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Protein

Hemagglutinin-esterase

Gene

HE

Organism
Murine coronavirus (strain S) (MHV-S) (Murine hepatitis virus)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei45Nucleophile1 Publication1
Active sitei342Charge relay system1 Publication1
Active sitei345Charge relay system1 Publication1

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 S) (MHV-S) (Murine hepatitis virus)
Taxonomic identifieri11145 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiMus musculus (Mouse) [TaxID: 10090]

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 407Virion surfaceSequence analysisAdd BLAST385
Transmembranei408 – 428HelicalSequence analysisAdd BLAST21
Topological domaini429 – 439IntravirionSequence analysisAdd BLAST11

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi45S → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi119L → A: Decreased receptor-binding activity. 1 Publication1
Mutagenesisi166I → A: Decreased receptor-binding activity. 1 Publication1
Mutagenesisi212F → A: Decreased receptor-binding activity. 1 Publication1
Mutagenesisi260L → A: Decreased receptor-binding activity. 1 Publication1
Mutagenesisi281Y → A: Decreased receptor-binding activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000003714823 – 439Hemagglutinin-esteraseAdd BLAST417

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 701 Publication
Glycosylationi94N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi118 ↔ 1671 Publication
Glycosylationi152N-linked (GlcNAc...); by host1 Publication1
Glycosylationi196N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi202 ↔ 2911 Publication
Disulfide bondi210 ↔ 2641 Publication
Glycosylationi246N-linked (GlcNAc...); by host1 Publication1
Glycosylationi309N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi316N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi322 ↔ 3271 Publication
Glycosylationi331N-linked (GlcNAc...); by host1 Publication1
Glycosylationi360N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi363 ↔ 3871 Publication
Glycosylationi374N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi400Interchain1 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

1439
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 31Combined sources3
Beta strandi35 – 37Combined sources3
Beta strandi39 – 45Combined sources7
Helixi61 – 63Combined sources3
Turni68 – 71Combined sources4
Beta strandi75 – 77Combined sources3
Helixi83 – 88Combined sources6
Beta strandi89 – 91Combined sources3
Beta strandi96 – 98Combined sources3
Beta strandi100 – 106Combined sources7
Turni112 – 114Combined sources3
Helixi124 – 141Combined sources18
Turni142 – 144Combined sources3
Beta strandi145 – 152Combined sources8
Beta strandi176 – 180Combined sources5
Beta strandi187 – 189Combined sources3
Beta strandi193 – 199Combined sources7
Beta strandi201 – 214Combined sources14
Beta strandi220 – 222Combined sources3
Beta strandi231 – 236Combined sources6
Turni237 – 239Combined sources3
Beta strandi241 – 246Combined sources6
Beta strandi253 – 257Combined sources5
Beta strandi261 – 269Combined sources9
Beta strandi271 – 285Combined sources15
Beta strandi287 – 295Combined sources9
Beta strandi301 – 305Combined sources5
Helixi317 – 321Combined sources5
Turni324 – 326Combined sources3
Beta strandi327 – 330Combined sources4
Helixi350 – 356Combined sources7
Beta strandi362 – 365Combined sources4
Beta strandi368 – 371Combined sources4
Beta strandi373 – 375Combined sources3
Beta strandi384 – 386Combined sources3
Beta strandi399 – 401Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C7LX-ray2.10A/B25-403[»]
4C7WX-ray2.50A/B25-403[»]
ProteinModelPortaliP31614.
SMRiP31614.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni12 – 132Esterase domain first partBy similarityAdd BLAST121
Regioni133 – 281Receptor bindingBy similarityAdd BLAST149
Regioni217 – 220Receptor binding4
Regioni282 – 395Esterase 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.

P31614-1 [UniParc]FASTAAdd to basket

« Hide

        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)DescriptionActionsGraphical viewLength
Sequence conflicti76S → Y in AAA46460 (PubMed:1649505).Curated1
Sequence conflicti208P → T in AAA46460 (PubMed:1649505).Curated1
Sequence conflicti212F → S in AAA46460 (PubMed:1649505).Curated1
Sequence conflicti218G → S in AAA46460 (PubMed:1649505).Curated1
Sequence conflicti231S → A in AAA46460 (PubMed:1649505).Curated1
Sequence conflicti403D → E in AAA46460 (PubMed:1649505).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AY771997 Genomic RNA. Translation: AAX08110.1.
AB008939 Genomic RNA. Translation: BAA23718.1.
M64316 Genomic RNA. Translation: AAA46460.1.
PIRiA40476. HMIHMS.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C7LX-ray2.10A/B25-403[»]
4C7WX-ray2.50A/B25-403[»]
ProteinModelPortaliP31614.
SMRiP31614.
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_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: November 2, 2016
This is version 96 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

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.