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HEMA_I79A7
ID   HEMA_I79A7              Reviewed;         564 AA.
AC   P19698; Q20PM3;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   02-DEC-2020, entry version 120.
DE   RecName: Full=Hemagglutinin {ECO:0000255|HAMAP-Rule:MF_04072};
DE   Contains:
DE     RecName: Full=Hemagglutinin HA1 chain {ECO:0000255|HAMAP-Rule:MF_04072};
DE   Contains:
DE     RecName: Full=Hemagglutinin HA2 chain {ECO:0000255|HAMAP-Rule:MF_04072};
DE   Flags: Precursor;
GN   Name=HA {ECO:0000255|HAMAP-Rule:MF_04072};
OS   Influenza A virus (strain A/Grey teal/Australia/2/1979 H4N4).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=402464;
OH   NCBI_TaxID=8782; Aves.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2705304; DOI=10.1016/0042-6822(89)90166-9;
RA   Donis R.O., Bean W.J., Kawaoka Y., Webster R.G.;
RT   "Distinct lineages of influenza virus H4 hemagglutinin genes in different
RT   regions of the world.";
RL   Virology 169:408-417(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16439620; DOI=10.1126/science.1121586;
RA   Obenauer J.C., Denson J., Mehta P.K., Su X., Mukatira S., Finkelstein D.B.,
RA   Xu X., Wang J., Ma J., Fan Y., Rakestraw K.M., Webster R.G., Hoffmann E.,
RA   Krauss S., Zheng J., Zhang Z., Naeve C.W.;
RT   "Large-scale sequence analysis of avian influenza isolates.";
RL   Science 311:1576-1580(2006).
CC   -!- FUNCTION: Binds to sialic acid-containing receptors on the cell
CC       surface, bringing about the attachment of the virus particle to the
CC       cell. This attachment induces virion internalization of about two third
CC       of the virus particles through clathrin-dependent endocytosis and about
CC       one third through a clathrin- and caveolin-independent pathway. Plays a
CC       major role in the determination of host range restriction and
CC       virulence. Class I viral fusion protein. Responsible for penetration of
CC       the virus into the cell cytoplasm by mediating the fusion of the
CC       membrane of the endocytosed virus particle with the endosomal membrane.
CC       Low pH in endosomes induces an irreversible conformational change in
CC       HA2, releasing the fusion hydrophobic peptide. Several trimers are
CC       required to form a competent fusion pore.
CC   -!- FUNCTION: Binds to sialic acid-containing receptors on the cell
CC       surface, bringing about the attachment of the virus particle to the
CC       cell. This attachment induces virion internalization either through
CC       clathrin-dependent endocytosis or through clathrin- and caveolin-
CC       independent pathway. Plays a major role in the determination of host
CC       range restriction and virulence. Class I viral fusion protein.
CC       Responsible for penetration of the virus into the cell cytoplasm by
CC       mediating the fusion of the membrane of the endocytosed virus particle
CC       with the endosomal membrane. Low pH in endosomes induces an
CC       irreversible conformational change in HA2, releasing the fusion
CC       hydrophobic peptide. Several trimers are required to form a competent
CC       fusion pore. {ECO:0000255|HAMAP-Rule:MF_04072}.
CC   -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2. {ECO:0000255|HAMAP-
CC       Rule:MF_04072}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04072}. Note=Targeted to the apical plasma membrane in
CC       epithelial polarized cells through a signal present in the
CC       transmembrane domain. Associated with glycosphingolipid- and
CC       cholesterol-enriched detergent-resistant lipid rafts.
CC       {ECO:0000255|HAMAP-Rule:MF_04072}.
CC   -!- PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072}.
CC   -!- PTM: In natural infection, inactive HA is matured into HA1 and HA2
CC       outside the cell by one or more trypsin-like, arginine-specific
CC       endoprotease secreted by the bronchial epithelial cells. One identified
CC       protease that may be involved in this process is secreted in lungs by
CC       Clara cells. {ECO:0000255|HAMAP-Rule:MF_04072}.
CC   -!- MISCELLANEOUS: Major glycoprotein, comprises over 80% of the envelope
CC       proteins present in virus particle.
CC   -!- MISCELLANEOUS: The extent of infection into host organism is determined
CC       by HA. Influenza viruses bud from the apical surface of polarized
CC       epithelial cells (e.g. bronchial epithelial cells) into lumen of lungs
CC       and are therefore usually pneumotropic. The reason is that HA is
CC       cleaved by tryptase clara which is restricted to lungs. However, HAs of
CC       H5 and H7 pantropic avian viruses subtypes can be cleaved by furin and
CC       subtilisin-type enzymes, allowing the virus to grow in other organs
CC       than lungs.
CC   -!- MISCELLANEOUS: The influenza A genome consist of 8 RNA segments.
