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P07975

- HEMA_INCJH

UniProt

P07975 - HEMA_INCJH

Protein

Hemagglutinin-esterase-fusion glycoprotein

Gene

HE

Organism
Influenza C virus (strain C/Johannesburg/1/1966)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      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.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei71 – 711Nucleophile
    Active sitei366 – 3661Charge relay system
    Active sitei369 – 3691Charge relay system

    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

    Protein family/group databases

    TCDBi1.G.14.1.1. the influenza virus hemagglutinin/fusion pore-forming protein (influenza-h/fpp) family.

    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/Johannesburg/1/1966)
    Taxonomic identifieri100673 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus C
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    Sus scrofa (Pig) [TaxID: 9823]

    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi71 – 711S → A: 96% loss of esterase activity. 1 Publication
    Mutagenesisi261 – 2611D → A: 64% loss of esterase activity. 1 Publication
    Mutagenesisi280 – 2801N → A: Complete loss of esterase activity. 1 Publication
    Mutagenesisi368 – 3681H → A: Complete loss of esterase activity. 1 Publication
    Mutagenesisi369 – 3691H → A: Complete loss of esterase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1414Add
    BLAST
    Chaini15 – 446432Hemagglutinin-esterase-fusion glycoprotein chain 1PRO_0000039152Add
    BLAST
    Chaini447 – 655209Hemagglutinin-esterase-fusion glycoprotein chain 2PRO_0000039153Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi20 ↔ 583Interchain (between HEF1 and HEF2 chains)
    Glycosylationi26 – 261N-linked (GlcNAc...); by host
    Glycosylationi61 – 611N-linked (GlcNAc...); by host
    Disulfide bondi120 ↔ 165
    Disulfide bondi140 ↔ 188
    Glycosylationi144 – 1441N-linked (GlcNAc...); by host
    Disulfide bondi210 ↔ 252
    Disulfide bondi229 ↔ 316
    Disulfide bondi237 ↔ 289
    Disulfide bondi346 ↔ 352
    Glycosylationi395 – 3951N-linked (GlcNAc...); by host

    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.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotrimer of disulfide-linked HEF1-HEF2.

    Structurei

    Secondary structure

    1
    655
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 257
    Beta strandi39 – 4810
    Beta strandi59 – 6911
    Beta strandi71 – 733
    Helixi80 – 834
    Helixi88 – 925
    Beta strandi94 – 963
    Helixi102 – 1076
    Beta strandi110 – 1123
    Beta strandi118 – 1203
    Beta strandi122 – 1265
    Helixi130 – 1323
    Helixi134 – 1363
    Helixi146 – 16015
    Beta strandi164 – 1696
    Beta strandi186 – 1883
    Beta strandi194 – 1974
    Turni205 – 2084
    Beta strandi214 – 2207
    Beta strandi222 – 2243
    Beta strandi230 – 24011
    Helixi244 – 2507
    Beta strandi256 – 2605
    Beta strandi262 – 2643
    Beta strandi266 – 2716
    Turni272 – 2743
    Beta strandi286 – 2949
    Beta strandi296 – 3038
    Beta strandi314 – 3174
    Beta strandi325 – 3284
    Helixi341 – 3477
    Beta strandi352 – 3554
    Beta strandi364 – 3663
    Helixi372 – 3776
    Helixi378 – 3825
    Beta strandi386 – 3894
    Beta strandi392 – 3943
    Beta strandi399 – 4035
    Beta strandi407 – 4126
    Turni419 – 4213
    Beta strandi424 – 4329
    Beta strandi452 – 4543
    Beta strandi459 – 4624
    Beta strandi469 – 4746
    Turni488 – 4903
    Helixi491 – 51020
    Beta strandi519 – 5213
    Helixi528 – 56942
    Turni573 – 5753
    Turni588 – 5903
    Helixi593 – 5997

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FLCX-ray3.20A/C/E15-446[»]
    B/D/F447-621[»]
    ProteinModelPortaliP07975.
    SMRiP07975. Positions 15-441, 450-611.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07975.

    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-1Add
    BLAST
    Regioni41 – 151111Esterase domain-1Add
    BLAST
    Regioni151 – 310160N-acetyl-9-O-acetylneuraminic acid bindingAdd
    BLAST
    Regioni311 – 36555Esterase domain-2Add
    BLAST
    Regioni366 – 651286Fusion domain-2Add
    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.

