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Q9IKD2 (HEMA_CVRSD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Hemagglutinin-esterase

Short name=HE protein
EC=3.1.1.53
Alternative name(s):
E3 glycoprotein
Gene names
Name:HE
OrganismRat coronavirus (strain 681) (RCV-SDAV) (Sialodacryoadenitis virus SDAV-681)
Taxonomic identifier33740 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostRattus norvegicus (Rat) [TaxID: 10116]

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

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.

Subcellular location

Virion membrane; Single-pass type I membrane protein Potential. Host cell membrane; Single-pass type I membrane protein Potential. 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.

Post-translational modification

N-glycosylated in the RER By similarity.

Sequence similarities

Belongs to the influenza type C/coronaviruses hemagglutinin-esterase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 439415Hemagglutinin-esterase
PRO_0000037152

Regions

Topological domain25 – 407383Virion surface Potential
Transmembrane408 – 42821Helical; Potential
Topological domain429 – 43911Intravirion Potential
Region12 – 132121Esterase domain first part By similarity
Region133 – 281149Receptor binding By similarity
Region282 – 395114Esterase domain second part By similarity

Sites

Active site451Nucleophile By similarity
Active site2381Charge relay system By similarity
Active site3451Charge relay system By similarity

Amino acid modifications

Glycosylation941N-linked (GlcNAc...); by host Potential
Glycosylation1961N-linked (GlcNAc...); by host Potential
Glycosylation2461N-linked (GlcNAc...); by host Potential
Glycosylation3091N-linked (GlcNAc...); by host Potential
Glycosylation3161N-linked (GlcNAc...); by host Potential
Glycosylation3311N-linked (GlcNAc...); by host Potential
Glycosylation3601N-linked (GlcNAc...); by host Potential
Glycosylation3741N-linked (GlcNAc...); by host Potential
Disulfide bond49 ↔ 70 By similarity
Disulfide bond118 ↔ 167 By similarity
Disulfide bond202 ↔ 291 By similarity
Disulfide bond210 ↔ 264 By similarity
Disulfide bond322 ↔ 327 By similarity
Disulfide bond363 ↔ 387 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9IKD2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 184E3AECFCE4EF53

FASTA43949,260
        10         20         30         40         50         60 
MGRMCIAMAP RTLLLLIGCQ LVFGFNEPIN IVSHLNDDWF LFGDSRSDCT YVENNGHPKL 

        70         80         90        100        110        120 
DWLDLDPKLC NSGKIAAKSG NSLFRSFHFT DFYNYTGEGD QIIFYEGVSF SPSHGFKCLV 

       130        140        150        160        170        180 
EGDNNKWMGN KARFYALLYK KMAQYRSLSF VTVPYAYGGN AKPTSICKDK TLTLNNPTFI 

       190        200        210        220        230        240 
SKESNYVDYY YVSEANFTLQ GCDEFIVPLC VFNGHSRGSS SDPANKYYTD SQSYYNIDTG 

       250        260        270        280        290        300 
VLYGFNSTLD VGNTAQNPGL DLTCMYLVLT PGNYKAVSLE YLLTIPSKAI CLRKPKRFMP 

       310        320        330        340        350        360 
VQVVDSRWNS TRQSDNMTAV ACQLPYCFFR NTSADYSGDT HDVHHGDFYF RQLLSGLLYN 

       370        380        390        400        410        420 
VSCIAQQGAF LYNNVSSIWP VYGYGHCPTA ANIGYMAPVC LYDPLPVILL GVLLGIAVLI 

       430 
IVFLILYFMA DSSVRLHEA 

« Hide

References

[1]"Primary structure of the sialodacryoadenitis virus genome: sequence of the structural-protein region and its application for differential diagnosis."
Yoo D., Pei Y., Christie N., Cooper M.
Clin. Diagn. Lab. Immunol. 7:568-573(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF207551 Genomic RNA. Translation: AAF97737.1.

3D structure databases

ProteinModelPortalQ9IKD2.
SMRQ9IKD2. Positions 26-392.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
[Graphical view]
PfamPF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
[Graphical view]
SUPFAMSSF49818. SSF49818. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEMA_CVRSD
AccessionPrimary (citable) accession number: Q9IKD2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families