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P68762 (HEMA_INCAA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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/Ann Arbor/1/1950) [Reference proteome]
Taxonomic identifier11553 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus C
Virus hostHomo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length655 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 – 446432Hemagglutinin-esterase-fusion glycoprotein chain 1
PRO_0000039142
Chain447 – 655209Hemagglutinin-esterase-fusion glycoprotein chain 2
PRO_0000039143

Regions

Topological domain15 – 630616Extracellular Potential
Transmembrane631 – 65121Helical; Potential
Topological domain652 – 6554Cytoplasmic Potential
Region15 – 4026Fusion domain-1 By similarity
Region41 – 151111Esterase domain-1 By similarity
Region151 – 310160N-acetyl-9-O-acetylneuraminic acid binding By similarity
Region311 – 36555Esterase domain-2 By similarity
Region366 – 651286Fusion domain-2 By similarity

Sites

Active site711Nucleophile By similarity
Active site3661Charge relay system By similarity
Active site3691Charge relay system By similarity

Amino acid modifications

Glycosylation261N-linked (GlcNAc...); by host Potential
Glycosylation611N-linked (GlcNAc...); by host Potential
Glycosylation1441N-linked (GlcNAc...); by host Potential
Glycosylation3951N-linked (GlcNAc...); by host Potential
Disulfide bond20 ↔ 583Interchain (between HEF1 and HEF2 chains) By similarity
Disulfide bond120 ↔ 165 By similarity
Disulfide bond140 ↔ 188 By similarity
Disulfide bond210 ↔ 252 By similarity
Disulfide bond229 ↔ 316 By similarity
Disulfide bond237 ↔ 289 By similarity

Experimental info

Sequence conflict207 – 2093VEK → EEI in AAA43782. Ref.2
Sequence conflict2141N → Y in AAA43782. Ref.2
Sequence conflict2631S → Y in AAA43782. Ref.2
Sequence conflict3241P → L in AAA43782. Ref.2
Sequence conflict3461C → Y in AAA43782. Ref.2
Sequence conflict4581L → F in AAA43782. Ref.2
Sequence conflict4771V → E in AAA43782. Ref.2
Sequence conflict637 – 6382AA → TP in AAA43782. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P68762 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 81869FEDA9CD8943

FASTA65571,956
        10         20         30         40         50         60 
MFFSLLLMLG LTEAEKIKIC LQKQVNSSFS LHNGFGGNLY ATEEKRMFEL VKPKAGASVL 

        70         80         90        100        110        120 
NQSTWIGFGD SRTDKSNSAF PRSADVSAKT ADKFRSLSGG SLMLSMFGPP GKVDYLYQGC 

       130        140        150        160        170        180 
GKHKVFYEGV NWSPHAAINC YRKNWTDIKL NFQKNIYELA SQSHCMSLVN ALDKTIPLQA 

       190        200        210        220        230        240 
TAGVAKNCNN SFLKNPALYT QEVNPSVEKC GKENLAFFTL PTQFGTYECK LHLVASCYFI 

       250        260        270        280        290        300 
YDSKEVYNKR GCDNYFQVIY DSSGKVVGGL DNRVSPYTGN SGDTPTMQCD MLQLKPGRYS 

       310        320        330        340        350        360 
VRSSPRFLLM PERSYCFDMK EKGPVTAVQS IWGKGRESDH AVDQACLSTP GCMLIQKQKP 

       370        380        390        400        410        420 
YIGEADDHHG DQEMRELLSG LDYEARCISQ SGWVNETSPF TEEYLLPPKF GRCPLAAKEE 

       430        440        450        460        470        480 
SIPKIPDGLL IPTSGTDTTV TKPKSRIFGI DDLIIGLLFV AIVEAGIGGY LLGSRKVSGG 

       490        500        510        520        530        540 
GVTKESAEKG FEKIGNDIQI LRSSTNIAIE KLNDRISHDE QAIRDLTLEI ENARSEALLG 

       550        560        570        580        590        600 
ELGIIRALLV GNISIGLQES LWELASEITN RAGDLAVEVS PGCWVIDNNI CDQSCQNFIF 

       610        620        630        640        650 
KFNETAPVPT IPPLDTKIDL QSDPFYWGSS LGLAITAAIS LAALVISGIA ICRTK 

« Hide

References

[1]"Identification of an amino acid residue on influenza C virus M1 protein responsible for formation of the cord-like structures of the virus."
Muraki Y., Washioka H., Sugawara K., Matsuzaki Y., Takashita E., Hongo S.
J. Gen. Virol. 85:1885-1893(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"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] OF 14-655.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB126194 Genomic RNA. Translation: BAD24940.1.
M11638 Genomic RNA. Translation: AAA43782.1.
RefSeqYP_089655.1. NC_006310.1.

3D structure databases

ProteinModelPortalP68762.
SMRP68762. Positions 15-441, 450-611.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3077359.

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_INCAA
AccessionPrimary (citable) accession number: P68762
Secondary accession number(s): P07969, Q6I7C1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 57 of the entry and version 2 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