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Protein

Hemagglutinin-esterase

Gene

HE

Organism
Breda virus 1 (BRV-1)
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-9-di-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. Also hydrolyzes 5-N-acetyl-4-O-acetylneuraminic acid and N-acetyl-9-O-acetylneuraminic acid, but displays a substrate preference for N-acetyl-9-di-O-acetylneuraminic acid. 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 sitei37NucleophileBy similarity1
Active sitei325Charge relay systemBy similarity1
Active sitei328Charge relay systemBy similarity1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB
  • sialate O-acetylesterase activity Source: UniProtKB

GO - Biological processi

  • fusion of virus membrane with host plasma membrane Source: InterPro
  • metabolic process Source: UniProtKB
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
OrganismiBreda virus 1 (BRV-1)
Taxonomic identifieri360393 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeTorovirinaeTorovirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Proteomesi
  • UP000000355 Componenti: Genome

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi64S → T: Strongly reduced activity toward 7,9-di-O-acetylated sialic acids and strongly increased activity toward 9-mono-O-acetylated sialic acids. 1 Publication1
Mutagenesisi103R → H: Strongly reduced activity toward both 7,9-di and 9-mono-O-acetylated sialic acids. Increased activity toward synthetic substrate (4-nitrophenyl)acetate. 1 Publication1
Mutagenesisi109W → A: Reduced lectin activity. 1 Publication1
Mutagenesisi168L → A: Reduced lectin activity. 1 Publication1
Mutagenesisi170L → A: Reduced lectin activity. 1 Publication1
Mutagenesisi207F → A: Loss of lectin activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 14Sequence analysisAdd BLAST14
ChainiPRO_000004539815 – 416Hemagglutinin-esteraseAdd BLAST402

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 571 Publication
Glycosylationi76N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi88 ↔ 1361 Publication
Disulfide bondi200 ↔ 2461 Publication
Disulfide bondi206 ↔ 2131 Publication
Glycosylationi257N-linked (GlcNAc...); by host1 Publication1
Glycosylationi278N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi304 ↔ 3091 Publication
Glycosylationi313N-linked (GlcNAc...); by host1 Publication1
Glycosylationi322N-linked (GlcNAc...); by host1 Publication1
Glycosylationi343N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi346 ↔ 3711 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

DIPiDIP-48962N.

Structurei

Secondary structure

1416
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi21 – 23Combined sources3
Beta strandi27 – 29Combined sources3
Beta strandi31 – 36Combined sources6
Helixi37 – 39Combined sources3
Turni44 – 49Combined sources6
Helixi54 – 59Combined sources6
Beta strandi60 – 62Combined sources3
Helixi68 – 73Combined sources6
Beta strandi86 – 88Combined sources3
Beta strandi90 – 95Combined sources6
Helixi102 – 104Combined sources3
Beta strandi108 – 111Combined sources4
Helixi112 – 131Combined sources20
Beta strandi135 – 141Combined sources7
Beta strandi151 – 153Combined sources3
Beta strandi164 – 173Combined sources10
Beta strandi177 – 183Combined sources7
Beta strandi185 – 187Combined sources3
Beta strandi193 – 202Combined sources10
Beta strandi207 – 209Combined sources3
Beta strandi212 – 214Combined sources3
Beta strandi216 – 222Combined sources7
Beta strandi225 – 231Combined sources7
Beta strandi244 – 251Combined sources8
Beta strandi253 – 267Combined sources15
Beta strandi269 – 274Combined sources6
Beta strandi283 – 286Combined sources4
Helixi299 – 303Combined sources5
Turni306 – 308Combined sources3
Beta strandi309 – 312Combined sources4
Beta strandi320 – 325Combined sources6
Beta strandi328 – 330Combined sources3
Helixi331 – 337Combined sources7
Helixi338 – 341Combined sources4
Beta strandi345 – 348Combined sources4
Beta strandi351 – 353Combined sources3
Beta strandi357 – 361Combined sources5
Beta strandi368 – 370Combined sources3
Helixi375 – 378Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3I26X-ray1.80A/B/C/D15-392[»]
3I27X-ray2.00A/B/C/D15-392[»]
ProteinModelPortaliP0C0V9.
SMRiP0C0V9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0V9.

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 biasi61 – 67Poly-Ser7
Compositional biasi402 – 405Poly-Val4

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19253.

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.

P0C0V9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLILFFPS FAFAATPVTP YYGPGHITFD WCGFGDSRSD CTNPQSPMSL
60 70 80 90 100
DIPQQLCPKF SSKSSSSMFL SLHWNNHSSF VSYDYFNCGV EKVFYEGVNF
110 120 130 140 150
SPRKQYSCWD EGVDGWIELK TRFYTKLYQM ATTSRCIKLI QLQAPSSLPT
160 170 180 190 200
LQAGVCRTNK QLPDNPRLAL LSDTVPTSVQ FVLPGSSGTT ICTKHLVPFC
210 220 230 240 250
YLNHGCFTTG GSCLPFGVSY VSDSFYYGYY DATPQIGSTE SHDYVCDYLF
260 270 280 290 300
MEPGTYNAST VGKFLVYPTK SYCMDTMNIT VPVQAVQSIW SEQYASDDAI
310 320 330 340 350
GQACKAPYCI FYNKTTPYTV TNGSDANHGD DEVRMMMQGL LRNSSCISPQ
360 370 380 390 400
GSTPLALYST EMIYEPNYGS CPQFYKLFDT SGNENIDVIS SSYFVATWVL
410
LVVVVILIFV IISFFC
Length:416
Mass (Da):46,440
Last modified:January 10, 2006 - v1
Checksum:i384C406385439054
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti29F → S.1
Natural varianti114D → G.1
Natural varianti133T → I.1
Natural varianti152Q → K.1
Natural varianti155V → E.1
Natural varianti159N → K.1
Natural varianti214L → R.1
Natural varianti234P → S.1
Natural varianti238S → L.1
Natural varianti416C → V.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076621 Genomic RNA. Translation: AAD03842.1.
AY427798 Genomic RNA. Translation: AAS17961.1.
RefSeqiYP_337909.1. NC_007447.1.

Genome annotation databases

GeneIDi3707767.
KEGGivg:3707767.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076621 Genomic RNA. Translation: AAD03842.1.
AY427798 Genomic RNA. Translation: AAS17961.1.
RefSeqiYP_337909.1. NC_007447.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3I26X-ray1.80A/B/C/D15-392[»]
3I27X-ray2.00A/B/C/D15-392[»]
ProteinModelPortaliP0C0V9.
SMRiP0C0V9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48962N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3707767.
KEGGivg:3707767.

Phylogenomic databases

KOiK19253.

Miscellaneous databases

EvolutionaryTraceiP0C0V9.

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_BRV1
AccessioniPrimary (citable) accession number: P0C0V9
Secondary accession number(s): O39517, Q3T8I8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: November 2, 2016
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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.