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Q91IJ0 (Q91IJ0_9INFA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
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 SAAS008980

Subunit structure

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

Sequence similarities

Belongs to the influenza viruses hemagglutinin family. RuleBase RU003324

Sequences

Sequence LengthMass (Da)Tools
Q91IJ0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: C4870EDBCEEAA3CF

FASTA56563,392
        10         20         30         40         50         60 
MKAKLLVLLC TFTATYADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDRHNGKLCL 

        70         80         90        100        110        120 
LKGIAPLQLG NCSVAGWILG NPECELLISK ESWSYIVETP NPENGTCYPG YFADYEELRE 

       130        140        150        160        170        180 
QLSSVSSFER FEIFPKESSW PNHTVTGVSA SCSHNGKSSF YRNLLWLTEK NGLYPNLSKS 

       190        200        210        220        230        240 
YVNNKEKEVL VLWGVHNPSN IGDQRAIYHT ENAYVSVVSS HYSRRFTPEI AKRPKVRDQE 

       250        260        270        280        290        300 
GRINYYWTLL EPGDTIIFEA NGNLIAPWYA FALSRGFGSG IITSNAPMDE CDAKCQTPQG 

       310        320        330        340        350        360 
AINSSLPFQN VHPVTIGECP KYVRSAKLRM VTGLRNIPSI QSRGLFGAIA GFIEGGWTGM 

       370        380        390        400        410        420 
IDGWYGYHHQ NEQGSGYAAD QKSTQNAING ITNKVNSVIE KMNTQFTAVG KEFNKLERRM 

       430        440        450        460        470        480 
ENLNKKVDDG FLDIWTYNAE LLVLLENERT LDFHDSNVKN LYEKVKSQLK NNAKEIGNGC 

       490        500        510        520        530        540 
FEFYHKCNNE CMESVKNGTY DYPKYSEESK LNREKIDGVK LESMGVYQIL AIYSTVASSL 

       550        560 
VLLVSLGAIS FWMCSNGSLQ CRICI 

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References

[1]"Distinct host range of influenza H3N2 virus isolates in Vero and MDCK cells is determined by cell specific glycosylation pattern."
Romanova J., Katinger D., Ferko B., Voglauer R., Mochalova L., Bovin N., Lim W., Katinger H., Egorov A.
Virology 307:90-97(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/Hong Kong/1035/98 EMBL AAK70453.1.
[2]"pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR."
Lorieau J.L., Louis J.M., Schwieters C.D., Bax A.
Proc. Natl. Acad. Sci. U.S.A. 109:19994-19999(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 344-366.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF386777 Genomic RNA. Translation: AAK70453.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LWANMR-A/B/C344-366[»]
HSSPHSSP built from PDB template 1IBN based on UniProtKB P03442.
ProteinModelPortalQ91IJ0.
SMRQ91IJ0. Positions 18-339, 344-518.
ModBaseSearch...

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. Capsid_hemag. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ91IJ0_9INFA
AccessionPrimary (citable) accession number: Q91IJ0
Entry history
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)