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HEMA_I61A1
ID   HEMA_I61A1              Reviewed;         566 AA.
AC   Q9WCD8; B3EUQ6;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   02-DEC-2020, entry version 104.
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/Swine/Wisconsin/1/1961 H1N1).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=383533;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9696833; DOI=10.1128/jvi.72.9.7367-7373.1998;
RA   Ito T., Couceiro J.N., Kelm S., Baum L.G., Krauss S., Castrucci M.R.,
RA   Donatelli I., Kida H., Paulson J.C., Webster R.G., Kawaoka Y.;
RT   "Molecular basis for the generation in pigs of influenza A viruses with
RT   pandemic potential.";
RL   J. Virol. 72:7367-7373(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Spiro D., Halpin R., Boyne A., Bera J., Ghedin E., Hostetler J.,
RA   Fedorova N., Kim M., Zaborsky J., Overton L., Djuric K., Sarmiento M.,
RA   Sitz J., Katzel D., Webster R.G., Hoffmann E., Krauss S., Naeve C.,
RA   Bolotov P., Bao Y., Sanders R., Dernovoy D., Kiryutin B., Lipman D.J.,
RA   Tatusova T.;
RT   "The NIAID influenza genome sequencing project.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RG   The NIAID Influenza Genome Sequencing Consortium;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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. Interacts with human
CC       CACNA1C. {ECO:0000250|UniProtKB:Q289M7}.
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; AF091307; AAD25302.1; -; mRNA.
DR   EMBL; CY032213; ACD85154.1; -; Viral_cRNA.
DR   SMR; Q9WCD8; -.
DR   PRO; PR:Q9WCD8; -.
DR   Proteomes; UP000007769; 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   2: Evidence at transcript level;
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..17
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CHAIN           18..566
FT                   /note="Hemagglutinin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT                   /id="PRO_0000440397"
FT   CHAIN           18..343
FT                   /note="Hemagglutinin HA1 chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT                   /id="PRO_5000055150"
FT   CHAIN           345..566
FT                   /note="Hemagglutinin HA2 chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT                   /id="PRO_5000055151"
FT   TOPO_DOM        18..529
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   TRANSMEM        530..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   TOPO_DOM        551..566
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   SITE            344..345
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   LIPID           555
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   LIPID           562
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   LIPID           565
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        498
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        21..481
FT                   /note="Interchain (between HA1 and HA2 chains)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        59..292
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        72..84
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        107..153
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        296..320
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        488..492
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   VARIANT         172
FT                   /note="E -> G"
SQ   SEQUENCE   566 AA;  63083 MW;  1CC621E7A3B45111 CRC64;
     MKAILLVLLC AFAATNADTL CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDRHNGKLCK
     LGGIAPLHLG KCNIAGWLLG NPECELLLTV SSWSYIVETS NSDNGTCYPG DFINYEELRE
     QLSSVSSFER FEIFPKTSSW PNHETNRGVT AACPYAGANS FYRNLIWLVK KESSYPKLSK
     SYVNNKGKEV LVLWGIHHPP TSTDQQSLYQ NADAYVFVGS SKYNRKFKPE IAARPKVRGQ
     AGRMNYYWTL IEPGDTITFE ATGNLVVPRY AFAMNRGSGS GIIISDAPVH DCNTKCQTPK
     GAINTSLPFQ NIHPVTIGEC PKYVKSTKLR MATGLRNIPS IQSRGLFGAI AGFIEGGWTG
     MIDGWYGYHH QNGQGSGYAA DQKSTQNAID GITNKVNSVI EKMNMQFTAV GKEFNNLEKR
     IENLNKKVDD GFLDVWTYNA ELLVLLENER TLDFHDSNVK NLYEKVRSQL RNNAKEIGNG
     CFEFYHKCDD TCMESVKNGT YDYPKYSEES KLNREEIDGV KLESTRVYQI LAIYSTVASS
     LVLLVSLGAI SFWMCSNGSL QCRICI
 
 
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