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Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (A/turkey/Turkey/1/2005(H5N1))
Status
Unreviewed-Annotation score: Annotation score: 4 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 either through clathrin-dependent endocytosis or through 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
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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHemagglutininUniRule annotationSAAS annotation
Biological processClathrin- and caveolin-independent endocytosis of virus by hostUniRule annotationSAAS annotation, Clathrin-mediated endocytosis of virus by hostUniRule annotationSAAS annotation, Fusion of virus membrane with host endosomal membraneUniRule annotationSAAS annotation, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cellUniRule annotationSAAS annotation, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
HemagglutininUniRule annotation
Cleaved into the following 2 chains:
Hemagglutinin HA2 chainUniRule annotation
Hemagglutinin HA1 chainUniRule annotation
Gene namesi
Name:HAUniRule annotationImported
OrganismiInfluenza A virus (A/turkey/Turkey/1/2005(H5N1))Imported
Taxonomic identifieri375457 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A

Subcellular locationi

  • Host apical cell membrane UniRule annotationSAAS annotation; Single-pass type I membrane protein UniRule annotationSAAS annotation
  • Virion membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Note: Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts.UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei533 – 555HelicalUniRule annotationAdd BLAST23

GO - Cellular componenti

Keywords - Cellular componenti

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

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi20Interchain (with C-483)Combined sources
Glycosylationi27N-linked (GlcNAc...)Combined sources1
Glycosylationi39N-linked (GlcNAc...)Combined sources1
Disulfide bondi58 ↔ 290UniRule annotationCombined sources
Disulfide bondi71 ↔ 83UniRule annotationCombined sources
Disulfide bondi106 ↔ 151UniRule annotationCombined sources
Glycosylationi181N-linked (GlcNAc...)Combined sources1
Disulfide bondi294 ↔ 318UniRule annotationCombined sources
Glycosylationi302N-linked (GlcNAc...)Combined sources1
Disulfide bondi483Interchain (with C-20)Combined sources
Disulfide bondi490 ↔ 494UniRule annotationCombined sources
Lipidationi557S-palmitoyl cysteine; by hostUniRule annotation1
Lipidationi564S-palmitoyl cysteine; by hostUniRule annotation1
Lipidationi567S-palmitoyl cysteine; by hostUniRule annotation1

Post-translational modificationi

In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in lungs by Clara cells.UniRule annotation
Palmitoylated.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei346 – 347Cleavage; by hostUniRule annotation2

Keywords - PTMi

Disulfide bondUniRule annotationSAAS annotation, GlycoproteinUniRule annotation, Lipoprotein, PalmitateUniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-60225N.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BGZX-ray2.68A/C/E17-338[»]
B/D/F347-512[»]
4BH0X-ray2.36A/C/E17-338[»]
B/D/F347-512[»]
4BH1X-ray2.15A/C/E17-338[»]
B/D/F347-512[»]
4CQVX-ray2.86A/C/E17-342[»]
B/D/F347-512[»]
4CQWX-ray2.30A/C/E17-342[»]
B/D/F347-512[»]
4CQXX-ray2.30A/C/E17-342[»]
B/D/F347-512[»]
4CQYX-ray2.05A/C/E17-342[»]
B/D/F347-512[»]
SMRiQ207Z6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni234 – 238Galactose bindingCombined sources5

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili402 – 436Sequence analysisAdd BLAST35

Sequence similaritiesi

Belongs to the influenza viruses hemagglutinin family.UniRule annotationSAAS annotation

Keywords - Domaini

Coiled coilSequence analysis, SignalUniRule annotation, Transmembrane, Transmembrane helixUniRule annotationSAAS annotation

Family and domain databases

Gene3Di3.90.209.20. 1 hit.
HAMAPiMF_04072. INFV_HEMA. 1 hit.
InterProiView protein in InterPro
IPR008980. Capsid_hemagglutn.
IPR013828. Hemagglutn_HA1_a/b_dom_sf.
IPR000149. Hemagglutn_influenz_A.
IPR001364. Hemagglutn_influenz_A/B.
PfamiView protein in Pfam
PF00509. Hemagglutinin. 1 hit.
PRINTSiPR00330. HEMAGGLUTN1.
PR00329. HEMAGGLUTN12.
SUPFAMiSSF49818. SSF49818. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q207Z6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKIVLLLAI VSLVKSDQIC IGYHANNSTE QVDTIMEKNV TVTHAQDILE
60 70 80 90 100
KTHNGKLCDL DGVKPLILRD CSVAGWLLGN PMCDEFLNVP EWSYIVEKIN
110 120 130 140 150
PANDLCYPGN FNDYEELKHL LSRINHFEKI QIIPKSSWSD HEASAGVSSA
160 170 180 190 200
CPYQGRSSFF RNVVWLIKKD NAYPTIKRSY NNTNQEDLLV LWGIHHPNDA
210 220 230 240 250
AEQTRLYQNP TTYISVGTST LNQRLVPKIA TRSKVNGQSG RMEFFWTILK
260 270 280 290 300
PNDAINFESN GNFIAPENAY KIVKKGDSTI MKSELEYGNC NTKCQTPIGA
310 320 330 340 350
INSSMPFHNI HPLTIGECPK YVKSSRLVLA TGLRNSPQGE RRRKKRGLFG
360 370 380 390 400
AIAGFIEGGW QGMVDGWYGY HHSNEQGSGY AADKESTQKA IDGVTNKVNS
410 420 430 440 450
IIDKMNTQFE AVGREFNNLE RRIENLNKKM EDGFLDVWTY NAELLVLMEN
460 470 480 490 500
ERTLDFHDSN VKNLYDKVRL QLRDNAKELG NGCFEFYHRC DNECMESVRN
510 520 530 540 550
GTYDYPQYSE EARLKREEIS GVKLESIGTY QILSIYSTVA SSLALAIMVA
560
GLSLWMCSNG SLQCRICI
Length:568
Mass (Da):64,248
Last modified:April 18, 2006 - v1
Checksum:i4763F22A2A73A57B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ407519 Genomic RNA. Translation: ABD73284.1.
EF619980 Viral cRNA. Translation: ABQ58921.1.

Similar proteinsi

Entry informationi

Entry nameiQ207Z6_9INFA
AccessioniPrimary (citable) accession number: Q207Z6
Entry historyiIntegrated into UniProtKB/TrEMBL: April 18, 2006
Last sequence update: April 18, 2006
Last modified: January 31, 2018
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

Keywords - Technical termi

3D-structureCombined sources