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P0C0V9

- HEMA_BRV1

UniProt

P0C0V9 - HEMA_BRV1

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Protein

Hemagglutinin-esterase

Gene

HE

Organism
Breda virus 1 (BRV-1)
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-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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei37 – 371NucleophileBy similarity
Active sitei325 – 3251Charge relay systemBy similarity
Active sitei328 – 3281Charge relay systemBy similarity

GO - Molecular functioni

  1. sialate O-acetylesterase activity Source: UniProtKB

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: InterPro
  2. 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 positive-strand viruses, no DNA stageNidoviralesCoronaviridaeTorovirinaeTorovirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
ProteomesiUP000000355: Genome

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini15 – 393379Virion surfaceSequence AnalysisAdd
BLAST
Transmembranei394 – 41421HelicalSequence AnalysisAdd
BLAST
Topological domaini415 – 4162IntravirionSequence Analysis

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
Mutagenesisi64 – 641S → T: Strongly reduced activity toward 7,9-di-O-acetylated sialic acids and strongly increased activity toward 9-mono-O-acetylated sialic acids. 1 Publication
Mutagenesisi103 – 1031R → 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 Publication
Mutagenesisi109 – 1091W → A: Reduced lectin activity. 1 Publication
Mutagenesisi168 – 1681L → A: Reduced lectin activity. 1 Publication
Mutagenesisi170 – 1701L → A: Reduced lectin activity. 1 Publication
Mutagenesisi207 – 2071F → A: Loss of lectin activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1414Sequence AnalysisAdd
BLAST
Chaini15 – 416402Hemagglutinin-esterasePRO_0000045398Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 571 Publication
Glycosylationi76 – 761N-linked (GlcNAc...); by host1 Publication
Disulfide bondi88 ↔ 1361 Publication
Disulfide bondi200 ↔ 2461 Publication
Disulfide bondi206 ↔ 2131 Publication
Glycosylationi257 – 2571N-linked (GlcNAc...); by host1 Publication
Glycosylationi278 – 2781N-linked (GlcNAc...); by host1 Publication
Disulfide bondi304 ↔ 3091 Publication
Glycosylationi313 – 3131N-linked (GlcNAc...); by host1 Publication
Glycosylationi322 – 3221N-linked (GlcNAc...); by host1 Publication
Glycosylationi343 – 3431N-linked (GlcNAc...); by host1 Publication
Disulfide bondi346 ↔ 3711 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

DIPiDIP-48962N.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 233Combined sources
Beta strandi27 – 293Combined sources
Beta strandi31 – 366Combined sources
Helixi37 – 393Combined sources
Turni44 – 496Combined sources
Helixi54 – 596Combined sources
Beta strandi60 – 623Combined sources
Helixi68 – 736Combined sources
Beta strandi86 – 883Combined sources
Beta strandi90 – 956Combined sources
Helixi102 – 1043Combined sources
Beta strandi108 – 1114Combined sources
Helixi112 – 13120Combined sources
Beta strandi135 – 1417Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi164 – 17310Combined sources
Beta strandi177 – 1837Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi193 – 20210Combined sources
Beta strandi207 – 2093Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi216 – 2227Combined sources
Beta strandi225 – 2317Combined sources
Beta strandi244 – 2518Combined sources
Beta strandi253 – 26715Combined sources
Beta strandi269 – 2746Combined sources
Beta strandi283 – 2864Combined sources
Helixi299 – 3035Combined sources
Turni306 – 3083Combined sources
Beta strandi309 – 3124Combined sources
Beta strandi320 – 3256Combined sources
Beta strandi328 – 3303Combined sources
Helixi331 – 3377Combined sources
Helixi338 – 3414Combined sources
Beta strandi345 – 3484Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi357 – 3615Combined sources
Beta strandi368 – 3703Combined sources
Helixi375 – 3784Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0C0V9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 121118Esterase domain first partBy similarityAdd
BLAST
Regioni122 – 263142Receptor bindingBy similarityAdd
BLAST
Regioni264 – 379116Esterase domain second partBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 677Poly-Ser
Compositional biasi402 – 4054Poly-Val

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291F → S.
Natural varianti114 – 1141D → G.
Natural varianti133 – 1331T → I.
Natural varianti152 – 1521Q → K.
Natural varianti155 – 1551V → E.
Natural varianti159 – 1591N → K.
Natural varianti214 – 2141L → R.
Natural varianti234 – 2341P → S.
Natural varianti238 – 2381S → L.
Natural varianti416 – 4161C → V.

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.

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 .
RefSeqi YP_337909.1. NC_007447.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3I26 X-ray 1.80 A/B/C/D 15-392 [» ]
3I27 X-ray 2.00 A/B/C/D 15-392 [» ]
ProteinModelPortali P0C0V9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48962N.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3707767.

Miscellaneous databases

EvolutionaryTracei P0C0V9.

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. "Bovine torovirus: sequencing of the structural genes and expression of the nucleocapsid protein of Breda virus."
    Duckmanton L.M., Tellier R., Liu P., Petric M.
    Virus Res. 58:83-96(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "The complete sequence of the bovine torovirus genome."
    Draker R., Roper R.L., Petric M., Tellier R.
    Virus Res. 115:56-68(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "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: CHARACTERIZATION.
  4. "Structural basis for ligand and substrate recognition by torovirus hemagglutinin esterases."
    Langereis M.A., Zeng Q., Gerwig G.J., Frey B., von Itzstein M., Kamerling J.P., de Groot R.J., Huizinga E.G.
    Proc. Natl. Acad. Sci. U.S.A. 106:15897-15902(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 15-392 OF APOPROTEIN AND IN COMPLEX WITH RECEPTOR ANALOG, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-76; ASN-257; ASN-278; ASN-313; ASN-322 AND ASN-343, DISULFIDE BONDS, MUTAGENESIS OF SER-64; ARG-103; TRP-109; LEU-168; LEU-170 AND PHE-207.

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 26, 2014
This is version 56 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

External Data

Dasty 3