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Protein

Hemagglutinin-esterase

Gene

HE

Organism
Human torovirus (HuTV)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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-9-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 sitei37NucleophileBy similarity1
Active sitei328Charge 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
OrganismiHuman torovirus (HuTV)
Taxonomic identifieri67605 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeTorovirinaeTorovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini15 – 393Virion surfaceSequence analysisAdd BLAST379
Transmembranei394 – 414HelicalSequence analysisAdd BLAST21
Topological domaini415 – 416IntravirionSequence analysis2

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 – 14Sequence analysisAdd BLAST14
ChainiPRO_000004540015 – 416Hemagglutinin-esteraseAdd BLAST402

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 57By similarity
Glycosylationi59N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi76N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi88 ↔ 136By similarity
Disulfide bondi108 ↔ 156By similarity
Disulfide bondi192 ↔ 273By similarity
Disulfide bondi200 ↔ 246By similarity
Disulfide bondi206 ↔ 213By similarity
Glycosylationi257N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi278N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi294N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi304 ↔ 309By similarity
Glycosylationi322N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi343N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi346 ↔ 371By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9Q9G3.
SMRiQ9Q9G3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4 – 121Esterase domain first partBy similarityAdd BLAST118
Regioni122 – 263Receptor bindingBy similarityAdd BLAST142
Regioni264 – 379Esterase domain second partBy similarityAdd BLAST116

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi64 – 67Poly-Ser4
Compositional biasi402 – 405Poly-Val4

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.

Q9Q9G3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLILFFPS FAFAVTPVTP YFGPLYITFN CCLFGDSRSD CTKVQSPMSL
60 70 80 90 100
DNPQNFCPNF SLKSSSSMFF SIHYNNHSSL VLFDNFNCRI EKVYYNGVNL
110 120 130 140 150
SPRNQYSCYD EGVDSYMELK TSFNIKLNQM ATILRCIKLI QLKARSSFTT
160 170 180 190 200
LQDVVCRTNK YLPNNPTFAL LSDTVPTWVQ FVLPDLSGKT ICIKYLVPFC
210 220 230 240 250
HLNHGCFTAG SSCPPFGVSY VSDSFNYGFN DATPYIGLAE SHDNVCDYLF
260 270 280 290 300
VEAGTHNASI VGNFLFYPTK SYCFNTMNFT VPVQAIQSIW SEGNESDDAI
310 320 330 340 350
AEACKPPFCI YYSKTTPYTV TNGSNADHRD DEVRMMVRGL LYNSSCISAQ
360 370 380 390 400
GSTPLALYST AMLYAPIYGS CPQYVKLFDT SGSESVDVIS SSYFVATWVL
410
LVVVVILIFV IISFFC
Length:416
Mass (Da):46,534
Last modified:May 1, 2000 - v1
Checksum:i13607F00B989ACD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159585 mRNA. Translation: AAF00614.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159585 mRNA. Translation: AAF00614.1.

3D structure databases

ProteinModelPortaliQ9Q9G3.
SMRiQ9Q9G3.
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_HUTV
AccessioniPrimary (citable) accession number: Q9Q9G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.