GLYCP_NIPAV
ID GLYCP_NIPAV Reviewed; 602 AA.
AC Q9IH62; Q4KTA8; Q5K4D8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Glycoprotein G;
GN Name=G;
OS Nipah virus.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Henipavirus.
OX NCBI_TaxID=121791;
OH NCBI_TaxID=58060; Cynopterus brachyotis (Lesser short-nosed fruit bat) (Pachysoma brachyotis).
OH NCBI_TaxID=58065; Eonycteris spelaea (Lesser dawn bat) (Macroglossus spelaeus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9405; Pteropus hypomelanus (Island flying fox) (Variable flying fox).
OH NCBI_TaxID=132908; Pteropus vampyrus (Large flying fox).
OH NCBI_TaxID=153297; Scotophilus kuhlii (Lesser asiatic yellow bat).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10860887; DOI=10.1006/viro.2000.0340;
RA Harcourt B.H., Tamin A., Rollin P.E., Ksiazek T.G., Anderson L.J.,
RA Bellini W.J., Rota P.A.;
RT "Molecular characterization of Nipah virus, a newly emergent
RT paramyxovirus.";
RL Virology 271:334-349(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10827955; DOI=10.1126/science.288.5470.1432;
RA Chua K.B., Bellini W.J., Rota P.A., Harcourt B.H., Tamin A., Lam S.K.,
RA Ksiazek T.G., Rollin P.E., Zaki S.R., Shieh W., Goldsmith C.S.,
RA Gubler D.J., Roehrig J.T., Eaton B., Gould A.R., Olson J., Field H.,
RA Daniels P., Ling A.E., Peters C.J., Anderson L.J., Mahy B.W.;
RT "Nipah virus: a recently emergent deadly paramyxovirus.";
RL Science 288:1432-1435(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate UMMC1, and Isolate UMMC2;
RX PubMed=11514724; DOI=10.1099/0022-1317-82-9-2151;
RA Chan Y.P., Chua K.B., Koh C.L., Lim M.E., Lam S.K.;
RT "Complete nucleotide sequences of Nipah virus isolates from Malaysia.";
RL J. Gen. Virol. 82:2151-2155(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Malaysian flying-fox;
RX PubMed=11880045; DOI=10.1016/s1286-4579(01)01522-2;
RA Chua K.B., Koh C.L., Hooi P.S., Wee K.F., Khong J.H., Chua B.H., Chan Y.P.,
RA Lim M.E., Lam S.K.;
RT "Isolation of Nipah virus from Malaysian island flying-foxes.";
RL Microbes Infect. 4:145-151(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate NiV/MY/99/UM-0128, Isolate NiV/MY/99/VRI-1413, and
RC Isolate NiV/MY/99/VRI-2794;
RX PubMed=15663869; DOI=10.3201/eid1012.040452;
RA Abubakar S., Chang L.Y., Mohdali A.R., Sharifah S.H., Yusoff K., Zamrod Z.;
RT "Isolation and molecular identification of Nipah virus from pigs.";
RL Emerg. Infect. Dis. 10:2228-2230(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate NiV/KHM/CSUR381;
RX PubMed=16022778; DOI=10.3201/eid1107.041350;
RA Reynes J.-M., Counor D., Ong S., Faure C., Seng V., Molia S., Walston J.,
RA Georges-Courbot M., Deubel V., Sarthou J.-L.;
RT "Nipah virus in Lyle's flying foxes, Cambodia.";
RL Emerg. Infect. Dis. 11:1042-1047(2005).
RN [7]
RP INTERACTION WITH HOST EFNB2.
RX PubMed=16007075; DOI=10.1038/nature03838;
RA Negrete O.A., Levroney E.L., Aguilar H.C., Bertolotti-Ciarlet A.,
RA Nazarian R., Tajyar S., Lee B.;
RT "EphrinB2 is the entry receptor for Nipah virus, an emergent deadly
RT paramyxovirus.";
RL Nature 436:401-405(2005).
RN [8]
RP INTERACTION WITH HOST EFNB3.
RX PubMed=16477309; DOI=10.1371/journal.ppat.0020007;
RA Negrete O.A., Wolf M.C., Aguilar H.C., Enterlein S., Wang W.,
RA Muehlberger E., Su S.V., Bertolotti-Ciarlet A., Flick R., Lee B.;
RT "Two key residues in ephrinB3 are critical for its use as an alternative
RT receptor for Nipah virus.";
RL PLoS Pathog. 2:78-86(2006).
