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P07967 - HEMA_INCP2

UniProt

P07967 - HEMA_INCP2

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Protein

Hemagglutinin-esterase-fusion glycoprotein

Gene

HE

Organism
Influenza C virus (strain C/Pig/Beijing/115/1981)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581NucleophileBy similarity
Active sitei353 – 3531Charge relay systemBy similarity
Active sitei356 – 3561Charge relay systemBy similarity

GO - Molecular functioni

  1. sialate O-acetylesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  2. fusion of virus membrane with host plasma membrane Source: InterPro
  3. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin, Hydrolase

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Hemagglutinin-esterase-fusion glycoprotein (EC:3.1.1.53)
Short name:
HEF
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 namesi
Name:HE
OrganismiInfluenza C virus (strain C/Pig/Beijing/115/1981)
Taxonomic identifieri203231 [NCBI]
Taxonomic lineageiViruses › ssRNA negative-strand viruses › Orthomyxoviridae › Influenzavirus C ›
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Subcellular locationi

Virion membrane Curated; Single-pass type I membrane protein Curated. Host cell membrane By similarity; Single-pass type I membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 617616ExtracellularSequence AnalysisAdd
BLAST
Transmembranei618 – 63821HelicalSequence AnalysisAdd
BLAST
Topological domaini639 – 6424CytoplasmicSequence Analysis

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
  4. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 1›1
Chaini2 – 433432Hemagglutinin-esterase-fusion glycoprotein chain 1PRO_0000039164Add
BLAST
Chaini434 – 642209Hemagglutinin-esterase-fusion glycoprotein chain 2PRO_0000039165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi7 ↔ 570Interchain (between HEF1 and HEF2 chains)By similarity
Glycosylationi13 – 131N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi48 – 481N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi107 ↔ 152By similarity
Disulfide bondi127 ↔ 175By similarity
Glycosylationi131 – 1311N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi197 ↔ 239By similarity
Disulfide bondi216 ↔ 303By similarity
Disulfide bondi224 ↔ 276By similarity
Disulfide bondi333 ↔ 339By similarity
Glycosylationi382 – 3821N-linked (GlcNAc...); by hostSequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HEF1-HEF2.By similarity

Structurei

3D structure databases

ProteinModelPortaliP07967.
SMRiP07967. Positions 2-428, 437-598.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2726Fusion domain-1By similarityAdd
BLAST
Regioni28 – 138111Esterase domain-1By similarityAdd
BLAST
Regioni138 – 297160N-acetyl-9-O-acetylneuraminic acid bindingBy similarityAdd
BLAST
Regioni298 – 35255Esterase domain-2By similarityAdd
BLAST
Regioni353 – 638286Fusion domain-2By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the influenza type C/coronaviruses hemagglutinin-esterase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.90.20.10. 1 hit.
InterProiIPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
IPR013829. Hemagglutn_stalk.
IPR014831. Hemagglutn_stalk_influenz-C.
[Graphical view]
PfamiPF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
PF08720. Hema_stalk. 1 hit.
[Graphical view]
SUPFAMiSSF49818. SSF49818. 1 hit.

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07967-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
AEKIKICLQK QVNSSFSLHN GFGGNLYATE EKRMFELVKP KAGASVLNQS 
        60         70         80         90        100
TWICFGDSRT DQSNSAFPRS ADVSAKTAEK FRSLSGGSLM LSMFGPPGKV 
       110        120        130        140        150
DYLYQGCGKH KVFYEGVNWS PHTAIDCYRK NWTDIKLNFQ KSIYELASQS 
       160        170        180        190        200
HCMSLVNALD KTIPLQATKG VAKNCNNSFL KNPALYTQEV KPLEQICGEE 
       210        220        230        240        250
NLAFFTLPTQ FGTYECKLHL VASCYFIYDS KEVYNKRGCG NYFQVIYDSS 
       260        270        280        290        300
GKVVGGLDNR VSPYTGNSGD TPTMQCDMLQ LKPGRYSVRS SPRFLLMPER 
       310        320        330        340        350
SYCFDMKEKG LVTAVQSIWG KGRKSDYAVD QACLSTPGCM LIQKQKPYIG 
       360        370        380        390        400
EADDHHGDQE MRELLSGLDY EARCISQSGW VNETSPFTEE YLLPPKFGRC 
       410        420        430        440        450
PLAAKEESIP KIPDGLLIPT SGTDTTVTKP KSRIFGIDDL IIGLLFVAIV 
       460        470        480        490        500
EAGIGGYLLG SRKESGGGVT KESAEKGFEK IGNDIQILRS STNIAIEKLN 
       510        520        530        540        550
DRISHDEQAI RDLTLEIENA RSEALLGELG IIRALLVGNI SIGLQESLWE 
       560        570        580        590        600
LASEITNRAG DLAVEVSPGC WIIDNNICDQ SCQNFIFKFN ETAPVPTIPP 
       610        620        630        640 
LDTKIDLQSD PFYWGSSLGL AITTPISLAA LVISGIAICR TK
Length:642
Mass (Da):70,719
Last modified:August 1, 1988 - v1
Checksum:i4F4CFA6E9D71EAC0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11644 Genomic RNA. Translation: AAA43793.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11644 Genomic RNA. Translation: AAA43793.1.

3D structure databases

ProteinModelPortaliP07967.
SMRiP07967. Positions 2-428, 437-598.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.90.20.10. 1 hit.
InterProiIPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
IPR013829. Hemagglutn_stalk.
IPR014831. Hemagglutn_stalk_influenz-C.
[Graphical view]
PfamiPF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
PF08720. Hema_stalk. 1 hit.
[Graphical view]
SUPFAMiSSF49818. SSF49818. 1 hit.
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiHEMA_INCP2
AccessioniPrimary (citable) accession number: P07967
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: January 7, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.