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C3W5S1 (C3W5S1_I09A0) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. SAAS SAAS000149 RuleBase RU003324

Subunit structure

Homotrimer of disulfide-linked HA1-HA2 By similarity. SAAS SAAS000149 RuleBase RU003324

Subcellular location

Virion membrane; Single-pass type I membrane protein. Host apical cell membrane; Single-pass type I membrane protein By similarity SAAS SAAS000149.

Sequence similarities

Belongs to the influenza viruses hemagglutinin family. RuleBase RU003324

Ontologies

Keywords
   Biological processClathrin- and caveolin-independent endocytosis of virus by host SAAS SAAS000149
Clathrin-mediated endocytosis of virus by host SAAS SAAS000149
Fusion of virus membrane with host endosomal membrane SAAS SAAS000149
Fusion of virus membrane with host membrane
Host-virus interaction
Viral attachment to host cell SAAS SAAS000149
Viral penetration into host cytoplasm
Virus endocytosis by host
Virus entry into host cell
   Cellular componentHost cell membrane SAAS SAAS000149
Host membrane
Membrane
Viral envelope protein SAAS SAAS000149 RuleBase RU003324
Virion
   DomainSignal EMBL ACP41105.1
Transmembrane
Transmembrane helix SAAS SAAS000149
   Molecular functionHemagglutinin SAAS SAAS000149 RuleBase RU003324
   PTMDisulfide bond SAAS SAAS000149
   Technical term3D-structure PDB 3UBJ PDB 4JTX PDB 3UBN PDB 4JTV PDB 3UYW PDB 3UYX PDB 3UBE PDB 3ZTN PDB 3AL4 PDB 4JU0 PDB 4M4Y PDB 3UBQ PDB 3LZG
Gene Ontology (GO)
   Biological_processclathrin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host endosome membrane

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host plasma membrane

Inferred from electronic annotation. Source: InterPro

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential EMBL ACP41105.1
Chain18 – 566549 Potential EMBL ACP41105.1
PRO_5000464216
Chain18 – 344327HA1 EMBL ACP41105.1
PRO_5000464217
Chain345 – 566222HA2 EMBL ACP41105.1
PRO_5000464218

Regions

Region150 – 1512Sulfate 2 binding PDB 3ZTN
Region236 – 2394Galactose binding PDB 4JU0

Sites

Binding site2041Galactose
Binding site2401Sulfate 2 PDB 3ZTN
Binding site3301Sulfate 1 PDB 3ZTN
Binding site3301Sulfate 3 PDB 3ZTN

Amino acid modifications

Glycosylation281N-linked (GlcNAc...)
Glycosylation401N-linked (GlcNAc...) PDB 4JTX PDB 3UBN PDB 4JTV PDB 3ZTN PDB 3AL4 PDB 4JU0 PDB 4M4Y
Glycosylation1041N-linked (GlcNAc...) PDB 3UBJ PDB 4JU0 PDB 3UBQ PDB 3LZG
Glycosylation2931N-linked (GlcNAc...) PDB 3UBJ PDB 3ZTN PDB 3AL4 PDB 4M4Y PDB 3UBQ PDB 3LZG
Glycosylation3041N-linked (GlcNAc...) PDB 3UBJ PDB 3AL4 PDB 3UBQ
Glycosylation4981N-linked (GlcNAc...) PDB 3UBJ PDB 3UBQ

Sequences

Sequence LengthMass (Da)Tools
C3W5S1 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: FBCE01FBF1FCA445

FASTA56663,276
        10         20         30         40         50         60 
MKAILVVLLY TFATANADTL CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDKHNGKLCK 

        70         80         90        100        110        120 
LRGVAPLHLG KCNIAGWILG NPECESLSTA SSWSYIVETP SSDNGTCYPG DFIDYEELRE 

       130        140        150        160        170        180 
QLSSVSSFER FEIFPKTSSW PNHDSNKGVT AACPHAGAKS FYKNLIWLVK KGNSYPKLSK 

       190        200        210        220        230        240 
SYINDKGKEV LVLWGIHHPS TSADQQSLYQ NADTYVFVGS SRYSKKFKPE IAIRPKVRDQ 

       250        260        270        280        290        300 
EGRMNYYWTL VEPGDKITFE ATGNLVVPRY AFAMERNAGS GIIISDTPVH DCNTTCQTPK 

       310        320        330        340        350        360 
GAINTSLPFQ NIHPITIGKC PKYVKSTKLR LATGLRNIPS IQSRGLFGAI AGFIEGGWTG 

       370        380        390        400        410        420 
MVDGWYGYHH QNEQGSGYAA DLKSTQNAID EITNKVNSVI EKMNTQFTAV GKEFNHLEKR 

       430        440        450        460        470        480 
IENLNKKVDD GFLDIWTYNA ELLVLLENER TLDYHDSNVK NLYEKVRSQL KNNAKEIGNG 

       490        500        510        520        530        540 
CFEFYHKCDN TCMESVKNGT YDYPKYSEEA KLNREEIDGV KLESTRIYQI LAIYSTVASS 

       550        560 
LVLVVSLGAI SFWMCSNGSL QCRICI 

« Hide

References

[1]"Emergence of a novel swine-origin influenza A (H1N1) virus in humans."
Novel Swine-Origin Influenza A (H1N1) Virus Investigation Team
Dawood F.S., Jain S., Finelli L., Shaw M.W., Lindstrom S., Garten R.J., Gubareva L.V., Xu X., Bridges C.B., Uyeki T.M.
N. Engl. J. Med. 360:2605-2615(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/California/04/2009 EMBL ACP41105.1.
[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. expand/collapse author list , 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/04/2009 EMBL ACP41105.1.
[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/04/2009 EMBL ACQ76318.1.
[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]"A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins."
Corti D., Voss J., Gamblin S.J., Codoni G., Macagno A., Jarrossay D., Vachieri S.G., Pinna D., Minola A., Vanzetta F., Silacci C., Fernandez-Rodriguez B.M., Agatic G., Bianchi S., Giacchetto-Sasselli I., Calder L., Sallusto F., Collins P. expand/collapse author list , Haire L.F., Temperton N., Langedijk J.P., Skehel J.J., Lanzavecchia A.
Science 333:850-856(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 18-344 AND 345-520 IN COMPLEX WITH SULFATE, 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ966082 Viral cRNA. Translation: ACP41105.1.
GQ117044 Viral cRNA. Translation: ACQ76318.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.10.77.10. 1 hit.
3.90.20.10. 1 hit.
3.90.209.20. 1 hit.
InterProIPR008980. 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]
PfamPF00509. Hemagglutinin. 1 hit.
[Graphical view]
PRINTSPR00330. HEMAGGLUTN1.
PR00329. HEMAGGLUTN12.
SUPFAMSSF49818. SSF49818. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceC3W5S1.

Entry information

Entry nameC3W5S1_I09A0
AccessionPrimary (citable) accession number: C3W5S1
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: March 19, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)