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Protein

Hemagglutinin-esterase

Gene

HE

Organism
Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei42NucleophileBy similarity1
Active sitei339Charge relay systemBy similarity1
Active sitei342Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

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 A59) (MHV-A59) (Murine hepatitis virus)
Taxonomic identifieri11142 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
Proteomesi
  • UP000007192 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 404Virion surfaceSequence analysisAdd BLAST384
Transmembranei405 – 425HelicalSequence analysisAdd BLAST21
Topological domaini426 – 428IntravirionSequence analysis3

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000003714521 – 428Hemagglutinin-esteraseAdd BLAST408

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46 ↔ 67By similarity
Glycosylationi91N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi115 ↔ 164By similarity
Glycosylationi149N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi193N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi199 ↔ 288By similarity
Disulfide bondi207 ↔ 261By similarity
Glycosylationi243N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi313N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi319 ↔ 324By similarity
Glycosylationi328N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi332N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi357N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi360 ↔ 384By similarity
Glycosylationi371N-linked (GlcNAc...); by hostSequence analysis1

Post-translational modificationi

N-glycosylated in the RER.

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.

Structurei

3D structure databases

ProteinModelPortaliP31615.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 129Esterase domain first partBy similarityAdd BLAST121
Regioni130 – 278Receptor bindingBy similarityAdd BLAST149
Regioni279 – 392Esterase domain second partBy similarityAdd BLAST114

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
[Graphical view]
SUPFAMiSSF49818. SSF49818. 1 hit.
SSF52266. SSF52266. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P31615-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCIAMAPRTL LLLIXCQLVF GFNEPLNIVS HLNDDWFLFG DSRSDCTYVE
60 70 80 90 100
NNGHPKLDWL DLDPKLCNSG KISAKSGNSL FRSFHFTDFY NYTGEGDQIV
110 120 130 140 150
FYEGVNFSPS HGFKCLAHGD NKRWMGNKAR FYARVYEKMA QYRSLSFVNV
160 170 180 190 200
SYAYGGNAKP ASICKDNTLT LNNPTFISKE SNYVDYYYES EANFTLEGCD
210 220 230 240 250
EFIVPLCGFN GHSKGSSSDA ANKYYTDSQS YYNMDIGVLY GFNSTLDVGN
260 270 280 290 300
TAKDPGLDLT CRYLALTPGN YKAVSLEYLL SLPSKAICLH KTKRFMPVQV
310 320 330 340 350
VDSRWSSIRQ SDNMTAAACQ LPYCFFRNTS ANYSGGTHDA HHGDFHFRQL
360 370 380 390 400
LSGLLYNVSC IAQQGAFLYN NVSSSWPAYG YGHCPTAANI GYMAPVCIYD
410 420
PLPVILLGVL LGIAVLIIVF LNVLFYDG
Length:428
Mass (Da):47,808
Last modified:May 30, 2000 - v2
Checksum:i0CB408413DFB20EC
GO

Sequence cautioni

The sequence AF029248 differs from that shown. Reason: Frameshift at position 427.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23256 Genomic RNA. Translation: AAA46449.1. Sequence problems.
AF029248 Genomic RNA. No translation available.
PIRiB31165. HMIHMH.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23256 Genomic RNA. Translation: AAA46449.1. Sequence problems.
AF029248 Genomic RNA. No translation available.
PIRiB31165. HMIHMH.

3D structure databases

ProteinModelPortaliP31615.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
[Graphical view]
SUPFAMiSSF49818. SSF49818. 1 hit.
SSF52266. SSF52266. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiHEMA_CVMA5
AccessioniPrimary (citable) accession number: P31615
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 30, 2000
Last modified: October 5, 2016
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Readthrough of the terminator UGA may occur between the codons for Ile-14 and Cys-16.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.