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P17005 (HEMA_INCNA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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/1982)
Taxonomic identifier203232 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus C
Virus hostHomo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length641 AA.
Sequence statusFragment.
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

Chain1 – 432432Hemagglutinin-esterase-fusion glycoprotein chain 1
PRO_0000039158
Chain433 – 641209Hemagglutinin-esterase-fusion glycoprotein chain 2
PRO_0000039159

Regions

Topological domain1 – 616616Extracellular Potential
Transmembrane617 – 63721Helical; Potential
Topological domain638 – 6414Cytoplasmic Potential
Region1 – 2626Fusion domain-1 By similarity
Region27 – 137111Esterase domain-1 By similarity
Region137 – 296160N-acetyl-9-O-acetylneuraminic acid binding By similarity
Region297 – 35155Esterase domain-2 By similarity
Region352 – 637286Fusion domain-2 By similarity

Sites

Active site571Nucleophile By similarity
Active site3521Charge relay system By similarity
Active site3551Charge relay system By similarity

Amino acid modifications

Glycosylation121N-linked (GlcNAc...); by host Potential
Glycosylation471N-linked (GlcNAc...); by host Potential
Glycosylation1301N-linked (GlcNAc...); by host Potential
Glycosylation3811N-linked (GlcNAc...); by host Potential
Disulfide bond6 ↔ 569Interchain (between HEF1 and HEF2 chains) By similarity
Disulfide bond106 ↔ 151 By similarity
Disulfide bond126 ↔ 174 By similarity
Disulfide bond196 ↔ 238 By similarity
Disulfide bond215 ↔ 302 By similarity
Disulfide bond223 ↔ 275 By similarity
Disulfide bond332 ↔ 338 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P17005 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: FA2477DFF44B3319

FASTA64170,561
        10         20         30         40         50         60 
EKIKICLQKQ VNSSFSLHNG FGGNLYATEE KRMFELVKPK AGASVLNQST WIGFGDSRTD 

        70         80         90        100        110        120 
KSNPNFPRSA DVSVKTANKF RSLTGGSLML SMFGPPGKVD YLYQGCGKHK VFYEGVNWSP 

       130        140        150        160        170        180 
HAAIDCYRKN WTDIKLNFQK NIYELASQSH CMSLVNALDK TIPLQATAGV AGNCNNSFLK 

       190        200        210        220        230        240 
NPALYTQEVT PPXXKCGKEN LAFFTLPTQF GTYECRLHLV ASCYFIYDSK EVYNKRGCDN 

       250        260        270        280        290        300 
YFQVIYDSSG KVVGGLDNRV SPYTGNSGDT PTMQCDMIQL KPGRYSVRSS PRFLLMPERS 

       310        320        330        340        350        360 
YCFDMKEKGP VTAVQSIWGK DRKSDYAVDQ ACLSTPGCML IQKQKPYTGE ADDHHGDQEM 

       370        380        390        400        410        420 
RELLSGLDYE ARCISQSGWV NETSPFTEEY LLPPKFGRCP LAAKEESIPK IPDGLLIPTS 

       430        440        450        460        470        480 
GTDTTVTKPK SRIFGIDDLI IGLLFVAIVE AGIGGYLLGS RKESGGGVTK ESAEKGFEKI 

       490        500        510        520        530        540 
GNDIQILRSS TNIAIEKLND RISHDEQAIR DLTLEIENAR SEALLGELGI IRALLVGNIS 

       550        560        570        580        590        600 
IGLQESLWEL ASEITNRAGD LAVEISPGCW IIDNNICDQS CQNFIFKFNE TAPVPTIPPL 

       610        620        630        640 
DTKIDLQSDP FYWGSSLGLA ITAAISLAAL VISGIAICRT K 

« Hide

References

[1]"Antigenic and genetic characterization of three influenza C strains isolated in the Kinki district of Japan in 1982-1983."
Adachi K., Kitame F., Sugawara K., Nishimura H., Nakamura K.
Virology 172:125-133(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25362 Genomic RNA. Translation: AAA43790.1.
PIRHMIVEB. B32665.

3D structure databases

ProteinModelPortalP17005.
SMRP17005. Positions 436-597.
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_INCNA
AccessionPrimary (citable) accession number: P17005
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 89 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