CC       Genetic variation of hemagglutinin and/or neuraminidase genes results
CC       in the emergence of new influenza strains. The mechanism of variation
CC       can be the result of point mutations or the result of genetic
CC       reassortment between segments of two different strains. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC       {ECO:0000255|HAMAP-Rule:MF_04072}.
CC   -!- CAUTION: PubMed:2705304 sequence differs from that shown due to a
CC       possible error of identification. The sequence is closer to
CC       A/Duck/Czeckoslovakia/56 that to sequenced Australian strains.
CC       {ECO:0000305}.
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DR   EMBL; M25284; AAA43217.1; -; Genomic_RNA.
DR   EMBL; CY005672; ABB20362.1; -; Genomic_RNA.
DR   SMR; P19698; -.
DR   PRO; PR:P19698; -.
DR   Proteomes; UP000008575; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046789; F:host cell surface receptor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR   GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.209.20; -; 1.
DR   HAMAP; MF_04072; INFV_HEMA; 1.
DR   InterPro; IPR008980; Capsid_hemagglutn.
DR   InterPro; IPR013828; Hemagglutn_HA1_a/b_dom_sf.
DR   InterPro; IPR000149; Hemagglutn_influenz_A.
DR   InterPro; IPR001364; Hemagglutn_influenz_A/B.
DR   Pfam; PF00509; Hemagglutinin; 1.
DR   PRINTS; PR00330; HEMAGGLUTN1.
DR   PRINTS; PR00329; HEMAGGLUTN12.
DR   SUPFAM; SSF49818; SSF49818; 1.
PE   3: Inferred from homology;
KW   Clathrin- and caveolin-independent endocytosis of virus by host;
KW   Clathrin-mediated endocytosis of virus by host; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Hemagglutinin;
KW   Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW   Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW   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   SIGNAL          1..16
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CHAIN           17..564
FT                   /note="Hemagglutinin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT                   /id="PRO_0000440480"
FT   CHAIN           17..342
FT                   /note="Hemagglutinin HA1 chain"
FT                   /id="PRO_0000038959"
FT   CHAIN           23..342
FT                   /note="Hemagglutinin HA1 chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT                   /id="PRO_0000440481"
FT   CHAIN           344..564
FT                   /note="Hemagglutinin HA2 chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT                   /id="PRO_0000038960"
FT   TOPO_DOM        17..527
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   TRANSMEM        528..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   TOPO_DOM        549..564
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   SITE            343..344
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   LIPID           553
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   LIPID           560
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   LIPID           563
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        497
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        26..480
FT                   /note="Interchain (between HA1 and HA2 chains)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        64..291
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        76..88
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        109..151
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        295..319
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        487..491
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CONFLICT        6..8
FT                   /note="VLL -> ILF (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        14
FT                   /note="S -> N (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="T -> A (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59
FT                   /note="I -> N (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79
FT                   /note="V -> I (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="S -> N (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116
FT                   /note="D -> E (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="G -> S (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243..244
FT                   /note="IS -> DC (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        267
FT                   /note="P -> S (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        273..275
FT                   /note="LDS -> VNN (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        286
FT                   /note="V -> I (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="I -> V (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321
FT                   /note="K -> R (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        404
FT                   /note="E -> D (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        424
FT                   /note="E -> K (in Ref. 1; AAA43217)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   564 AA;  63073 MW;  3020602C217E1C56 CRC64;
     MLSIVVLLLL IAESSSQNYT GNPVICMGHH AVANGTMVKT LTDDQVEVVT AQELVESQIL
     PELCPSPLRL VDGQTCDIVN GALGSPGCDH LNGAEWDVFI ERPSAVDTCY PFDVPDYQSL
     RSILANNGKF EFIAEEFQWN TVKQNGKSGA CKRANVNDFF NRLNWLVKSD GNAYPLQNLT
     KINNGDYARL YIWGVHHPST DTEQTNLYKN NPGRVTVSTK TSQTSVVPNI GSRPLVRGQS
     GRISFYWTIV EPGDLIVFNT IGNLIAPRGH YKLDSQKKST ILNTAVPIGS CVSKCHTDKG
     SLSTTKPFQN ISRIAIGDCP KYVKQGSLKL ATGMRNIPEK ASRGLFGAIA GFIENGWQGL
     IDGWYGFRHQ NAEGTGTAAD LKSTQAAIDQ INGKLNRLIE KTNEKYHQIE KEFEQVEGRI
     QDLEKYVEDT KIDLWSYNAE LLVALENQHT IDVTDSEMNK LFERVRRQLR ENAEDKGNGC
     FEIFHKCDNN CIESIRNGTY DHDIYRDEAI NNRFQIQGVK LTQGYKDIIL WISFSISCFL
     LVALLLAFIL WACQNGNIRC QICI
 
 
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