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P68762

- HEMA_INCAA

UniProt

P68762 - HEMA_INCAA

Protein

Hemagglutinin-esterase-fusion glycoprotein

Gene

HE

Organism
Influenza C virus (strain C/Ann Arbor/1/1950)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 2 (12 Dec 2006)
      Previous versions | rss
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    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 sitei71 – 711NucleophileBy similarity
    Active sitei366 – 3661Charge relay systemBy similarity
    Active sitei369 – 3691Charge 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

    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:
    Gene namesi
    Name:HE
    OrganismiInfluenza C virus (strain C/Ann Arbor/1/1950)
    Taxonomic identifieri11553 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus C
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    Sus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000008286: Genome

    Subcellular locationi

    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

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1414By similarityAdd
    BLAST
    Chaini15 – 446432Hemagglutinin-esterase-fusion glycoprotein chain 1PRO_0000039142Add
    BLAST
    Chaini447 – 655209Hemagglutinin-esterase-fusion glycoprotein chain 2PRO_0000039143Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi20 ↔ 583Interchain (between HEF1 and HEF2 chains)By similarity
    Glycosylationi26 – 261N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi61 – 611N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi120 ↔ 165By similarity
    Disulfide bondi140 ↔ 188By similarity
    Glycosylationi144 – 1441N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi210 ↔ 252By similarity
    Disulfide bondi229 ↔ 316By similarity
    Disulfide bondi237 ↔ 289By similarity
    Glycosylationi395 – 3951N-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

    ProteinModelPortaliP68762.
    SMRiP68762. Positions 15-441, 450-611.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini15 – 630616ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini652 – 6554CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei631 – 65121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni15 – 4026Fusion domain-1By similarityAdd
    BLAST
    Regioni41 – 151111Esterase domain-1By similarityAdd
    BLAST
    Regioni151 – 310160N-acetyl-9-O-acetylneuraminic acid bindingBy similarityAdd
    BLAST
    Regioni311 – 36555Esterase domain-2By similarityAdd
    BLAST
    Regioni366 – 651286Fusion domain-2By similarityAdd
    BLAST

    Sequence similaritiesi

    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: Complete.

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

    P68762-1 [UniParc]FASTAAdd to Basket

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    MFFSLLLMLG LTEAEKIKIC LQKQVNSSFS LHNGFGGNLY ATEEKRMFEL    50
    VKPKAGASVL NQSTWIGFGD SRTDKSNSAF PRSADVSAKT ADKFRSLSGG 100
    SLMLSMFGPP GKVDYLYQGC GKHKVFYEGV NWSPHAAINC YRKNWTDIKL 150
    NFQKNIYELA SQSHCMSLVN ALDKTIPLQA TAGVAKNCNN SFLKNPALYT 200
    QEVNPSVEKC GKENLAFFTL PTQFGTYECK LHLVASCYFI YDSKEVYNKR 250
    GCDNYFQVIY DSSGKVVGGL DNRVSPYTGN SGDTPTMQCD MLQLKPGRYS 300
    VRSSPRFLLM PERSYCFDMK EKGPVTAVQS IWGKGRESDH AVDQACLSTP 350
    GCMLIQKQKP YIGEADDHHG DQEMRELLSG LDYEARCISQ SGWVNETSPF 400
    TEEYLLPPKF GRCPLAAKEE SIPKIPDGLL IPTSGTDTTV TKPKSRIFGI 450
    DDLIIGLLFV AIVEAGIGGY LLGSRKVSGG GVTKESAEKG FEKIGNDIQI 500
    LRSSTNIAIE KLNDRISHDE QAIRDLTLEI ENARSEALLG ELGIIRALLV 550
    GNISIGLQES LWELASEITN RAGDLAVEVS PGCWVIDNNI CDQSCQNFIF 600
    KFNETAPVPT IPPLDTKIDL QSDPFYWGSS LGLAITAAIS LAALVISGIA 650
    ICRTK 655
    Length:655
    Mass (Da):71,956
    Last modified:December 12, 2006 - v2
    Checksum:i81869FEDA9CD8943
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2093VEK → EEI in AAA43782. (PubMed:3855244)Curated
    Sequence conflicti214 – 2141N → Y in AAA43782. (PubMed:3855244)Curated
    Sequence conflicti263 – 2631S → Y in AAA43782. (PubMed:3855244)Curated
    Sequence conflicti324 – 3241P → L in AAA43782. (PubMed:3855244)Curated
    Sequence conflicti346 – 3461C → Y in AAA43782. (PubMed:3855244)Curated
    Sequence conflicti458 – 4581L → F in AAA43782. (PubMed:3855244)Curated
    Sequence conflicti477 – 4771V → E in AAA43782. (PubMed:3855244)Curated
    Sequence conflicti637 – 6382AA → TP in AAA43782. (PubMed:3855244)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB126194 Genomic RNA. Translation: BAD24940.1.
    M11638 Genomic RNA. Translation: AAA43782.1.
    RefSeqiYP_089655.1. NC_006310.1.

    Genome annotation databases

    GeneIDi3077359.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB126194 Genomic RNA. Translation: BAD24940.1 .
    M11638 Genomic RNA. Translation: AAA43782.1 .
    RefSeqi YP_089655.1. NC_006310.1.

    3D structure databases

    ProteinModelPortali P68762.
    SMRi P68762. Positions 15-441, 450-611.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3077359.

    Family and domain databases

    Gene3Di 3.90.20.10. 1 hit.
    InterProi IPR008980. Capsid_hemagglutn.
    IPR007142. Hemagglutn-estrase_core.
    IPR003860. Hemagglutn-estrase_hemagglutn.
    IPR013829. Hemagglutn_stalk.
    IPR014831. Hemagglutn_stalk_influenz-C.
    [Graphical view ]
    Pfami PF03996. Hema_esterase. 1 hit.
    PF02710. Hema_HEFG. 1 hit.
    PF08720. Hema_stalk. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49818. SSF49818. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiHEMA_INCAA
    AccessioniPrimary (citable) accession number: P68762
    Secondary accession number(s): P07969, Q6I7C1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 58 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3