    P07975-1 [UniParc]FASTAAdd to Basket

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    MFFSLLLVLG LTEAEKIKIC LQKQVNSSFS LHNGFGGNLY ATEEKRMFEL    50
    VKPKAGASVL NQSTWIGFGD SRTDKSNSAF PRSADVSAKT ADKFRFLSGG 100
    SLMLSMFGPP GKVDYLYQGC GKHKVFYEGV NWSPHAAINC YRKNWTDIKL 150
    NFQKNIYELA SQSHCMSLVN ALDKTIPLQV TAGTAGNCNN SFLKNPALYT 200
    QEVKPSENKC GKENLAFFTL PTQFGTYECK LHLVASCYFI YDSKEVYNKR 250
    GCDNYFQVIY DSFGKVVGGL DNRVSPYTGN SGDTPTMQCD MLQLKPGRYS 300
    VRSSPRFLLM PERSYCFDMK EKGPVTAVQS IWGKGRESDY AVDQACLSTP 350
    GCMLIQKQKP YIGEADDHHG DQEMRELLSG LDYEARCISQ SGWVNETSPF 400
    TEKYLLPPKF GRCPLAAKEE SIPKIPDGLL IPTSGTDTTV TKPKSRIFGI 450
    DDLIIGVLFV AIVETGIGGY LLGSRKESGG GVTKESAEKG FEKIGNDIQI 500
    LKSSINIAIE KLNDRISHDE QAIRDLTLEI ENARSEALLG ELGIIRALLV 550
    GNISIGLQES LWELASEITN RAGDLAVEVS PGCWIIDNNI CDQSCQNFIF 600
    KFNETAPVPT IPPLDTKIDL QSDPFYWGSS LGLAITATIS LAALVISGIA 650
    ICRTK 655
    Length:655
    Mass (Da):72,131
    Last modified:August 1, 1988 - v1
    Checksum:i52C78BFCC5A24AC8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961F → S.
    Natural varianti263 – 2631F → S.
    Natural varianti457 – 4571V → L.
    Natural varianti465 – 4651T → A.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17868 Genomic RNA. Translation: AAA43788.1.
    AJ872181 Genomic RNA. Translation: CAI43342.1.
    AY880247 mRNA. Translation: AAW73083.1.
    PIRiS07412.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17868 Genomic RNA. Translation: AAA43788.1 .
    AJ872181 Genomic RNA. Translation: CAI43342.1 .
    AY880247 mRNA. Translation: AAW73083.1 .
    PIRi S07412.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FLC X-ray 3.20 A/C/E 15-446 [» ]
    B/D/F 447-621 [» ]
    ProteinModelPortali P07975.
    SMRi P07975. Positions 15-441, 450-611.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    TCDBi 1.G.14.1.1. the influenza virus hemagglutinin/fusion pore-forming protein (influenza-h/fpp) family.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P07975.

    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. "Structure of the influenza C glycoprotein gene as determined from cloned DNA."
      Pfeifer J.B., Compans R.W.
      Virus Res. 1:281-296(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Use of influenza C virus glycoprotein HEF for generation of vesicular stomatitis virus pseudotypes."
      Hanika A., Larisch B., Steinmann E., Schwegmann-Wessels C., Herrler G., Zimmer G.
      J. Gen. Virol. 86:1455-1465(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA].
    3. "The catalytic triad of the influenza C virus glycoprotein HEF esterase: characterization by site-directed mutagenesis and functional analysis."
      Pleschka S., Klenk H.D., Herrler G.
      J. Gen. Virol. 76:2529-2537(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-71; ASP-261; ASN-280; HIS-368 AND HIS-369.
    4. "Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus."
      Rosenthal P.B., Zhang X., Formanowski F., Fitz W., Wong C.H., Meier-Ewert H., Skehel J.J., Wiley D.C.
      Nature 396:92-96(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 15-621 AND ACTIVE SITE.

    Entry informationi

    Entry nameiHEMA_INCJH
    AccessioniPrimary (citable) accession number: P07975
    Secondary accession number(s): Q5EI66, Q5JZY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3