Hemagglutinin-esterase-fusion glycoprotein precursor - Influenza C virus (strain C/Ann Arbor/1/1950)

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P68762 (HEMA_INCAA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 53. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Hemagglutinin-esterase-fusion glycoprotein
Short name=HEF
EC=3.1.1.53

Cleaved into the following 2 chains:

Hemagglutinin-esterase-fusion glycoprotein chain 1
Short name=HEF1
Hemagglutinin-esterase-fusion glycoprotein chain 2
Short name=HEF2

Gene names

Name:

Organism

Influenza C virus (strain C/Ann Arbor/1/1950) [Reference proteome]

Taxonomic identifier

11553 [NCBI]

Taxonomic lineage

Viruses › ssRNA negative-strand viruses › Orthomyxoviridae › Influenzavirus C ›

Virus host

Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	655 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Fusion of virus membrane with host endosomal membrane Fusion of virus membrane with host membrane Host-virus interaction Viral attachment to host cell Viral penetration into host cytoplasm Virus entry into host cell
Cellular component	Host cell membrane Host membrane Membrane Viral envelope protein Virion
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Hemagglutinin Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via membrane fusion with the plasma membrane Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: UniProtKB-KW virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	sialate O-acetylesterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 14

By similarity

Chain

15 – 446

432

Hemagglutinin-esterase-fusion glycoprotein chain 1

PRO_0000039142

Chain

447 – 655

209

Hemagglutinin-esterase-fusion glycoprotein chain 2

PRO_0000039143

Regions

Topological domain

15 – 630

616

Extracellular Potential

Transmembrane

631 – 651

Helical; Potential

Topological domain

652 – 655

Cytoplasmic Potential

Region

15 – 40

Fusion domain-1 By similarity

Region

41 – 151

111

Esterase domain-1 By similarity

Region

151 – 310

160

N-acetyl-9-O-acetylneuraminic acid binding By similarity

Region

311 – 365

Esterase domain-2 By similarity

Region

366 – 651

286

Fusion domain-2 By similarity

Sites

Active site

Nucleophile By similarity

Active site

366

Charge relay system By similarity

Active site

369

Charge relay system By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...); by host Potential

Glycosylation

N-linked (GlcNAc...); by host Potential

Glycosylation

144

N-linked (GlcNAc...); by host Potential

Glycosylation

395

N-linked (GlcNAc...); by host Potential

Disulfide bond

20 ↔ 583

Interchain (between HEF1 and HEF2 chains) By similarity

Disulfide bond

120 ↔ 165

By similarity

Disulfide bond

140 ↔ 188

By similarity

Disulfide bond

210 ↔ 252

By similarity

Disulfide bond

229 ↔ 316

By similarity

Disulfide bond

237 ↔ 289

By similarity

Experimental info

Sequence conflict

207 – 209

VEK → EEI in AAA43782. Ref.2

Sequence conflict

214

N → Y in AAA43782. Ref.2

Sequence conflict

263

S → Y in AAA43782. Ref.2

Sequence conflict

324

P → L in AAA43782. Ref.2

Sequence conflict

346

C → Y in AAA43782. Ref.2

Sequence conflict

458

L → F in AAA43782. Ref.2

Sequence conflict

477

V → E in AAA43782. Ref.2

Sequence conflict

637 – 638

AA → TP in AAA43782. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P68762 [UniParc].

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

FASTA

655

71,956

        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

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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.
RefSeq	YP_089655.1. NC_006310.1.
3D structure databases
ProteinModelPortal	P68762.
SMR	P68762. Positions 15-441, 450-611.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3077359.
Family and domain databases
Gene3D	3.90.20.10. 1 hit.
InterPro	IPR008980. Capsid_hemagglutn. IPR007142. Hemagglutn-estrase_core. IPR003860. Hemagglutn-estrase_hemagglutn. IPR013829. Hemagglutn_stalk. IPR014831. Hemagglutn_stalk_influenz-C. [Graphical view]
Pfam	PF03996. Hema_esterase. 1 hit. PF02710. Hema_HEFG. 1 hit. PF08720. Hema_stalk. 1 hit. [Graphical view]
SUPFAM	SSF49818. Capsid_hemag. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HEMA_INCAA

Accession

Primary (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 3, 2013
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Family and domain databases

Entry information

Relevant documents