Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07967 (HEMA_INCP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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
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

Cleaved into the following 2 chains:

  1. Hemagglutinin-esterase-fusion glycoprotein chain 1
    Short name=HEF1
  2. Hemagglutinin-esterase-fusion glycoprotein chain 2
    Short name=HEF2
Gene names
Name:HE
OrganismInfluenza C virus (strain C/Pig/Beijing/115/1981)
Taxonomic identifier203231 [NCBI]
Taxonomic lineageViruses › ssRNA negative-strand viruses › Orthomyxoviridae › Influenzavirus C ›
Virus hostHomo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length642 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

Signal peptide‹1›1
Chain2 – 433432Hemagglutinin-esterase-fusion glycoprotein chain 1
PRO_0000039164
Chain434 – 642209Hemagglutinin-esterase-fusion glycoprotein chain 2
PRO_0000039165

Regions

Topological domain2 – 617616Extracellular Potential
Transmembrane618 – 63821Helical; Potential
Topological domain639 – 6424Cytoplasmic Potential
Region2 – 2726Fusion domain-1 By similarity
Region28 – 138111Esterase domain-1 By similarity
Region138 – 297160N-acetyl-9-O-acetylneuraminic acid binding By similarity
Region298 – 35255Esterase domain-2 By similarity
Region353 – 638286Fusion domain-2 By similarity

Sites

Active site581Nucleophile By similarity
Active site3531Charge relay system By similarity
Active site3561Charge relay system By similarity

Amino acid modifications

Glycosylation131N-linked (GlcNAc...); by host Potential
Glycosylation481N-linked (GlcNAc...); by host Potential
Glycosylation1311N-linked (GlcNAc...); by host Potential
Glycosylation3821N-linked (GlcNAc...); by host Potential
Disulfide bond7 ↔ 570Interchain (between HEF1 and HEF2 chains) By similarity
Disulfide bond107 ↔ 152 By similarity
Disulfide bond127 ↔ 175 By similarity
Disulfide bond197 ↔ 239 By similarity
Disulfide bond216 ↔ 303 By similarity
Disulfide bond224 ↔ 276 By similarity
Disulfide bond333 ↔ 339 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P07967 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 4F4CFA6E9D71EAC0

FASTA64270,719
        10         20         30         40         50         60 
AEKIKICLQK QVNSSFSLHN GFGGNLYATE EKRMFELVKP KAGASVLNQS TWICFGDSRT 

        70         80         90        100        110        120 
DQSNSAFPRS ADVSAKTAEK FRSLSGGSLM LSMFGPPGKV DYLYQGCGKH KVFYEGVNWS 

       130        140        150        160        170        180 
PHTAIDCYRK NWTDIKLNFQ KSIYELASQS HCMSLVNALD KTIPLQATKG VAKNCNNSFL 

       190        200        210        220        230        240 
KNPALYTQEV KPLEQICGEE NLAFFTLPTQ FGTYECKLHL VASCYFIYDS KEVYNKRGCG 

       250        260        270        280        290        300 
NYFQVIYDSS GKVVGGLDNR VSPYTGNSGD TPTMQCDMLQ LKPGRYSVRS SPRFLLMPER 

       310        320        330        340        350        360 
SYCFDMKEKG LVTAVQSIWG KGRKSDYAVD QACLSTPGCM LIQKQKPYIG EADDHHGDQE 

       370        380        390        400        410        420 
MRELLSGLDY EARCISQSGW VNETSPFTEE YLLPPKFGRC PLAAKEESIP KIPDGLLIPT 

       430        440        450        460        470        480 
SGTDTTVTKP KSRIFGIDDL IIGLLFVAIV EAGIGGYLLG SRKESGGGVT KESAEKGFEK 

       490        500        510        520        530        540 
IGNDIQILRS STNIAIEKLN DRISHDEQAI RDLTLEIENA RSEALLGELG IIRALLVGNI 

       550        560        570        580        590        600 
SIGLQESLWE LASEITNRAG DLAVEVSPGC WIIDNNICDQ SCQNFIFKFN ETAPVPTIPP 

       610        620        630        640 
LDTKIDLQSD PFYWGSSLGL AITTPISLAA LVISGIAICR TK

« Hide

References

[1]"Noncumulative sequence changes in the hemagglutinin genes of influenza C virus isolates."
Buonagurio D.A., Nakada S., Desselberger U., Krystal M., Palese P.
Virology 146:221-232(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M11644 Genomic RNA. Translation: AAA43793.1.

3D structure databases

ProteinModelPortalP07967.
SMRP07967. Positions 2-428, 437-598.
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_INCP2
AccessionPrimary (citable) accession number: P07967
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: February 19, 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents