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C3W5S1

- C3W5S1_I09A0

UniProt

C3W5S1 - C3W5S1_I09A0

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Protein
Submitted name: Hemagglutinin
Gene
HA
Organism
Influenza A virus (strain swl A/California/04/2009 H1N1)
Status
Unreviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore By similarity.UniRule annotationSAAS annotations

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei204 – 2041GalactoseImported

GO - Biological processi

  1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  3. fusion of virus membrane with host plasma membrane Source: InterPro
  4. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

HemagglutininUniRule annotationSAAS annotations

Keywords - Biological processi

Clathrin- and caveolin-independent endocytosis of virus by hostSAAS annotations, Clathrin-mediated endocytosis of virus by hostSAAS annotations, Fusion of virus membrane with host endosomal membraneSAAS annotations, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cellSAAS annotations, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Submitted name:
HemagglutininImported
Gene namesi
Name:HAImported
OrganismiInfluenza A virus (strain swl A/California/04/2009 H1N1)Imported
Taxonomic identifieri641501 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Subcellular locationi

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
  4. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membraneSAAS annotations, Host membrane, Membrane, Viral envelope proteinUniRule annotationSAAS annotations, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 PredictedImported
Add
BLAST
Chaini18 – 566549 PredictedImported
PRO_5000464216Add
BLAST
Chaini18 – 344327HA1Imported
PRO_5000464217Add
BLAST
Chaini345 – 566222HA2Imported
PRO_5000464218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...)Imported
Glycosylationi40 – 401N-linked (GlcNAc...)Imported
Glycosylationi104 – 1041N-linked (GlcNAc...)Imported
Glycosylationi293 – 2931N-linked (GlcNAc...)Imported
Glycosylationi304 – 3041N-linked (GlcNAc...)
Glycosylationi498 – 4981N-linked (GlcNAc...)Imported

Keywords - PTMi

Disulfide bondSAAS annotations

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HA1-HA2 By similarity.UniRule annotationSAAS annotations

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AL4X-ray2.87A/C/E/G/I/K18-344[»]
B/D/F/H/J/L345-520[»]
3LZGX-ray2.60A/C/E/G/I/K18-344[»]
B/D/F/H/J/L345-518[»]
3UBEX-ray2.15A/C/E/G/I/K18-344[»]
B/D/F/H/J/L345-518[»]
3UBJX-ray2.25A/C/E/G/I/K18-344[»]
B/D/F/H/J/L345-518[»]
3UBNX-ray2.51A/C/E/G/I/K18-344[»]
B/D/F/H/J/L345-518[»]
3UBQX-ray2.00A/C/E/G/I/K18-344[»]
B/D/F/H/J/L345-518[»]
3UYWX-ray1.90A/B/C/D65-278[»]
3UYXX-ray1.80A/B65-278[»]
3ZTNX-ray3.00A18-344[»]
B345-520[»]
4JTVX-ray3.00A/C/E/G/I/K18-338[»]
B/D/F/H/J/L345-506[»]
4JTXX-ray3.00A/C/E/G/I/K18-339[»]
B/D/F/H/J/L345-510[»]
4JU0X-ray2.91A/C/E/G/I/K18-339[»]
B/D/F/H/J/L345-508[»]
4M4YX-ray2.20A/C/E18-344[»]
B/D/F345-518[»]

Miscellaneous databases

EvolutionaryTraceiC3W5S1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni236 – 2394Galactose bindingImported

Sequence similaritiesi

Keywords - Domaini

SignalImported, Transmembrane, Transmembrane helixSAAS annotations

Family and domain databases

Gene3Di2.10.77.10. 1 hit.
3.90.20.10. 1 hit.
3.90.209.20. 1 hit.
InterProiIPR008980. Capsid_hemagglutn.
IPR013828. Hemagglutn_HA1_a/b_dom.
IPR013827. Hemagglutn_HA1_b-rbn_dom.
IPR000149. Hemagglutn_influenz_A.
IPR001364. Hemagglutn_influenz_A/B.
IPR013829. Hemagglutn_stalk.
[Graphical view]
PfamiPF00509. Hemagglutinin. 1 hit.
[Graphical view]
PRINTSiPR00330. HEMAGGLUTN1.
PR00329. HEMAGGLUTN12.
SUPFAMiSSF49818. SSF49818. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