RN [9]
RP FUNCTION.
RX PubMed=17470910; DOI=10.1196/annals.1408.003;
RA Diederich S., Maisner A.;
RT "Molecular characteristics of the Nipah virus glycoproteins.";
RL Ann. N. Y. Acad. Sci. 1102:39-50(2007).
RN [10]
RP FUNCTION.
RX PubMed=15961384; DOI=10.1074/jbc.m504598200;
RA Diederich S., Moll M., Klenk H.D., Maisner A.;
RT "The nipah virus fusion protein is cleaved within the endosomal
RT compartment.";
RL J. Biol. Chem. 280:29899-29903(2005).
CC -!- FUNCTION: Interacts with host ephrinB2/EFNB2 or ephrin B3/EFNB3 to
CC provide virion attachment to target cell. This attachment induces
CC virion internalization predominantly through clathrin-mediated
CC endocytosis. {ECO:0000269|PubMed:15961384,
CC ECO:0000269|PubMed:17470910}.
CC -!- SUBUNIT: Interacts with host EFNB2 and host EFNB3.
CC {ECO:0000269|PubMed:16007075, ECO:0000269|PubMed:16477309}.
CC -!- INTERACTION:
CC Q9IH62; Q9IH62: G; NbExp=2; IntAct=EBI-15702710, EBI-15702710;
CC Q9IH62; P52799: EFNB2; Xeno; NbExp=5; IntAct=EBI-15702710, EBI-7532268;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type
CC II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC family. {ECO:0000305}.
CC -!- CAUTION: Henipavirus glycoproteins have no neuraminidase activity.
CC {ECO:0000305}.
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DR EMBL; AF238467; AAF73957.1; -; mRNA.
DR EMBL; AF212302; AAK29088.1; -; Genomic_RNA.
DR EMBL; AY029767; AAK50545.1; -; Genomic_RNA.
DR EMBL; AF376747; AAM13406.1; -; Genomic_RNA.
DR EMBL; AY029768; AAK50554.1; -; Genomic_RNA.
DR EMBL; AJ564621; CAD92351.1; -; Genomic_RNA.
DR EMBL; AJ564622; CAD92357.1; -; Genomic_RNA.
DR EMBL; AJ564623; CAD92363.1; -; Genomic_RNA.
DR EMBL; AJ627196; CAF25497.1; -; Genomic_RNA.
DR EMBL; AY858111; AAX51853.1; -; Genomic_RNA.
DR RefSeq; NP_112027.1; NC_002728.1.
DR PDB; 2VSM; X-ray; 1.80 A; A=188-602.
DR PDB; 2VWD; X-ray; 2.25 A; A/B=183-602.
DR PDB; 3D11; X-ray; 2.31 A; A=176-602.
DR PDB; 3D12; X-ray; 3.00 A; A/D=176-602.
DR PDB; 6VY5; X-ray; 3.40 A; A=183-602.
DR PDB; 7TXZ; EM; 3.20 A; A/B/C/D=70-601.
DR PDB; 7TY0; EM; 3.50 A; A/B/C/D=70-601.
DR PDBsum; 2VSM; -.
DR PDBsum; 2VWD; -.
DR PDBsum; 3D11; -.
DR PDBsum; 3D12; -.
DR PDBsum; 6VY5; -.
DR PDBsum; 7TXZ; -.
DR PDBsum; 7TY0; -.
DR SMR; Q9IH62; -.
DR DIP; DIP-46380N; -.
DR IntAct; Q9IH62; 9.
DR MINT; Q9IH62; -.
DR BindingDB; Q9IH62; -.
DR ChEMBL; CHEMBL6047; -.
DR CAZy; GH83; Glycoside Hydrolase Family 83.
DR ABCD; Q9IH62; 6 sequenced antibodies.
DR GeneID; 920955; -.
DR KEGG; vg:920955; -.
DR EvolutionaryTrace; Q9IH62; -.
DR PRO; PR:Q9IH62; -.
DR Proteomes; UP000002330; Genome.
DR Proteomes; UP000007527; Genome.
DR Proteomes; UP000008676; Genome.
DR Proteomes; UP000100567; Genome.
DR Proteomes; UP000110983; Genome.
DR Proteomes; UP000130871; Genome.
