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HN_NDVB
ID   HN_NDVB                 Reviewed;         577 AA.
AC   P32884; P06158;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   02-JUN-2021, entry version 115.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Newcastle disease virus (strain Beaudette C/45) (NDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC   Orthoavulavirus; Avian orthoavulavirus 1.
OX   NCBI_TaxID=11178;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3018130; DOI=10.1099/0022-1317-67-9-1917;
RA   Millar N.S., Chambers P., Emmerson P.T.;
RT   "Nucleotide sequence analysis of the haemagglutinin-neuraminidase gene of
RT   Newcastle disease virus.";
RL   J. Gen. Virol. 67:1917-1927(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2705297; DOI=10.1016/0042-6822(89)90151-7;
RA   Sakaguchi T., Toyoda T., Gotoh B., Inocencio N.M., Kuma K., Miyata T.,
RA   Nagai Y.;
RT   "Newcastle disease virus evolution. I. Multiple lineages defined by
RT   sequence variability of the hemagglutinin-neuraminidase gene.";
RL   Virology 169:260-272(1989).
CC   -!- FUNCTION: Mediates the viral entry into the host cell together with
CC       fusion/F protein. Attaches the virus to sialic acid-containing cell
CC       receptors and thereby initiates infection. Binding of HN protein to the
CC       receptor induces a conformational change that allows the F protein to
CC       trigger virion/cell membranes fusion. {ECO:0000250|UniProtKB:Q91UL0}.
CC   -!- FUNCTION: Neuraminidase activity ensures the efficient spread of the
CC       virus by dissociating the mature virions from the neuraminic acid
CC       containing glycoproteins. {ECO:0000250|UniProtKB:Q91UL0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC         (2->8)- glycosidic linkages of terminal sialic acid residues in
CC         oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC         synthetic substrates.; EC=3.2.1.18;
CC         Evidence={ECO:0000250|UniProtKB:Q91UL0};
CC   -!- SUBUNIT: Homodimer. Forms homotetramers. Interacts with fusion/F
CC       protein. Interacts with host CG-1B; this interaction inhibits viral
CC       adsorption and replication rather than internalization.
CC       {ECO:0000250|UniProtKB:Q91UL0}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:Q91UL0};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q91UL0}.
CC       Host cell membrane {ECO:0000250|UniProtKB:Q91UL0}; Single-pass type II
CC       membrane protein {ECO:0000250|UniProtKB:Q91UL0}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC       family. {ECO:0000305}.
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DR   EMBL; X04355; CAA27880.1; -; Genomic_RNA.
DR   EMBL; M24710; AAA46660.1; -; Genomic_RNA.
DR   PIR; F46328; F46328.
DR   PDB; 1USR; X-ray; 2.00 A; A/B=124-577.
DR   PDB; 1USX; X-ray; 2.70 A; A/B/C=124-577.
DR   PDBsum; 1USR; -.
DR   PDBsum; 1USX; -.
DR   SMR; P32884; -.
DR   DrugBank; DB03991; 2-deoxy-2,3-dehydro-N-acetylneuraminic acid.
DR   DrugBank; DB04508; Methyl(6s)-1-Thio-L-Manno-Hexodialdo-6,2-Pyranoside.
DR   DrugBank; DB03740; N-acetyl-alpha-D-glucosamine.
DR   DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   EvolutionaryTrace; P32884; -.
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:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
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   CDD; cd15469; HN; 1.
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; Hydrolase; Membrane; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Virion; Virus entry into host cell.
FT   CHAIN           1..577
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142607"
FT   TOPO_DOM        1..26
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..577
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   REGION          124..152
FT                   /note="Important for interaction with fusion/F protein"
FT                   /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT   MOD_RES         1
FT                   /note="Blocked amino end (Met); by host"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT   CARBOHYD        538
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          144..146
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          167..170
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          172..180
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          185..194
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          203..213
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          219..229
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          231..233
FT                   /evidence="ECO:0007829|PDB:1USX"
FT   STRAND          235..243
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          246..253
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   HELIX           258..263
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          264..266
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          269..275
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          281..285
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   HELIX           288..291
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   TURN            292..294
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          295..300
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          306..308
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          311..320
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   HELIX           325..330
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   HELIX           348..358
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   HELIX           362..364
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          368..377
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          379..381
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          387..389
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   TURN            393..395
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          402..407
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          410..415
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          423..432
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          435..438
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          442..444
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          473..478
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          484..492
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          495..499
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          501..506
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          515..517
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          523..534
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   TURN            535..538
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          539..549
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          551..553
FT                   /evidence="ECO:0007829|PDB:1USR"
FT   STRAND          555..568
FT                   /evidence="ECO:0007829|PDB:1USR"
SQ   SEQUENCE   577 AA;  63142 MW;  1D4C52B4887EC1A1 CRC64;
     MDRAVSQVAL ENDEREAKNT WRLIFRIAIL LLTVVTLATS VASLVYSMGA STPSDLVGIP
     TRISRAEEKI TSALGSNQDV VDRIYKQVAL ESPLALLNTE TTIMNAITSL SYQINGAANN
     SGWGAPIHDP DFIGGIGKEL IVDDASDVTS FYPSAFQEHL NFIPAPTTGS GCTRIPSFDM
     SATHYCYTHN VILSGCRDHS HSHQYLALGV LRTTATGRIF FSTLRSISLD DTQNRKSCSV
     SATPLGCDML CSKVTETEEE DYNSAVPTLM AHGRLGFDGQ YHEKDLDVTT LFEDWVANYP
     GVGGGSFIDG RVWFSVYGGL KPNSPSDTVQ EGKYVIYKRY NDTCPDEQDY QIRMAKSSYK
     PGRFGGKRIQ QAILSIKVST SLGEDPVLTV PPNTVTLMGA EGRILTVGTS HFLYQRGSSY
     FSPALLYPMT VSNKTATLHS PYTFNAFTRP GSIPCQASAR CPNSCVTGVY TDPYPLIFYR
     NHTLRGVFGT MLDSEQARLN PTSAVFDSTS RSRITRVSSS STKAAYTTST CFKVVKTNKT
     YCLSIAEISN TLFGEFRIVP LLVEILKNDG VREARSG
 
 
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