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P31614

- HEMA_CVMS

UniProt

P31614 - HEMA_CVMS

Protein

Hemagglutinin-esterase

Gene

HE

Organism
Murine coronavirus (strain S) (MHV-S) (Murine hepatitis virus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (01 Oct 2014)
      Previous versions | rss
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    Functioni

    Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-4-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture. However, its presence in the virus may alter its pathogenicity. May become a target for both the humoral and the cellular branches of the immune system.1 Publication

    Catalytic activityi

    N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei45 – 451Nucleophile1 Publication
    Active sitei342 – 3421Charge relay system1 Publication
    Active sitei345 – 3451Charge relay system1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. fusion of virus membrane with host plasma membrane Source: InterPro

    Keywords - Molecular functioni

    Hemagglutinin, Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hemagglutinin-esterase (EC:3.1.1.53)
    Short name:
    HE protein
    Alternative name(s):
    E3 glycoprotein
    Gene namesi
    Name:HE
    ORF Names:2b
    OrganismiMurine coronavirus (strain S) (MHV-S) (Murine hepatitis virus)
    Taxonomic identifieri11145 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]

    Subcellular locationi

    Virion membrane Curated; Single-pass type I membrane protein Curated. Host cell membrane Curated; Single-pass type I membrane protein Curated
    Note: In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis Golgi. However, some may escape incorporation into virions and subsequently migrate to the cell surface By similarity.By similarity

    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
    Mutagenesisi45 – 451S → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi119 – 1191L → A: Decreased receptor-binding activity. 1 Publication
    Mutagenesisi166 – 1661I → A: Decreased receptor-binding activity. 1 Publication
    Mutagenesisi212 – 2121F → A: Decreased receptor-binding activity. 1 Publication
    Mutagenesisi260 – 2601L → A: Decreased receptor-binding activity. 1 Publication
    Mutagenesisi281 – 2811Y → A: Decreased receptor-binding activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 439417Hemagglutinin-esterasePRO_0000037148Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi49 ↔ 701 Publication
    Glycosylationi94 – 941N-linked (GlcNAc...); by host1 Publication
    Disulfide bondi118 ↔ 1671 Publication
    Glycosylationi152 – 1521N-linked (GlcNAc...); by host1 Publication
    Glycosylationi196 – 1961N-linked (GlcNAc...); by host1 Publication
    Disulfide bondi202 ↔ 2911 Publication
    Disulfide bondi210 ↔ 2641 Publication
    Glycosylationi246 – 2461N-linked (GlcNAc...); by host1 Publication
    Glycosylationi309 – 3091N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi316 – 3161N-linked (GlcNAc...); by host1 Publication
    Disulfide bondi322 ↔ 3271 Publication
    Glycosylationi331 – 3311N-linked (GlcNAc...); by host1 Publication
    Glycosylationi360 – 3601N-linked (GlcNAc...); by host1 Publication
    Disulfide bondi363 ↔ 3871 Publication
    Glycosylationi374 – 3741N-linked (GlcNAc...); by host1 Publication
    Disulfide bondi400 – 400Interchain1 Publication

    Post-translational modificationi

    N-glycosylated in the RER.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Forms a complex with the M protein in the pre-Golgi. Associates then with S-M complex to form a ternary complex S-M-HE.1 Publication

    Structurei

    Secondary structure

    1
    439
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 313
    Beta strandi35 – 373
    Beta strandi39 – 457
    Helixi61 – 633
    Turni68 – 714
    Beta strandi75 – 773
    Helixi83 – 886
    Beta strandi89 – 913
    Beta strandi96 – 983
    Beta strandi100 – 1067
    Helixi124 – 14118
    Turni142 – 1443
    Beta strandi145 – 1528
    Beta strandi176 – 1805
    Beta strandi187 – 1893
    Beta strandi193 – 1997
    Beta strandi201 – 21414
    Beta strandi220 – 2223
    Beta strandi231 – 2366
    Turni237 – 2393
    Beta strandi241 – 2466
    Beta strandi253 – 2575
    Beta strandi261 – 2699
    Beta strandi271 – 28515
    Beta strandi287 – 2959
    Beta strandi301 – 3055
    Helixi317 – 3215
    Turni324 – 3263
    Beta strandi327 – 3304
    Helixi350 – 3567
    Beta strandi362 – 3654
    Beta strandi368 – 3714
    Beta strandi373 – 3753
    Beta strandi384 – 3863
    Beta strandi399 – 4013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4C7LX-ray2.10A/B25-403[»]
    4C7WX-ray2.50A/B25-403[»]
    ProteinModelPortaliP31614.
    SMRiP31614. Positions 23-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 407385Virion surfaceSequence AnalysisAdd
    BLAST
    Topological domaini429 – 43911IntravirionSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei408 – 42821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni12 – 132121Esterase domain first partBy similarityAdd
    BLAST
    Regioni133 – 281149Receptor bindingBy similarityAdd
    BLAST
    Regioni217 – 2204Receptor binding
    Regioni282 – 395114Esterase domain second partBy similarityAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    InterProiIPR008980. Capsid_hemagglutn.
    IPR007142. Hemagglutn-estrase_core.
    IPR003860. Hemagglutn-estrase_hemagglutn.
    [Graphical view]
    PfamiPF03996. Hema_esterase. 1 hit.
    PF02710. Hema_HEFG. 1 hit.
    [Graphical view]
    SUPFAMiSSF49818. SSF49818. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P31614-1 [UniParc]FASTAAdd to Basket

