145

Regions

Topological domain15 – 629615Extracellular Potential
Transmembrane630 – 65021Helical; Potential
Topological domain651 – 6544Cytoplasmic Potential
Region15 – 4026Fusion domain-1 By similarity
Region41 – 150110Esterase domain-1 By similarity
Region150 – 309160N-acetyl-9-O-acetylneuraminic acid binding By similarity
Region310 – 36455Esterase domain-2 By similarity
Region365 – 650286Fusion domain-2 By similarity

Sites

Active site711Nucleophile By similarity
Active site3651Charge relay system By similarity
Active site3681Charge relay system By similarity

Amino acid modifications

Glycosylation261N-linked (GlcNAc...); by host Potential
Glycosylation611N-linked (GlcNAc...); by host Potential
Glycosylation1431N-linked (GlcNAc...); by host Potential
Glycosylation3941N-linked (GlcNAc...); by host Potential
Disulfide bond20 ↔ 582Interchain (between HEF1 and HEF2 chains) By similarity
Disulfide bond119 ↔ 164 By similarity
Disulfide bond139 ↔ 187 By similarity
Disulfide bond209 ↔ 251 By similarity
Disulfide bond228 ↔ 315 By similarity
Disulfide bond236 ↔ 288 By similarity
Disulfide bond345 ↔ 351 By similarity

Sequences

Sequence LengthMass (Da)Tools
P03465 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 7F4C28D9EFD2E429

FASTA65472,085
        10         20         30         40         50         60 
MFFSLLLMLG LTEAEKIKIC LQKQVNSSFS LHNGFGGNLY ATEEKRMFEL VKPKAGASVL 

        70         80         90        100        110        120 
NQSTWIGFGD SRTDQSNSAF PRSLMSAKTA DKFRSLSGGS LMLSMFGPPG KVDYLYQGCG 

       130        140        150        160        170        180 
KHKVFYEGVN WSPHAAIDCY RKNWTDIKLN FQKSIYELAS QSHCMSLVNA LDKTIPLQVT 

       190        200        210        220        230        240 
KGVAKNCNNS FLKNPALYTQ EVKPLEQICG EENLAFFTLP TQFGTYECKL HLVASCYFIY 

       250        260        270        280        290        300 
DSKEVYNKRG CGNYFQVIYD SSGKVVGGLD NRVSPYTGNS GDTPTMQCDM LQLKPGRYSV 

       310        320        330        340        350        360 
RSSPRFLLMP ERSYCFDMKE KGPVTAVQSI WGKGRKSDYA VDQACLSTPG CMLIQKQKPY 

       370        380        390        400        410        420 
IGEADDHHGD QEMRELLSGL DYEARCISQS GWVNETSPFT EEYLLPPKFG RCPLAAKEES 

       430        440        450        460        470        480 
IPKIPDGLLI PTSGTDTTVT KPKSRIFGID DLIIGLLFVA IVEAGIGGYL LGSRKESGGG 

       490        500        510        520        530        540 
VTKESAEKGF EKIGNDIQIL RSSTNIAIEK LNDRISHDEQ AIRDLTLEIE NARSEALLGE 

       550        560        570        580        590        600 
LGIIRALLVG NISIGLQESL WELASEITNR AGDLAVEVSP GCWIIDNNIC DQSCQNFIFK 

       610        620        630        640        650 
FNETAPVPTI PPLDTKIDLQ SDPFYWGSSL GLAITAANLM AALVISGIAI CRTK 

« Hide

References

[1]"Influenza C virus hemagglutinin: comparison with influenza A and B virus hemagglutinins."
Nakada S., Creager R.S., Krystal M., Aaronson R.P., Palese P.
J. Virol. 50:118-124(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01689 Genomic RNA. Translation: AAA43791.1.
PIRHMIVC8. A04076.

3D structure databases

ProteinModelPortalP03465.
SMRP03465. Positions 15-440, 449-610.
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_INCCA
AccessionPrimary (citable) accession number: P03465
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 86 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