DR Proteomes; UP000170143; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IDA:CAFA.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR016285; Hemagglutn-neuramid.
DR InterPro; IPR000665; Hemagglutn/HN.
DR InterPro; IPR036278; Sialidase_sf.
DR Pfam; PF00423; HN; 1.
DR PIRSF; PIRSF001072; Hemagglut-neuramid_paramyxoV; 1.
DR SUPFAM; SSF50939; SSF50939; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Clathrin-mediated endocytosis of virus by host; Glycoprotein;
KW Hemagglutinin; Host cell membrane; Host membrane; Host-virus interaction;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..602
FT /note="Glycoprotein G"
FT /id="PRO_0000236009"
FT TOPO_DOM 1..49
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..602
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VARIANT 5
FT /note="N -> S (in strain: Isolate NiV/KHM/CSUR38)"
FT VARIANT 20
FT /note="I -> N (in strain: Isolate NiV/MY/99/VRI-0626)"
FT VARIANT 24
FT /note="V -> I (in strain: Isolate NiV/KHM/CSUR38)"
FT VARIANT 248
FT /note="R -> K (in strain: Isolate NiV/KHM/CSUR38)"
FT VARIANT 272
FT /note="T -> A (in strain: Isolate NiV/MY/99/VRI-0626)"
FT VARIANT 327
FT /note="G -> D (in strain: Isolate NiV/KHM/CSUR38)"
FT VARIANT 408
FT /note="I -> V (in strain: Isolate NiV/KHM/CSUR38)"
FT VARIANT 426
FT /note="V -> I (in strain: Isolate NiV/KHM/CSUR38)"
FT VARIANT 470
FT /note="L -> Q (in strain: Isolate NiV/KHM/CSUR38)"
FT VARIANT 478
FT /note="N -> S (in strain: Isolate NiV/KHM/CSUR38)"
FT VARIANT 481
FT /note="N -> D (in strain: Isolate NiV/KHM/CSUR38)"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3D12"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:2VSM"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3D11"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:2VWD"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 228..238
FT /evidence="ECO:0007829|PDB:2VSM"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 243..257
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 278..287
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:2VSM"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2VSM"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 314..322
FT /evidence="ECO:0007829|PDB:2VSM"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 361..371
FT /evidence="ECO:0007829|PDB:2VSM"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:2VSM"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:2VSM"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 406..417
FT /evidence="ECO:0007829|PDB:2VSM"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:2VSM"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 511..515
FT /evidence="ECO:0007829|PDB:2VSM"
FT TURN 516..519
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 520..526
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 544..550
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 557..568
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 571..581
FT /evidence="ECO:0007829|PDB:2VSM"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:6VY5"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 591..596
FT /evidence="ECO:0007829|PDB:2VSM"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:3D11"
SQ SEQUENCE 602 AA; 67039 MW; 3BD2A917D30A73BE CRC64;
MPAENKKVRF ENTTSDKGKI PSKVIKSYYG TMDIKKINEG LLDSKILSAF NTVIALLGSI
VIIVMNIMII QNYTRSTDNQ AVIKDALQGI QQQIKGLADK IGTEIGPKVS LIDTSSTITI
PANIGLLGSK ISQSTASINE NVNEKCKFTL PPLKIHECNI SCPNPLPFRE YRPQTEGVSN
LVGLPNNICL QKTSNQILKP KLISYTLPVV GQSGTCITDP LLAMDEGYFA YSHLERIGSC
SRGVSKQRII GVGEVLDRGD EVPSLFMTNV WTPPNPNTVY HCSAVYNNEF YYVLCAVSTV
GDPILNSTYW SGSLMMTRLA VKPKSNGGGY NQHQLALRSI EKGRYDKVMP YGPSGIKQGD
TLYFPAVGFL VRTEFKYNDS NCPITKCQYS KPENCRLSMG IRPNSHYILR SGLLKYNLSD
GENPKVVFIE ISDQRLSIGS PSKIYDSLGQ PVFYQASFSW DTMIKFGDVL TVNPLVVNWR
NNTVISRPGQ SQCPRFNTCP EICWEGVYND AFLIDRINWI SAGVFLDSNQ TAENPVFTVF
KDNEILYRAQ LASEDTNAQK TITNCFLLKN KIWCISLVEI YDTGDNVIRP KLFAVKIPEQ
CT
