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Q9IH62

- GLYCP_NIPAV

UniProt

Q9IH62 - GLYCP_NIPAV

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Protein

Glycoprotein G

Gene

G

Organism
Nipah virus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Interacts with host ephrinB2/EFNB2 or ephrin B3/EFNB3 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.2 Publications

GO - Molecular functioni

  1. exo-alpha-sialidase activity Source: InterPro

GO - Biological processi

  1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  2. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin

Keywords - Biological processi

Clathrin-mediated endocytosis of virus by host, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus endocytosis by host, 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
OrganismiNipah virus
Taxonomic identifieri121791 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeHenipavirus
Virus hostiCynopterus brachyotis (Lesser short-nosed fruit bat) (Pachysoma brachyotis) [TaxID: 58060]
Eonycteris spelaea (Lesser dawn bat) (Macroglossus spelaeus) [TaxID: 58065]
Homo sapiens (Human) [TaxID: 9606]
Pteropus hypomelanus (Island flying fox) (Variable flying fox) [TaxID: 9405]
Pteropus vampyrus (Large flying fox) [TaxID: 132908]
Scotophilus kuhlii (Lesser asiatic yellow bat) [TaxID: 153297]
Sus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000002330: Genome, UP000007527: Genome, UP000008676: Genome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4949IntravirionSequence AnalysisAdd
BLAST
Transmembranei50 – 7021HelicalSequence AnalysisAdd
BLAST
Topological domaini71 – 602532Virion surfaceSequence AnalysisAdd
BLAST

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 602602Glycoprotein GPRO_0000236009Add
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

Subunit structurei

Interacts with host EFNB2 and host EFNB3.2 Publications

Protein-protein interaction databases

DIPiDIP-46380N.

Structurei

Secondary structure

1
602
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi178 – 1803Combined sources
Beta strandi201 – 2033Combined sources
Helixi204 – 2063Combined sources
Turni208 – 2114Combined sources
Beta strandi215 – 22511Combined sources
Beta strandi228 – 23811Combined sources
Turni240 – 2423Combined sources
Beta strandi243 – 25715Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi263 – 2719Combined sources
Beta strandi278 – 28710Combined sources
Beta strandi290 – 2978Combined sources
Beta strandi299 – 3013Combined sources
Turni303 – 3053Combined sources
Turni307 – 3093Combined sources
Beta strandi314 – 3229Combined sources
Helixi328 – 3314Combined sources
Beta strandi332 – 3365Combined 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
Helixi418 – 4203Combined sources
Beta strandi426 – 4316Combined 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 – 5507Combined sources
Beta strandi557 – 56812Combined sources
Beta strandi571 – 58111Combined 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
2VSMX-ray1.80A188-602[»]
2VWDX-ray2.25A/B183-602[»]
3D11X-ray2.31A176-602[»]
3D12X-ray3.00A/D176-602[»]
DisProtiDP00686.
ProteinModelPortaliQ9IH62.
SMRiQ9IH62. Positions 176-602.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9IH62.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR000665. Hemagglutn-neuramid.
IPR016285. Hemagglutn-neuramid_paramyxo.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00423. HN. 1 hit.
[Graphical view]
PIRSFiPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9IH62-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPAENKKVRF ENTTSDKGKI PSKVIKSYYG TMDIKKINEG LLDSKILSAF
60 70 80 90 100
NTVIALLGSI VIIVMNIMII QNYTRSTDNQ AVIKDALQGI QQQIKGLADK
110 120 130 140 150
IGTEIGPKVS LIDTSSTITI PANIGLLGSK ISQSTASINE NVNEKCKFTL
160 170 180 190 200
PPLKIHECNI SCPNPLPFRE YRPQTEGVSN LVGLPNNICL QKTSNQILKP
210 220 230 240 250
KLISYTLPVV GQSGTCITDP LLAMDEGYFA YSHLERIGSC SRGVSKQRII
260 270 280 290 300
GVGEVLDRGD EVPSLFMTNV WTPPNPNTVY HCSAVYNNEF YYVLCAVSTV
310 320 330 340 350
GDPILNSTYW SGSLMMTRLA VKPKSNGGGY NQHQLALRSI EKGRYDKVMP
360 370 380 390 400
YGPSGIKQGD TLYFPAVGFL VRTEFKYNDS NCPITKCQYS KPENCRLSMG
410 420 430 440 450
IRPNSHYILR SGLLKYNLSD GENPKVVFIE ISDQRLSIGS PSKIYDSLGQ
460 470 480 490 500
PVFYQASFSW DTMIKFGDVL TVNPLVVNWR NNTVISRPGQ SQCPRFNTCP
510 520 530 540 550
EICWEGVYND AFLIDRINWI SAGVFLDSNQ TAENPVFTVF KDNEILYRAQ
560 570 580 590 600
LASEDTNAQK TITNCFLLKN KIWCISLVEI YDTGDNVIRP KLFAVKIPEQ

