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C7S226 (C7S226_I57A0) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 37. 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 names
Gene names
Name:HA EMBL ACV49600.1
OrganismInfluenza A virus (strain A/Japan/305/1957 H2N2) EMBL ACV49600.1
Taxonomic identifier387161 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length562 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. RuleBase RU003324 SAAS SAAS000149

Subunit structure

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

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 ACV49600.1
Transmembrane
Transmembrane helix SAAS SAAS000149
   Molecular functionHemagglutinin SAAS SAAS000149 RuleBase RU003324
   PTMDisulfide bond SAAS SAAS000149
   Technical term3D-structure PDB 4HF5 PDB 4HLZ PDB 3KU3 PDB 3KU5 PDB 3KU6 PDB 3QQB PDB 3QQO PDB 3QQI PDB 3QQE
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 – 1515 Potential EMBL ACV49600.1
Chain16 – 562547 Potential EMBL ACV49600.1
PRO_5000514962
Chain16 – 340325HA1 EMBL ACV49600.1
PRO_5000514963
Chain341 – 562222HA2 EMBL ACV49600.1
PRO_5000514964

Regions

Region378 – 3792Sulfate 2 binding PDB 4HLZ
Region378 – 3792Sulfate 3 binding PDB 4HLZ

Sites

Binding site531Sulfate 1 PDB 4HLZ

Amino acid modifications

Glycosylation261N-linked (GlcNAc...)
Glycosylation381N-linked (GlcNAc...) PDB 3KU3 PDB 3KU5 PDB 3KU6 PDB 3QQB PDB 3QQE
Glycosylation1791N-linked (GlcNAc...) PDB 4HF5 PDB 4HLZ PDB 3KU3 PDB 3KU5 PDB 3KU6 PDB 3QQB PDB 3QQO PDB 3QQI PDB 3QQE
Glycosylation3001N-linked (GlcNAc...) PDB 4HF5
Glycosylation4941N-linked (GlcNAc...) PDB 4HLZ PDB 3KU3 PDB 3KU5 PDB 3QQB PDB 3QQE

Sequences

Sequence LengthMass (Da)Tools
C7S226 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: D4747A6A6733E733

FASTA56263,120
        10         20         30         40         50         60 
MAIIYLILLF TAVRGDQICI GYHANNSTEK VDTILERNVT VTHAKDILEK THNGKLCKLN 

        70         80         90        100        110        120 
GIPPLELGDC SIAGWLLGNP ECDRLLSVPE WSYIMEKENP RDGLCYPGSF NDYEELKHLL 

       130        140        150        160        170        180 
SSVKHFEKVK ILPKDRWTQH TTTGGSRACA VSGNPSFFRN MVWLTEKGSN YPVAKGSYNN 

       190        200        210        220        230        240 
TSGEQMLIIW GVHHPNDETE QRTLYQNVGT YVSVGTSTLN KRSTPEIATR PKVNGQGGRM 

       250        260        270        280        290        300 
EFSWTLLDMW DTINFESTGN LIAPEYGFKI SKRGSSGIMK TEGTLENCET KCQTPLGAIN 

       310        320        330        340        350        360 
TTLPFHNVHP LTIGECPKYV KSEKLVLATG LRNVPQIESR GLFGAIAGFI EGGWQGMVDG 

       370        380        390        400        410        420 
WYGYHHSNDQ GSGYAADKES TQKAFDGITN KVNSVIEKMN TQFEAVGKEF SNLERRLENL 

       430        440        450        460        470        480 
NKKMEDGFLD VWTYNAELLV LMENERTLDF HDSNVKNLYD KVRMQLRDNV KELGNGCFEF 

       490        500        510        520        530        540 
YHKCDDECMN SVKNGTYDYP KYEEESKLNR NEIKGVKLSS MGVYQILAIY ATVAGSLSLA 

       550        560 
IMMAGISFWM CSNGSLQCRI CI 

« Hide

References

[1]"The NIAID Influenza Genome Sequencing Project."
Spiro D., Halpin R., Boyne A., Bera J., Ghedin E., Hostetler J., Fedorova N., Kim M., Zaborsky J., Overton L., Djuric K., Sarmiento M., Sitz J., Katzel D., Brown E.G., Keleta L., Bao Y., Sanders R. expand/collapse author list , Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/Japan/305/1957 EMBL ACV49600.1.
[2]The NIAID Influenza Genome Sequencing Consortium
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/Japan/305/1957 EMBL ACV49600.1.
[3]"Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic."
Xu R., McBride R., Paulson J.C., Basler C.F., Wilson I.A.
J. Virol. 84:1715-1721(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 15-340 AND 341-514, GLYCOSYLATION AT ASN-38; ASN-179 AND ASN-494.
[4]"Structural characterization of an early fusion intermediate of influenza virus hemagglutinin."
Xu R., Wilson I.A.
J. Virol. 85:5172-5182(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 61-279, GLYCOSYLATION AT ASN-26; ASN-38; ASN-179; ASN-300 AND ASN-494.
[5]"Structure of a classical broadly neutralizing stem antibody in complex with a pandemic H2 influenza virus hemagglutinin."
Dreyfus C., Ekiert D.C., Wilson I.A.
J. Virol. 87:7149-7154(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 15-340 AND 341-514 IN COMPLEX WITH SULFATE, GLYCOSYLATION AT ASN-26; ASN-179; ASN-300 AND ASN-494.
[6]"A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin."
Xu R., Krause J.C., McBride R., Paulson J.C., Crowe J.E., Wilson I.A.
Nat. Struct. Mol. Biol. 20:363-370(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 15-340 AND 341-514, GLYCOSYLATION AT ASN-179 AND ASN-300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CY045804 Viral cRNA. Translation: ACV49600.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KU3X-ray1.60A15-340[»]
B341-514[»]
3KU5X-ray1.73A15-340[»]
B341-514[»]
3KU6X-ray1.75A15-340[»]
B341-514[»]
3QQBX-ray1.97A15-340[»]
B341-514[»]
3QQEX-ray2.10A15-340[»]
B341-514[»]
3QQIX-ray1.65A/B61-279[»]
3QQOX-ray2.90A/C/E15-340[»]
B/D/F341-514[»]
4HF5X-ray3.00A15-340[»]
B341-514[»]
4HLZX-ray2.90A/C/E15-340[»]
B/D/F341-514[»]
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

EvolutionaryTraceC7S226.

Entry information

Entry nameC7S226_I57A0
AccessionPrimary (citable) accession number: C7S226
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: March 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)