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Protein

Glycoprotein G

Gene

G

Organism
Hendra virus (isolate Horse/Autralia/Hendra/1994)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Virus entry into host cell

Protein family/group databases

CAZyiGH83. Glycoside Hydrolase Family 83.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycoprotein G
Gene namesi
Name:G
OrganismiHendra virus (isolate Horse/Autralia/Hendra/1994)
Taxonomic identifieri928303 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeHenipavirus
Virus hostiEquus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Pteropus alecto (Black flying fox) [TaxID: 9402]
Pteropus poliocephalus (Grey-headed flying fox) [TaxID: 9403]
Pteropus scapulatus (Little red flying fox) [TaxID: 94117]
Proteomesi
  • UP000008771 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4949IntravirionSequence analysisAdd
BLAST
Transmembranei50 – 7021HelicalSequence analysisAdd
BLAST
Topological domaini71 – 604534Virion surfaceSequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 604604Glycoprotein GPRO_0000236008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi159 – 1591N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi306 – 3061N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi378 – 3781N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi417 – 4171N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi481 – 4811N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi529 – 5291N-linked (GlcNAc...); by hostSequence analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

DIPiDIP-46379N.

Structurei

Secondary structure

1
604
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi205 – 2084Combined sources
Beta strandi214 – 22512Combined sources
Beta strandi228 – 23811Combined sources
Turni240 – 2423Combined sources
Beta strandi243 – 25715Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi263 – 2719Combined sources
Helixi276 – 2783Combined sources
Beta strandi279 – 2879Combined sources
Beta strandi290 – 2978Combined sources
Beta strandi299 – 3013Combined sources
Turni303 – 3053Combined sources
Turni307 – 3093Combined sources
Beta strandi314 – 3229Combined sources
Beta strandi328 – 33710Combined sources
Beta strandi339 – 3413Combined sources
Beta strandi346 – 3505Combined sources
Beta strandi352 – 3543Combined sources
Beta strandi356 – 3583Combined sources
Beta strandi361 – 37111Combined sources
Helixi372 – 3743Combined sources
Helixi379 – 3813Combined sources
Helixi394 – 3974Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi406 – 41712Combined sources
Beta strandi425 – 4317Combined sources
Beta strandi442 – 4476Combined sources
Beta strandi450 – 4556Combined sources
Beta strandi465 – 4717Combined sources
Turni472 – 4743Combined sources
Beta strandi475 – 4795Combined sources
Beta strandi491 – 4933Combined sources
Beta strandi511 – 5155Combined sources
Turni516 – 5194Combined sources
Beta strandi520 – 5267Combined sources
Beta strandi529 – 5335Combined sources
Beta strandi535 – 5417Combined sources
Beta strandi544 – 5529Combined sources
Beta strandi561 – 5688Combined sources
Beta strandi571 – 5788Combined sources
Beta strandi586 – 5883Combined sources
Beta strandi591 – 5966Combined sources
Beta strandi599 – 6013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VSKX-ray3.30A/C188-603[»]
2X9MX-ray2.90A/B/C/D185-604[»]
ProteinModelPortaliO89343.
SMRiO89343. Positions 188-603.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO89343.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19247.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR016285. Hemagglutn-neuramid.
IPR000665. Hemagglutn/HN.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00423. HN. 1 hit.
[Graphical view]
PIRSFiPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

O89343-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMADSKLVSL NNNLSGKIKD QGKVIKNYYG TMDIKKINDG LLDSKILGAF
60 70 80 90 100
NTVIALLGSI IIIVMNIMII QNYTRTTDNQ ALIKESLQSV QQQIKALTDK
110 120 130 140 150
IGTEIGPKVS LIDTSSTITI PANIGLLGSK ISQSTSSINE NVNDKCKFTL
160 170 180 190 200
PPLKIHECNI SCPNPLPFRE YRPISQGVSD LVGLPNQICL QKTTSTILKP
210 220 230 240 250
RLISYTLPIN TREGVCITDP LLAVDNGFFA YSHLEKIGSC TRGIAKQRII
260 270 280 290 300
GVGEVLDRGD KVPSMFMTNV WTPPNPSTIH HCSSTYHEDF YYTLCAVSHV
310 320 330 340 350
GDPILNSTSW TESLSLIRLA VRPKSDSGDY NQKYIAITKV ERGKYDKVMP
360 370 380 390 400
YGPSGIKQGD TLYFPAVGFL PRTEFQYNDS NCPIIHCKYS KAENCRLSMG
410 420 430 440 450
VNSKSHYILR SGLLKYNLSL GGDIILQFIE IADNRLTIGS PSKIYNSLGQ
460 470 480 490 500
PVFYQASYSW DTMIKLGDVD TVDPLRVQWR NNSVISRPGQ SQCPRFNVCP
510 520 530 540 550
EVCWEGTYND AFLIDRLNWV SAGVYLNSNQ TAENPVFAVF KDNEILYQVP
560 570 580 590 600
LAEDDTNAQK TITDCFLLEN VIWCISLVEI YDTGDSVIRP KLFAVKIPAQ

CSES
Length:604
Mass (Da):67,191
Last modified:June 1, 2003 - v2
Checksum:iE2FA826A8ED5BE4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017149 Genomic RNA. Translation: AAC83193.2.
PIRiT08211.
RefSeqiNP_047112.2. NC_001906.3.

Genome annotation databases

GeneIDi1446471.
KEGGivg:1446471.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017149 Genomic RNA. Translation: AAC83193.2.
PIRiT08211.
RefSeqiNP_047112.2. NC_001906.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VSKX-ray3.30A/C188-603[»]
2X9MX-ray2.90A/B/C/D185-604[»]
ProteinModelPortaliO89343.
SMRiO89343. Positions 188-603.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46379N.

Protein family/group databases

CAZyiGH83. Glycoside Hydrolase Family 83.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1446471.
KEGGivg:1446471.

Phylogenomic databases

KOiK19247.

Miscellaneous databases

EvolutionaryTraceiO89343.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR016285. Hemagglutn-neuramid.
IPR000665. Hemagglutn/HN.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00423. HN. 1 hit.
[Graphical view]
PIRSFiPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiGLYCP_HENDH
AccessioniPrimary (citable) accession number: O89343
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: June 1, 2003
Last modified: October 14, 2015
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Caution

Henipavirus glycoproteins have no neuraminidase activity.Curated

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.