C3W5S1-1 [UniParc]FASTAAdd to Basket

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MKAILVVLLY TFATANADTL CIGYHANNST DTVDTVLEKN VTVTHSVNLL    50
EDKHNGKLCK LRGVAPLHLG KCNIAGWILG NPECESLSTA SSWSYIVETP 100
SSDNGTCYPG DFIDYEELRE QLSSVSSFER FEIFPKTSSW PNHDSNKGVT 150
AACPHAGAKS FYKNLIWLVK KGNSYPKLSK SYINDKGKEV LVLWGIHHPS 200
TSADQQSLYQ NADTYVFVGS SRYSKKFKPE IAIRPKVRDQ EGRMNYYWTL 250
VEPGDKITFE ATGNLVVPRY AFAMERNAGS GIIISDTPVH DCNTTCQTPK 300
GAINTSLPFQ NIHPITIGKC PKYVKSTKLR LATGLRNIPS IQSRGLFGAI 350
AGFIEGGWTG MVDGWYGYHH QNEQGSGYAA DLKSTQNAID EITNKVNSVI 400
EKMNTQFTAV GKEFNHLEKR IENLNKKVDD GFLDIWTYNA ELLVLLENER 450
TLDYHDSNVK NLYEKVRSQL KNNAKEIGNG CFEFYHKCDN TCMESVKNGT 500
YDYPKYSEEA KLNREEIDGV KLESTRIYQI LAIYSTVASS LVLVVSLGAI 550
SFWMCSNGSL QCRICI 566
Length:566
Mass (Da):63,276
Last modified:June 16, 2009 - v1
Checksum:iFBCE01FBF1FCA445
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FJ966082 Viral cRNA. Translation: ACP41105.1.
GQ117044 Viral cRNA. Translation: ACQ76318.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FJ966082 Viral cRNA. Translation: ACP41105.1 .
GQ117044 Viral cRNA. Translation: ACQ76318.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3AL4 X-ray 2.87 A/C/E/G/I/K 18-344 [» ]
B/D/F/H/J/L 345-520 [» ]
3LZG X-ray 2.60 A/C/E/G/I/K 18-344 [» ]
B/D/F/H/J/L 345-518 [» ]
3UBE X-ray 2.15 A/C/E/G/I/K 18-344 [» ]
B/D/F/H/J/L 345-518 [» ]
3UBJ X-ray 2.25 A/C/E/G/I/K 18-344 [» ]
B/D/F/H/J/L 345-518 [» ]
3UBN X-ray 2.51 A/C/E/G/I/K 18-344 [» ]
B/D/F/H/J/L 345-518 [» ]
3UBQ X-ray 2.00 A/C/E/G/I/K 18-344 [» ]
B/D/F/H/J/L 345-518 [» ]
3UYW X-ray 1.90 A/B/C/D 65-278 [» ]
3UYX X-ray 1.80 A/B 65-278 [» ]
3ZTN X-ray 3.00 A 18-344 [» ]
B 345-520 [» ]
4JTV X-ray 3.00 A/C/E/G/I/K 18-338 [» ]
B/D/F/H/J/L 345-506 [» ]
4JTX X-ray 3.00 A/C/E/G/I/K 18-339 [» ]
B/D/F/H/J/L 345-510 [» ]
4JU0 X-ray 2.91 A/C/E/G/I/K 18-339 [» ]
B/D/F/H/J/L 345-508 [» ]
4M4Y X-ray 2.20 A/C/E 18-344 [» ]
B/D/F 345-518 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei C3W5S1.

