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Q91LS8 (Q91LS8_9INFA) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 78. 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 SAAS SAAS008980

Subunit structure

Homotrimer of disulfide-linked HA1-HA2 By similarity. RuleBase RU003324 SAAS SAAS008980

Subcellular location

Virion membrane; Single-pass type I membrane protein. Host apical cell membrane; Single-pass type I membrane protein By similarity SAAS SAAS008980.

Sequence similarities

Belongs to the influenza viruses hemagglutinin family. RuleBase RU003324

Ontologies

Keywords
   Biological processClathrin- and caveolin-independent endocytosis of virus by host SAAS SAAS008980
Clathrin-mediated endocytosis of virus by host SAAS SAAS008980
Fusion of virus membrane with host endosomal membrane SAAS SAAS013828
Fusion of virus membrane with host membrane
Host-virus interaction
Viral attachment to host cell SAAS SAAS013828
Viral penetration into host cytoplasm
Virus endocytosis by host
Virus entry into host cell
   Cellular componentHost cell membrane SAAS SAAS013828
Host membrane
Membrane
Viral envelope protein RuleBase RU003324 SAAS SAAS013828
Virion
   DomainTransmembrane
Transmembrane helix SAAS SAAS013828
   Molecular functionHemagglutinin SAAS SAAS013828 RuleBase RU003324
   PTMDisulfide bond SAAS SAAS013828
   Technical term3D-structure PDB 2OJE
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

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

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]"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.
[2]"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
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: July 9, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)