CT
Length:602
Mass (Da):67,039
Last modified:October 1, 2000 - v1
Checksum:i3BD2A917D30A73BE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51N → S in strain: Isolate NiV/KHM/CSUR38.
Natural varianti20 – 201I → N in strain: Isolate NiV/MY/99/VRI-0626.
Natural varianti24 – 241V → I in strain: Isolate NiV/KHM/CSUR38.
Natural varianti248 – 2481R → K in strain: Isolate NiV/KHM/CSUR38.
Natural varianti272 – 2721T → A in strain: Isolate NiV/MY/99/VRI-0626.
Natural varianti327 – 3271G → D in strain: Isolate NiV/KHM/CSUR38.
Natural varianti408 – 4081I → V in strain: Isolate NiV/KHM/CSUR38.
Natural varianti426 – 4261V → I in strain: Isolate NiV/KHM/CSUR38.
Natural varianti470 – 4701L → Q in strain: Isolate NiV/KHM/CSUR38.
Natural varianti478 – 4781N → S in strain: Isolate NiV/KHM/CSUR38.
Natural varianti481 – 4811N → D in strain: Isolate NiV/KHM/CSUR38.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF238467 mRNA. Translation: AAF73957.1.
AF212302 Genomic RNA. Translation: AAK29088.1.
AY029767 Genomic RNA. Translation: AAK50545.1.
AF376747 Genomic RNA. Translation: AAM13406.1.
AY029768 Genomic RNA. Translation: AAK50554.1.
AJ564621 Genomic RNA. Translation: CAD92351.1.
AJ564622 Genomic RNA. Translation: CAD92357.1.
AJ564623 Genomic RNA. Translation: CAD92363.1.
AJ627196 Genomic RNA. Translation: CAF25497.1.
AY858111 Genomic RNA. Translation: AAX51853.1.
RefSeqiNP_112027.1. NC_002728.1.

Genome annotation databases

GeneIDi920955.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF238467 mRNA. Translation: AAF73957.1 .
AF212302 Genomic RNA. Translation: AAK29088.1 .
AY029767 Genomic RNA. Translation: AAK50545.1 .
AF376747 Genomic RNA. Translation: AAM13406.1 .
AY029768 Genomic RNA. Translation: AAK50554.1 .
AJ564621 Genomic RNA. Translation: CAD92351.1 .
AJ564622 Genomic RNA. Translation: CAD92357.1 .
AJ564623 Genomic RNA. Translation: CAD92363.1 .
AJ627196 Genomic RNA. Translation: CAF25497.1 .
AY858111 Genomic RNA. Translation: AAX51853.1 .
RefSeqi NP_112027.1. NC_002728.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VSM X-ray 1.80 A 188-602 [» ]
2VWD X-ray 2.25 A/B 183-602 [» ]
3D11 X-ray 2.31 A 176-602 [» ]
3D12 X-ray 3.00 A/D 176-602 [» ]
DisProti DP00686.
ProteinModelPortali Q9IH62.
SMRi Q9IH62. Positions 176-602.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-46380N.

Chemistry

BindingDBi Q9IH62.
ChEMBLi CHEMBL6047.

Protein family/group databases

CAZyi GH83. Glycoside Hydrolase Family 83.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 920955.

Miscellaneous databases

EvolutionaryTracei Q9IH62.

Family and domain databases

Gene3Di 2.120.10.10. 1 hit.
InterProi IPR000665. Hemagglutn-neuramid.
IPR016285. Hemagglutn-neuramid_paramyxo.
IPR011040. Sialidases.
[Graphical view ]
Pfami PF00423. HN. 1 hit.
[Graphical view ]
PIRSFi PIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMi SSF50939. SSF50939. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Molecular characterization of Nipah virus, a newly emergent paramyxovirus."
    Harcourt B.H., Tamin A., Rollin P.E., Ksiazek T.G., Anderson L.J., Bellini W.J., Rota P.A.
    Virology 271:334-349(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Complete nucleotide sequences of Nipah virus isolates from Malaysia."
    Chan Y.P., Chua K.B., Koh C.L., Lim M.E., Lam S.K.
    J. Gen. Virol. 82:2151-2155(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate UMMC1 and Isolate UMMC2.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate Malaysian flying-fox.
  5. "Isolation and molecular identification of Nipah virus from pigs."
    Abubakar S., Chang L.Y., Mohdali A.R., Sharifah S.H., Yusoff K., Zamrod Z.
    Emerg. Infect. Dis. 10:2228-2230(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate NiV/MY/99/UM-0128, Isolate NiV/MY/99/VRI-1413 and Isolate NiV/MY/99/VRI-2794.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate NiV/KHM/CSUR381.
  7. "EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus."
    Negrete O.A., Levroney E.L., Aguilar H.C., Bertolotti-Ciarlet A., Nazarian R., Tajyar S., Lee B.
    Nature 436:401-405(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST EFNB2.
  8. "Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virus."
    Negrete O.A., Wolf M.C., Aguilar H.C., Enterlein S., Wang W., Muehlberger E., Su S.V., Bertolotti-Ciarlet A., Flick R., Lee B.
    PLoS Pathog. 2:78-86(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST EFNB3.
  9. "Molecular characteristics of the Nipah virus glycoproteins."
    Diederich S., Maisner A.
    Ann. N. Y. Acad. Sci. 1102:39-50(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The nipah virus fusion protein is cleaved within the endosomal compartment."
    Diederich S., Moll M., Klenk H.D., Maisner A.
    J. Biol. Chem. 280:29899-29903(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiGLYCP_NIPAV
AccessioniPrimary (citable) accession number: Q9IH62
Secondary accession number(s): Q4KTA8, Q5K4D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 85 of the entry and version 1 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

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