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HEMA_I80A8
ID   HEMA_I80A8              Reviewed;         564 AA.
AC   P19702; Q0A3T9;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   25-MAY-2022, entry version 132.
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/Turkey/Minnesota/833/1980 H4N2).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=383603;
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}.
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DR   EMBL; M25290; AAA43223.1; -; Genomic_RNA.
DR   EMBL; CY014751; ABI84643.1; -; Genomic_RNA.
DR   SMR; P19702; -.
DR   Proteomes; UP000008579; 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_0000440488"
FT   CHAIN           17..342
FT                   /note="Hemagglutinin HA1 chain"
FT                   /id="PRO_0000039050"
FT   CHAIN           344..564
FT                   /note="Hemagglutinin HA2 chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT                   /id="PRO_0000039051"
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        303
FT                   /note="S -> T (in Ref. 1; AAA43223)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        391
FT                   /note="I -> T (in Ref. 1; AAA43223)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        519
FT                   /note="V -> D (in Ref. 1; AAA43223)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   564 AA;  63231 MW;  85B67BEC3D2176DC CRC64;
     MLSITILFLL IAEGSSQNYT GNPVICLGHH AVPNGTMVKT LTDDQVEVVT AQELVESQHL
     PELCPSPLRL VDGQTCDIVN GALGSPGCDH LNGAEWDVFI ERPTAVDTCY PFDVPDYQSL
     RSILANNGKF EFIAEEFQWN TVKQNGKSGA CKRANVNDFF NRLNWLTKSD GNAYPLQNLT
     KVNNGDYARL YIWGVHHPST DTEQTNLYEN NPGRVTVSTQ TSQTSVVPNI GSRPWVRGQS
     GRISFYWTIV EPGDLIVFNT IGNLIAPRGH YKLNSQKKST ILNTAVPIGS CVSKCHTDRG
     SISTTKPFQN ISRISIGDCP KYVKQGSLKL ATGMRNIPEK ATRGLFGAIA GFIENGWQGL
     IDGWYGFRHQ NAEGTGTAAD LKSTQAAIDQ INGKLNRLIE KTNEKYHQIE KEFEQVEGRI
     QDLEKYVEDT KIDLWSYNAE LLVALENQHT IDVTDSEMNK LFERVRRQLR ENAEDKGNGC
     FEIFHQCDNS CIESIRNGTY DHDIYRDEAI NNRFQIQGVK LTQGYKDIIL WISFSISCFL
     LVALLLAFIL WACQNGNIRC QICI
 
 
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