Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q91LS8 (Q91LS8_9INFA) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 76. 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 length281 AA.
Sequence statusFragment.
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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Experimental info

Non-terminal residue11 EMBL AAK82869.1
Non-terminal residue2811 EMBL AAK82869.1

Sequences

Sequence LengthMass (Da)Tools
Q91LS8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 63B306D7AD351E2D

FASTA28131,362
        10         20         30         40         50         60 
STGRICDSPH RILDGKNCTL IDALLGDPHC DGFQNKEWDL FVERSKAYSN CYPYDVPDYA 

        70         80         90        100        110        120 
SLRSLVASSG TLEFTNEGFN WTGVAQNGTS YACKRGSVKS FFSRLNWLHK LEYKYPALNV 

       130        140        150        160        170        180 
TMPNNDKFDK LYIWGVHHPS TDSDQTSLYV QASGRITVST KRSQQTVIPN IGSRPWVRGV 

       190        200        210        220        230        240 
SSIISIYWTI VKPGDILLIN STGNLIAPRG YFKIRSGKSS IMRSDAPIGN CNSECITPNG 

       250        260        270        280 
SIPNDKPFQN VNRITYGACP KYVKQNTLKL ATGMRNVPEK Q 

« Hide

References

[1]"Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence."
Petersson K., Hakansson M., Nilsson H., Forsberg G., Svensson L.A., Liljas A., Walse B.
EMBO J. 20:3306-3312(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 260-272.
[2]"Browser-Based Java Applications for Search and Analysis of Influenza Sequences in GenBank Format."
Shih S.-R., Chen G.-W., Bair C.-H., Bai Y.-L., Yang C.-C., Tsai M.-C.
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/human/Taiwan/0095/96 EMBL AAK82869.1.
[3]"Zinc induces dimerization of the class II major histocompatibility complex molecule that leads to cooperative binding to a superantigen."
Li H., Zhao Y., Guo Y., Li Z., Eisele L., Mourad W.
J. Biol. Chem. 282:5991-6000(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 260-272.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF362820 mRNA. Translation: AAK82869.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HXYX-ray2.60C260-272[»]
2OJEX-ray3.00C/G260-272[»]
ProteinModelPortalQ91LS8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Other

EvolutionaryTraceQ91LS8.

Entry information

Entry nameQ91LS8_9INFA
AccessionPrimary (citable) accession number: Q91LS8
Entry history
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)