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O89343 (GLYCP_HENDH) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length604 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of glycoprotein G to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion By similarity.

Subcellular location

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

Sequence similarities

Belongs to the paramyxoviruses hemagglutinin-neuraminidase family.

Caution

Henipavirus glycoproteins have no neuraminidase activity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 604604Glycoprotein G
PRO_0000236008

Regions

Topological domain1 – 4949Cytoplasmic Potential
Transmembrane50 – 7021Helical; Potential
Topological domain71 – 604534Extracellular Potential

Amino acid modifications

Glycosylation721N-linked (GlcNAc...); by host Potential
Glycosylation1591N-linked (GlcNAc...); by host Potential
Glycosylation3061N-linked (GlcNAc...); by host Potential
Glycosylation3781N-linked (GlcNAc...); by host Potential
Glycosylation4171N-linked (GlcNAc...); by host Potential
Glycosylation4811N-linked (GlcNAc...); by host Potential
Glycosylation5291N-linked (GlcNAc...); by host Potential

Secondary structure

1 ............................................................. 604
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O89343 [UniParc].

Last modified June 1, 2003. Version 2.
Checksum: E2FA826A8ED5BE4D

FASTA60467,191
        10         20         30         40         50         60 
MMADSKLVSL NNNLSGKIKD QGKVIKNYYG TMDIKKINDG LLDSKILGAF NTVIALLGSI 

        70         80         90        100        110        120 
IIIVMNIMII QNYTRTTDNQ ALIKESLQSV QQQIKALTDK IGTEIGPKVS LIDTSSTITI 

       130        140        150        160        170        180 
PANIGLLGSK ISQSTSSINE NVNDKCKFTL PPLKIHECNI SCPNPLPFRE YRPISQGVSD 

       190        200        210        220        230        240 
LVGLPNQICL QKTTSTILKP RLISYTLPIN TREGVCITDP LLAVDNGFFA YSHLEKIGSC 

       250        260        270        280        290        300 
TRGIAKQRII GVGEVLDRGD KVPSMFMTNV WTPPNPSTIH HCSSTYHEDF YYTLCAVSHV 

       310        320        330        340        350        360 
GDPILNSTSW TESLSLIRLA VRPKSDSGDY NQKYIAITKV ERGKYDKVMP YGPSGIKQGD 

       370        380        390        400        410        420 
TLYFPAVGFL PRTEFQYNDS NCPIIHCKYS KAENCRLSMG VNSKSHYILR SGLLKYNLSL 

       430        440        450        460        470        480 
GGDIILQFIE IADNRLTIGS PSKIYNSLGQ PVFYQASYSW DTMIKLGDVD TVDPLRVQWR 

       490        500        510        520        530        540 
NNSVISRPGQ SQCPRFNVCP EVCWEGTYND AFLIDRLNWV SAGVYLNSNQ TAENPVFAVF 

       550        560        570        580        590        600 
KDNEILYQVP LAEDDTNAQK TITDCFLLEN VIWCISLVEI YDTGDSVIRP KLFAVKIPAQ 


CSES

« Hide

References

[1]"The attachment protein of Hendra virus has high structural similarity but limited primary sequence homology compared with viruses in the genus Paramyxovirus."
Yu M., Hansson E., Langedijk J.P., Eaton B.T., Wang L.F.
Virology 251:227-233(1998) [PubMed: 9837786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF017149 Genomic RNA. Translation: AAC83193.2.
PIRT08211.
RefSeqNP_047112.2. NC_001906.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VSKX-ray3.30A/C188-603[»]
2X9MX-ray2.90A/B/C/D185-604[»]
ProteinModelPortalO89343.
SMRO89343. Positions 188-603.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-46379N.

Protein family/group databases

CAZyGH83. Glycoside Hydrolase Family 83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1446471.

Family and domain databases

InterProIPR000665. Hemagglutn-neuramid_glycoprot.
IPR016285. Hemagglutn-neuramid_paramyxo.
IPR011040. Neuraminidase.
[Graphical view]
Gene3DG3DSA:2.120.10.10. Neuraminidase. 1 hit.
PfamPF00423. HN. 1 hit.
[Graphical view]
PIRSFPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMSSF50939. Sialidase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLYCP_HENDH
AccessionPrimary (citable) accession number: O89343
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: June 1, 2003
Last modified: September 21, 2011
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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