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Protein

Hemagglutinin

Gene
N/A
Organism
Influenza A virus (A/swine/Hong Kong/9/98(H9N2))
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 annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei233 – 2331Galactose; via carbonyl oxygenCombined sources

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
OrganismiInfluenza A virus (A/swine/Hong Kong/9/98(H9N2))Imported
Taxonomic identifieri145307 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A

Subcellular locationi

  • Host apical cell membrane SAAS annotation; Single-pass type I membrane protein SAAS annotation
  • Virion membrane SAAS annotation; Single-pass type I membrane protein SAAS annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei525 – 54824HelicalSequence analysisAdd
BLAST

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 – 22Interchain (with C-475)Combined sources
Glycosylationi29 – 291N-linked (GlcNAc...)Combined sourcesCAR_5005390083
Disulfide bondi60 ↔ 286Combined sources
Disulfide bondi73 ↔ 85Combined sources
Disulfide bondi108 ↔ 151Combined sources
Glycosylationi141 – 1411N-linked (GlcNAc...)Combined sourcesCAR_5005390086
Disulfide bondi290 ↔ 314Combined sources
Glycosylationi298 – 2981N-linked (GlcNAc...)Combined sourcesCAR_5005390082
Glycosylationi305 – 3051N-linked (GlcNAc...)Combined sourcesCAR_5005390084
Disulfide bondi475 – 475Interchain (with C-22)Combined sources
Disulfide bondi482 ↔ 486Combined sources
Glycosylationi492 – 4921N-linked (GlcNAc...)Combined sourcesCAR_5005390085

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
1JSDX-ray1.80A19-337[»]
B339-514[»]
1JSHX-ray2.40A19-337[»]
B339-514[»]
1JSIX-ray2.40A19-337[»]
B339-514[»]
ProteinModelPortaliQ91CD4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91CD4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni143 – 1475Glucose bindingCombined sources
Regioni163 – 1642Galactose bindingCombined sources

Sequence similaritiesi

Belongs to the influenza viruses hemagglutinin family.UniRule annotationSAAS annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysisSAAS 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: Fragment.

Q91CD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAASLITIL LVVTASNADK ICIGYQSTNS TETVDTLTET NVPVTHAKEL
60 70 80 90 100
LHTEHNGMLC ATNLGHPLIL DTCTIEGLIY GNPSCDLLLG GREWSYIVER
110 120 130 140 150
PSAVNGMCYP GNVENLEELR SLFSSASSYQ RIQIFPDTIW NVSYSGTSKA
160 170 180 190 200
CSDSFYRSMR WLTQKNNAYP IQDAQYTNNR GKSILFMWGI NHPPTDTVQT
210 220 230 240 250
NLYTRTDTTT SVTTEDINRT FKPVIGPRPL VNGLHGRIDY YWSVLKPGQT
260 270 280 290 300
LRVRSNGNLI APWYGHILSG ESHGRILKTD LNSGNCVVQC QTERGGLNTT
310 320 330 340 350
LPFHNVSKYA FGNCPKYVGV KSLKLAVGLR NVPARSSRGL FGAIAGFIEG
360 370 380 390 400
GWPGLVAGWY GFQHSNDQGV GMAADRDSTQ KAIDKITSKV NNIVDKMNKQ
410 420 430 440 450
YGIIDHEFSE IETRLNMINN KIDDQIQDIW TYNAELLVLL ENQKTLDEHD
460 470 480 490 500
ANVNNLYNKV KRALGSNAME DGKGCFELYH KCDDQCMETI RNGTYNRRKY
510 520 530 540 550
KEESKLERQK IEGIKLESEG TYKILTIYST VASSLVIAMG FAAFLFWAMS
Length:550
Mass (Da):61,453
Last modified:December 1, 2001 - v1
Checksum:i0CED2FFA7258E94F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei550 – 5501Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222810 Genomic DNA. Translation: AAL14080.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222810 Genomic DNA. Translation: AAL14080.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JSDX-ray1.80A19-337[»]
B339-514[»]
1JSHX-ray2.40A19-337[»]
B339-514[»]
1JSIX-ray2.40A19-337[»]
B339-514[»]
ProteinModelPortaliQ91CD4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ91CD4.

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. "Cocirculation of avian H9N2 and contemporary "human" H3N2 influenza A viruses in pigs in southeastern China: potential for genetic reassortment?"
    Peiris J.S., Guan Y., Markwell D., Ghose P., Webster R.G., Shortridge K.F.
    J. Virol. 75:9679-9686(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Swine/Hong Kong/9/98Imported.
  2. "X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs."
    Ha Y., Stevens D.J., Skehel J.J., Wiley D.C.
    Proc. Natl. Acad. Sci. U.S.A. 98:11181-11186(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 19-337 AND 339-514 IN COMPLEX WITH GALACTOSE AND GLUCOSE, GLYCOSYLATION AT ASN-29; ASN-141; ASN-298; ASN-305 AND ASN-492, DISULFIDE BONDS.
  3. "H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes."
    Ha Y., Stevens D.J., Skehel J.J., Wiley D.C.
    EMBO J. 21:865-875(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 19-337 AND 339-514, GLYCOSYLATION AT ASN-29; ASN-141; ASN-298; ASN-305 AND ASN-492, DISULFIDE BONDS.

Entry informationi

Entry nameiQ91CD4_9INFA
AccessioniPrimary (citable) accession number: Q91CD4
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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 one 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.