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Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (A/black-headed gull/Sweden/2/99(H16N3))
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation
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).SAAS annotation

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

HemagglutininUniRule annotationSAAS annotation

Keywords - Biological processi

Clathrin- and caveolin-independent endocytosis of virus by hostSAAS annotation, Clathrin-mediated endocytosis of virus by hostSAAS annotation, Fusion of virus membrane with host endosomal membraneSAAS annotation, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cellSAAS annotation, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
HemagglutininSAAS annotation
Gene namesi
Name:HAImported
OrganismiInfluenza A virus (A/black-headed gull/Sweden/2/99(H16N3))Imported
Taxonomic identifieri304362 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membraneSAAS annotation, Host membrane, Membrane, Viral envelope proteinUniRule annotationSAAS annotation, Virion

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi22 ↔ 478Combined sources
Disulfide bondi60 ↔ 289Combined sources
Disulfide bondi73 ↔ 85Combined sources
Disulfide bondi108 ↔ 151Combined sources
Glycosylationi181 – 1811N-linked (GlcNAc...)Combined sources
Disulfide bondi293 ↔ 317Combined sources
Disulfide bondi485 ↔ 489Combined sources
Glycosylationi495 – 4951N-linked (GlcNAc...)Combined sources

Keywords - PTMi

Disulfide bondSAAS annotation

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HA1-HA2.UniRule annotationSAAS annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F23X-ray1.70A/B/C19-517[»]
4FIUX-ray2.00A/B/C19-517[»]
ProteinModelPortaliQ5DL24.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the influenza viruses hemagglutinin family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSAAS annotation

Family and domain databases

Gene3Di2.10.77.10. 1 hit.
3.90.20.10. 1 hit.
3.90.209.20. 1 hit.
InterProiIPR008980. 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]
PfamiPF00509. Hemagglutinin. 1 hit.
[Graphical view]
PRINTSiPR00330. HEMAGGLUTN1.
PR00329. HEMAGGLUTN12.
SUPFAMiSSF49818. SSF49818. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5DL24-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTLYLLVL IFVKYSRADK ICIGYLSNNS TDTVDTLTEN GVPVTSSIDL
60 70 80 90 100
VETNHTGTYC SLNGVSPIHL GDCSFEGWIV GNPSCASNIN IREWSYLIED
110 120 130 140 150
PNAPHKLCFP GEVDNNGELR HLFSGVNSFS RTELIPPSKW GDILEGTTAS
160 170 180 190 200
CQNRGANSFY RNLIWLVNKL NKYPVVKGEY NNTTGRDVLV LWGIHHPDTE
210 220 230 240 250
ATANKLYVNK NPYTLVSTKE WSRRYELEIG TRIGDGQRSW MKIYWHLMHP
260 270 280 290 300
GERITFESSG GLLAPRYGYI IEKYGTGRIF QSGVRLAKCN TKCQTSMGGI
310 320 330 340 350
NTNKTFQNIE RNALGDCPKY IKSGQLKLAT GLRNVPSIVE RGLFGAIAGF
360 370 380 390 400
IEGGWPGLIN GWYGFQHQNE QGTGIAADKT STQKAINEIT TKINNIIEKM
410 420 430 440 450
NGNYDSIRGE FNQVEKRINM IADRVDDAVT DIWSYNAKLL VLIENDRTLD
460 470 480 490 500
LHDANVRNLH EQIKRALKDN AIDEGDGCFS ILHKCNDSCM ETIRNGTYNH
510 520 530 540 550
EDYKEESQLK RQEIEGIKLK TEDNVYKILS IYSCIASSVV LVGLILAFIL
560
WACSSGNCRF NVCI
Length:564
Mass (Da):63,266
Last modified:March 29, 2005 - v1
Checksum:i24ECBDF6D2233971
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY684888 Genomic RNA. Translation: AAV91214.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY684888 Genomic RNA. Translation: AAV91214.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F23X-ray1.70A/B/C19-517[»]
4FIUX-ray2.00A/B/C19-517[»]
ProteinModelPortaliQ5DL24.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.10.77.10. 1 hit.
3.90.20.10. 1 hit.
3.90.209.20. 1 hit.
InterProiIPR008980. 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]
PfamiPF00509. Hemagglutinin. 1 hit.
[Graphical view]
PRINTSiPR00330. HEMAGGLUTN1.
PR00329. HEMAGGLUTN12.
SUPFAMiSSF49818. SSF49818. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/black-headed gull/Sweden/2/99Imported.
  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/2/99Imported.
  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, DISULFIDE BONDS, GLYCOSYLATION AT ASN-181 AND ASN-495.

Entry informationi

Entry nameiQ5DL24_9INFA
AccessioniPrimary (citable) accession number: Q5DL24
Entry historyi
Integrated into UniProtKB/TrEMBL: March 29, 2005
Last sequence update: March 29, 2005
Last modified: June 24, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.