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P31614

- HEMA_CVMS

UniProt

P31614 - HEMA_CVMS

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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

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
Complete GO annotation...

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-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
Complete GO annotation...

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/B22-400[»]
4C7WX-ray2.50A/B22-400[»]
ProteinModelPortaliP31614.
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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        10         20         30         40         50
MGCMCIAMAP RTLLLLIGCQ LVFGFNEPLN IVSHLNDDWF LFGDSRSDCT
60 70 80 90 100
YVENNGHPKL DWLDLDPKLC NSGRISAKSG NSLFRSFHFI DFYNYSGEGD
110 120 130 140 150
QVIFYEGVNF SPSHGFKCLA YGDNKRWMGN KARFYARVYE KMAQYRSLSF
160 170 180 190 200
VNVSYAYGGN AKPTSICKDK TLTLNNPTFI SKESNYVDYY YESEANFTLQ
210 220 230 240 250
GCDEFIVPLC VFNGHSKGSS SDPANKYYTD SQSYYNMDTG VLYGFNSTLD
260 270 280 290 300
VGNTVQNPGL DLTCRYLALT PGNYKAVSLE YLLSLPSKAI CLRKPKSFMP
310 320 330 340 350
VQVVDSRWNS TRQSDNMTAV ACQLPYCFFR NTSADYSGGT HDVHHGDFHF
360 370 380 390 400
RQLLSGLLYN VSCIAQQGAF VYNNVSSSWP AYGYGHCPTA ANIGYMAPVC
410 420 430
IYDPLPVILL GVLLGIAVLI IVFLMFYFMT DSGVRLHEA
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. Translation: AAX08110.1.
AB008939 Genomic RNA. Translation: BAA23718.1.
M64316 Genomic RNA. Translation: AAA46460.1.
PIRiA40476. HMIHMS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY771997 Genomic RNA. Translation: AAX08110.1 .
AB008939 Genomic RNA. Translation: BAA23718.1 .
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 22-400 [» ]
4C7W X-ray 2.50 A/B 22-400 [» ]
ProteinModelPortali P31614.
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. "Murine hepatitis virus DVIM strain hemagglutinin-esterase glycoprotein gene, complete cds."
    Sugiyama K., Morita E., Ebina H., Muto A., Himeno H.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: DVIM.
  4. "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.
  5. "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.
  6. "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
Secondary accession number(s): O55252
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 2014
Last modified: October 29, 2014
This is version 91 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