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Q5DL24 (Q5DL24_9INFA) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 61. 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 length564 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 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 RuleBase RU003324 SAAS SAAS000149
Virion
   DomainTransmembrane
Transmembrane helix SAAS SAAS000149
   Molecular functionHemagglutinin SAAS SAAS000149 RuleBase RU003324
   PTMDisulfide bond SAAS SAAS000149
   Technical term3D-structure PDB 4F23 PDB 4FIU
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

Amino acid modifications

Glycosylation1811N-linked (GlcNAc...) PDB 4F23 PDB 4FIU
Glycosylation4951N-linked (GlcNAc...) PDB 4F23 PDB 4FIU

Sequences

Sequence LengthMass (Da)Tools
Q5DL24 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: 24ECBDF6D2233971

FASTA56463,266
        10         20         30         40         50         60 
MAKTLYLLVL IFVKYSRADK ICIGYLSNNS TDTVDTLTEN GVPVTSSIDL VETNHTGTYC 

        70         80         90        100        110        120 
SLNGVSPIHL GDCSFEGWIV GNPSCASNIN IREWSYLIED PNAPHKLCFP GEVDNNGELR 

       130        140        150        160        170        180 
HLFSGVNSFS RTELIPPSKW GDILEGTTAS CQNRGANSFY RNLIWLVNKL NKYPVVKGEY 

       190        200        210        220        230        240 
NNTTGRDVLV LWGIHHPDTE ATANKLYVNK NPYTLVSTKE WSRRYELEIG TRIGDGQRSW 

       250        260        270        280        290        300 
MKIYWHLMHP GERITFESSG GLLAPRYGYI IEKYGTGRIF QSGVRLAKCN TKCQTSMGGI 

       310        320        330        340        350        360 
NTNKTFQNIE RNALGDCPKY IKSGQLKLAT GLRNVPSIVE RGLFGAIAGF IEGGWPGLIN 

       370        380        390        400        410        420 
GWYGFQHQNE QGTGIAADKT STQKAINEIT TKINNIIEKM NGNYDSIRGE FNQVEKRINM 

       430        440        450        460        470        480 
IADRVDDAVT DIWSYNAKLL VLIENDRTLD LHDANVRNLH EQIKRALKDN AIDEGDGCFS 

       490        500        510        520        530        540 
ILHKCNDSCM ETIRNGTYNH EDYKEESQLK RQEIEGIKLK TEDNVYKILS IYSCIASSVV 

       550        560 
LVGLILAFIL WACSSGNCRF NVCI 

« Hide

References

[1]Fouchier R.A.M., Munster V., Wallensten A., Bestebroer T.M., Herfst S., Smith D.J., Rimmelzwaan G.F., Olsen B., Osterhaus A.D.M.E.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/black-headed gull/Sweden/2/99 EMBL AAV91214.1.
[2]"Characterization of a novel influenza A virus hemagglutinin subtype (H16) obtained from black-headed gulls."
Fouchier R.A., Munster V., Wallensten A., Bestebroer T.M., Herfst S., Smith D., Rimmelzwaan G.F., Olsen B., Osterhaus A.D.
J. Virol. 79:2814-2822(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/black-headed gull/Sweden/2/99 EMBL AAV91214.1.
[3]"Insights into avian influenza virus pathogenicity: the hemagglutinin precursor HA0 of subtype H16 has an alpha-helix structure in its cleavage site with inefficient HA1/HA2 cleavage."
Lu X., Shi Y., Gao F., Xiao H., Wang M., Qi J., Gao G.F.
J. Virol. 86:12861-12870(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 19-517, GLYCOSYLATION AT ASN-181 AND ASN-495.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY684888 Genomic RNA. Translation: AAV91214.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4F23X-ray1.70A/B/C19-517[»]
4FIUX-ray2.00A/B/C19-517[»]
ProteinModelPortalQ5DL24.
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...

Entry information

Entry nameQ5DL24_9INFA
AccessionPrimary (citable) accession number: Q5DL24
Entry history
Integrated into UniProtKB/TrEMBL: March 29, 2005
Last sequence update: March 29, 2005
Last modified: February 19, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)