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HN_NDVH4
ID   HN_NDVH4                Reviewed;         577 AA.
AC   P12559; P06158;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   07-APR-2021, entry version 111.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Newcastle disease virus (strain B1-Hitchner/47) (NDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC   Orthoavulavirus; Avian orthoavulavirus 1.
OX   NCBI_TaxID=11181;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3027962; DOI=10.1016/0042-6822(87)90431-4;
RA   Jorgensen E.D., Collins P.L., Lomedico P.T.;
RT   "Cloning and nucleotide sequence of Newcastle disease virus hemagglutinin-
RT   neuraminidase mRNA: identification of a putative sialic acid binding
RT   site.";
RL   Virology 156:12-24(1987).
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; M16573; AAA46668.1; -; mRNA.
DR   EMBL; M24708; AAA46658.1; -; Genomic_RNA.
DR   PIR; A26355; HNNZNC.
DR   SMR; P12559; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
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   2: Evidence at transcript level;
KW   Glycoprotein; Hemagglutinin; Host cell membrane; Host membrane;
KW   Host-virus interaction; Hydrolase; Membrane; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Virion; Virus entry into host cell.
FT   CHAIN           1..577
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142611"
FT   TOPO_DOM        1..26
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..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   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   VARIANT         200
FT                   /note="L -> S"
FT   VARIANT         203
FT                   /note="H -> Y"
FT   VARIANT         324
FT                   /note="T -> S"
SQ   SEQUENCE   577 AA;  63241 MW;  A7BCF780AA8FF70E CRC64;
     MDRAVSQVAL ENDEREAKNT WRLIFRIAIL FLTVVTLAIS VASLLYSMGA STPSDLVGIP
     TRISRAEEKI TSTLGSNQDV VDRIYKQVAL ESPLALLNTE TTIMNAITSL SYQINGAANN
     SGWGAPIHDP DYIGGIGKEL IVDDASDVTS FYPSAFQEHL NFIPAPTTGS GCTRIPSFDM
     SATHYCYTHN VILSGCRDHL HSHQYLALGV LRTSATGRVF FSTLRSINLD DTQNRKSCSV
     SATPLGCDML CSKATETEEE DYNSAVPTRM VHGRLGFDGQ YHEKDLDVTT LFGDWVANYP
     GVGGGSFIDS RVWFSVYGGL KPNTPSDTVQ EGKYVIYKRY NDTCPDEQDY QIRMAKSSYK
     PGRFGGKRIQ QAILSIKVST SLGEDPVLTV PPNTVTLMGA EGRILTVGTS HFLYQRGSSY
     FSPALLYPMT VSNKTATLHS PYTFNAFTRP GSIPCQASAR CPNSCVTGVY TDPYPLIFYR
     NHTLRGVFGT MLDGEQARLN PASAVFDSTS RSRITRVSSS SIKAAYTTST CFKVVKTNKT
     YCLSIAEISN TLFGEFRIVP LLVEILKDDG VREARSG
 
 
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