Family and domain databases

Gene3Di 2.10.77.10. 1 hit.
3.90.20.10. 1 hit.
3.90.209.20. 1 hit.
InterProi IPR008980. Capsid_hemagglutn.
IPR013828. Hemagglutn_HA1_a/b_dom.
IPR013827. Hemagglutn_HA1_b-rbn_dom.
IPR000149. Hemagglutn_influenz_A.
IPR001364. Hemagglutn_influenz_A/B.
IPR013829. Hemagglutn_stalk.
[Graphical view ]
Pfami PF00509. Hemagglutinin. 1 hit.
[Graphical view ]
PRINTSi PR00330. HEMAGGLUTN1.
PR00329. HEMAGGLUTN12.
SUPFAMi SSF49818. SSF49818. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/California/04/2009Imported.
  2. "Antigenic and genetic characteristics of swine-origin 2009 A(H1N1) influenza viruses circulating in humans."
    Garten R.J., Davis C.T., Russell C.A., Shu B., Lindstrom S., Balish A., Sessions W.M., Xu X., Skepner E., Deyde V., Okomo-Adhiambo M., Gubareva L., Barnes J., Smith C.B., Emery S.L., Hillman M.J., Rivailler P., Smagala J.
    , de Graaf M., Burke D.F., Fouchier R.A., Pappas C., Alpuche-Aranda C.M., Lopez-Gatell H., Olivera H., Lopez I., Myers C.A., Faix D., Blair P.J., Yu C., Keene K.M., Dotson P.D.Jr., Boxrud D., Sambol A.R., Abid S.H., St George K., Bannerman T., Moore A.L., Stringer D.J., Blevins P., Demmler-Harrison G.J., Ginsberg M., Kriner P., Waterman S., Smole S., Guevara H.F., Belongia E.A., Clark P.A., Beatrice S.T., Donis R., Katz J., Finelli L., Bridges C.B., Shaw M., Jernigan D.B., Uyeki T.M., Smith D.J., Klimov A.I., Cox N.J.
    Science 325:197-201(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/California/04/2009Imported.
  3. "Human infection with novel swine H1N1 influenza."
    Shu B., Balish A., Garten R., Smith C., Emery S., Barnes J., Deyde V., Klimov A., Cox N.
    Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/California/04/2009Imported.
  4. "Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus."
    Zhang W., Qi J., Shi Y., Li Q., Gao F., Sun Y., Lu X., Lu Q., Vavricka C.J., Liu D., Yan J., Gao G.F.
    Protein Cell 1:459-467(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 18-344 AND 345-520, GLYCOSYLATION AT ASN-40; ASN-104; ASN-293 AND ASN-304.
  5. "Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus."
    Xu R., Ekiert D.C., Krause J.C., Hai R., Crowe J.E., Wilson I.A.
    Science 328:357-360(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 18-344 AND 345-518, GLYCOSYLATION AT ASN-104 AND ASN-293.
  6. "Structural vaccinology: structure-based design of influenza A virus hemagglutinin subtype-specific subunit vaccines."
    Xuan C., Shi Y., Qi J., Zhang W., Xiao H., Gao G.F.
    Protein Cell 2:997-1005(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 65-278.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 18-344 AND 345-520, GLYCOSYLATION AT ASN-40 AND ASN-293.
  8. "Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic."
    Xu R., McBride R., Nycholat C.M., Paulson J.C., Wilson I.A.
    J. Virol. 86:982-990(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 18-344 AND 345-518 IN COMPLEX WITH GALACTOSE, GLYCOSYLATION AT ASN-28; ASN-40; ASN-104; ASN-293; ASN-304 AND ASN-498.
  9. "Molecular basis of the receptor binding specificity switch of the hemagglutinins from both the 1918 and 2009 pandemic influenza A viruses by a D225G substitution."
    Zhang W., Shi Y., Qi J., Gao F., Li Q., Fan Z., Yan J., Gao G.F.
    J. Virol. 87:5949-5958(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 18-339 AND 345-508 IN COMPLEX WITH GALACTOSE, GLYCOSYLATION AT ASN-28; ASN-40; ASN-104 AND ASN-293.
  10. "Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site."
    Hong M., Lee P.S., Hoffman R.M., Zhu X., Krause J.C., Laursen N.S., Yoon S.I., Song L., Tussey L., Crowe J.E., Ward A.B., Wilson I.A.
    J. Virol. 87:12471-12480(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 18-344 AND 345-518, GLYCOSYLATION AT ASN-28; ASN-40; ASN-104 AND ASN-293.

Entry informationi

Entry nameiC3W5S1_I09A0
AccessioniPrimary (citable) accession number: C3W5S1
Entry historyi
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: September 3, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

Similar proteinsi