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    MGCMCIAMAP RTLLLLIGCQ LVFGFNEPLN IVSHLNDDWF LFGDSRSDCT    50
    YVENNGHPKL DWLDLDPKLC NSGRISAKSG NSLFRSFHFI DFYNYSGEGD 100
    QVIFYEGVNF SPSHGFKCLA YGDNKRWMGN KARFYARVYE KMAQYRSLSF 150
    VNVSYAYGGN AKPTSICKDK TLTLNNPTFI SKESNYVDYY YESEANFTLQ 200
    GCDEFIVPLC VFNGHSKGSS SDPANKYYTD SQSYYNMDTG VLYGFNSTLD 250
    VGNTVQNPGL DLTCRYLALT PGNYKAVSLE YLLSLPSKAI CLRKPKSFMP 300
    VQVVDSRWNS TRQSDNMTAV ACQLPYCFFR NTSADYSGGT HDVHHGDFHF 350
    RQLLSGLLYN VSCIAQQGAF VYNNVSSSWP AYGYGHCPTA ANIGYMAPVC 400
    IYDPLPVILL GVLLGIAVLI IVFLMFYFMT DSGVRLHEA 439
    Length:439
    Mass (Da):49,205
    Last modified:October 1, 2014 - v2
    Checksum:i68CC6EC9CD108FAA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761S → Y in AAA46460. (PubMed:1649505)Curated
    Sequence conflicti208 – 2081P → T in AAA46460. (PubMed:1649505)Curated
    Sequence conflicti212 – 2121F → S in AAA46460. (PubMed:1649505)Curated
    Sequence conflicti218 – 2181G → S in AAA46460. (PubMed:1649505)Curated
    Sequence conflicti231 – 2311S → A in AAA46460. (PubMed:1649505)Curated
    Sequence conflicti403 – 4031D → E in AAA46460. (PubMed:1649505)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY771997 Genomic RNA. No translation available.
    M64316 Genomic RNA. Translation: AAA46460.1.
    PIRiA40476. HMIHMS.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY771997 Genomic RNA. No translation available.
    M64316 Genomic RNA. Translation: AAA46460.1 .
    PIRi A40476. HMIHMS.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4C7L X-ray 2.10 A/B 25-403 [» ]
    4C7W X-ray 2.50 A/B 25-403 [» ]
    ProteinModelPortali P31614.
    SMRi P31614. Positions 23-389.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR008980. Capsid_hemagglutn.
    IPR007142. Hemagglutn-estrase_core.
    IPR003860. Hemagglutn-estrase_hemagglutn.
    [Graphical view ]
    Pfami PF03996. Hema_esterase. 1 hit.
    PF02710. Hema_HEFG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49818. SSF49818. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nidovirus sialate-O-acetylesterases: evolution and substrate specificity of coronaviral and toroviral receptor-destroying enzymes."
      Smits S.L., Gerwig G.J., van Vliet A.L., Lissenberg A., Briza P., Kamerling J.P., Vlasak R., de Groot R.J.
      J. Biol. Chem. 280:6933-6941(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], CHARACTERIZATION.
      Strain: S.
    2. "Luxury at a cost? Recombinant mouse hepatitis viruses expressing the accessory hemagglutinin esterase protein display reduced fitness in vitro."
      Lissenberg A., Vrolijk M.M., van Vliet A.L., Langereis M.A., de Groot-Mijnes J.D., Rottier P.J., de Groot R.J.
      J. Virol. 79:15054-15063(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: S.
    3. "Heterogeneity of gene expression of the hemagglutinin-esterase (HE) protein of murine coronaviruses."
      Yokomori K., Banner L.R., Lai M.M.C.
      Virology 183:647-657(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-434.
      Strain: S.
    4. "The sialate-4-O-acetylesterases of coronaviruses related to mouse hepatitis virus: a proposal to reorganize group 2 Coronaviridae."
      Wurzer W.J., Obojes K., Vlasak R.
      J. Gen. Virol. 83:395-402(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. "The murine coronavirus hemagglutinin-esterase receptor-binding site: a major shift in ligand specificity through modest changes in architecture."
      Langereis M.A., Zeng Q., Heesters B.A., Huizinga E.G., de Groot R.J.
      PLoS Pathog. 8:E1002492-E1002492(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 25-403 OF PROTEIN MUTANT ALA-45 AND IN COMPLEX WITH RECEPTOR ANALOG, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, GLYCOSYLATION AT ASN-94; ASN-152; ASN-196; ASN-246; ASN-316; ASN-331; ASN-360 AND ASN-374, DISULFIDE BONDS, MUTAGENESIS OF SER-45; LEU-119; ILE-166; PHE-212; LEU-260 AND TYR-281.
      Strain: S.

    Entry informationi

    Entry nameiHEMA_CVMS
    AccessioniPrimary (citable) accession number: P31614
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: October 1, 2014
    Last modified: October 1, 2014
    This is version 90 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

    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