GLYCP_HENDH
ID GLYCP_HENDH Reviewed; 604 AA.
AC O89343;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Glycoprotein G;
GN Name=G;
OS Hendra virus (isolate Horse/Autralia/Hendra/1994).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Henipavirus.
OX NCBI_TaxID=928303;
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9837786; DOI=10.1006/viro.1998.9302;
RA Yu M., Hansson E., Langedijk J.P., Eaton B.T., Wang L.F.;
RT "The attachment protein of Hendra virus has high structural similarity but
RT limited primary sequence homology compared with viruses in the genus
RT Paramyxovirus.";
RL Virology 251:227-233(1998).
CC -!- FUNCTION: Attaches the virus to sialic acid-containing cell receptors
CC and thereby initiating infection. Binding of glycoprotein G to the
CC receptor induces a conformational change that allows the F protein to
CC trigger virion/cell membranes fusion (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O89343; P52799: EFNB2; Xeno; NbExp=2; IntAct=EBI-15702753, 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; AF017149; AAC83193.2; -; Genomic_RNA.
DR PIR; T08211; T08211.
DR RefSeq; NP_047112.2; NC_001906.3.
DR PDB; 2VSK; X-ray; 3.30 A; A/C=188-603.
DR PDB; 2X9M; X-ray; 2.90 A; A/B/C/D=185-604.
DR PDB; 6CMG; X-ray; 2.70 A; A=176-603.
DR PDB; 6CMI; X-ray; 2.72 A; B=176-603.
DR PDB; 6PD4; X-ray; 2.20 A; A/B=171-604.
DR PDB; 6PDL; X-ray; 2.70 A; A/C/E/G=171-604.
DR PDB; 6VY4; X-ray; 2.00 A; A/B=185-604.
DR PDB; 6VY6; X-ray; 2.60 A; A=185-604.
DR PDBsum; 2VSK; -.
DR PDBsum; 2X9M; -.
DR PDBsum; 6CMG; -.
DR PDBsum; 6CMI; -.
DR PDBsum; 6PD4; -.
DR PDBsum; 6PDL; -.
DR PDBsum; 6VY4; -.
DR PDBsum; 6VY6; -.
DR SMR; O89343; -.
DR DIP; DIP-46379N; -.
DR IntAct; O89343; 1.
DR CAZy; GH83; Glycoside Hydrolase Family 83.
DR ABCD; O89343; 11 sequenced antibodies.
DR GeneID; 1446471; -.
DR KEGG; vg:1446471; -.
DR EvolutionaryTrace; O89343; -.
DR Proteomes; UP000008771; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044228; C:host cell surface; IDA:CACAO.
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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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; Glycoprotein; Hemagglutinin; Host cell membrane;
KW Host membrane; Host-virus interaction; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..604
FT /note="Glycoprotein G"
FT /id="PRO_0000236008"
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..604
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 STRAND 178..181
FT /evidence="ECO:0007829|PDB:6PD4"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6PDL"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 228..238
FT /evidence="ECO:0007829|PDB:6VY4"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 243..257
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 259..271
FT /evidence="ECO:0007829|PDB:6VY4"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:6VY4"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6VY4"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 314..322
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 361..371
FT /evidence="ECO:0007829|PDB:6VY4"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:6VY4"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:6VY4"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 406..417
FT /evidence="ECO:0007829|PDB:6VY4"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:6VY4"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 511..515
FT /evidence="ECO:0007829|PDB:6VY4"
FT TURN 516..519
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 520..526
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 544..552
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 557..568
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 571..580
FT /evidence="ECO:0007829|PDB:6VY4"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:2X9M"
FT STRAND 589..596
FT /evidence="ECO:0007829|PDB:6VY4"
FT STRAND 599..602
FT /evidence="ECO:0007829|PDB:6PD4"
SQ SEQUENCE 604 AA; 67191 MW; E2FA826A8ED5BE4D CRC64;
MMADSKLVSL NNNLSGKIKD QGKVIKNYYG TMDIKKINDG LLDSKILGAF NTVIALLGSI
IIIVMNIMII QNYTRTTDNQ ALIKESLQSV QQQIKALTDK IGTEIGPKVS LIDTSSTITI
PANIGLLGSK ISQSTSSINE NVNDKCKFTL PPLKIHECNI SCPNPLPFRE YRPISQGVSD
LVGLPNQICL QKTTSTILKP RLISYTLPIN TREGVCITDP LLAVDNGFFA YSHLEKIGSC
TRGIAKQRII GVGEVLDRGD KVPSMFMTNV WTPPNPSTIH HCSSTYHEDF YYTLCAVSHV
GDPILNSTSW TESLSLIRLA VRPKSDSGDY NQKYIAITKV ERGKYDKVMP YGPSGIKQGD
TLYFPAVGFL PRTEFQYNDS NCPIIHCKYS KAENCRLSMG VNSKSHYILR SGLLKYNLSL
GGDIILQFIE IADNRLTIGS PSKIYNSLGQ PVFYQASYSW DTMIKLGDVD TVDPLRVQWR
NNSVISRPGQ SQCPRFNVCP EVCWEGTYND AFLIDRLNWV SAGVYLNSNQ TAENPVFAVF
KDNEILYQVP LAEDDTNAQK TITDCFLLEN VIWCISLVEI YDTGDSVIRP KLFAVKIPAQ
CSES
