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Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (A/swine/Scotland/410440/94(H1N2))
Status
Unreviewed-Annotation score: -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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.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 HA1 chainUniRule annotation
Hemagglutinin HA2 chainUniRule annotation
Gene namesi
Name:HAUniRule annotation
OrganismiInfluenza A virus (A/swine/Scotland/410440/94(H1N2))Imported
Taxonomic identifieri83206 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeAlphainfluenzavirus

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
Transmembranei531 – 553HelicalUniRule 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 bondi72 ↔ 84UniRule annotation
Disulfide bondi296 ↔ 320UniRule annotation
Disulfide bondi488 ↔ 492UniRule annotation
Lipidationi555S-palmitoyl cysteine; by hostUniRule annotation1
Lipidationi562S-palmitoyl cysteine; by hostUniRule annotation1
Lipidationi565S-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
Sitei344 – 345Cleavage; 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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KXANMR-A345-367[»]
ProteinModelPortaliQ9YTC2
SMRiQ9YTC2
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9YTC2

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili407 – 427Sequence analysisAdd BLAST21

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.

Q9YTC2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEKLLVLLC ALSATDADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL
60 70 80 90 100
EDSHNGKLCR LKGIAPLQLG KCSIAGWILG NPECELLFSK KSWSYIAETP
110 120 130 140 150
NSENGICYPG YFSDYEELRE QLSSVSSFER FEIFPKESSW PKHSVNKGVT
160 170 180 190 200
KSCSHKGKSS FYRNLLWLTE KNGSYPNLSK SYVNNKEKEV LVLWGVHHPS
210 220 230 240 250
NIENQKTIYR KETAYVSVVS SHYNRRFTPE ITRRPKVRDQ EGRINYYWTL
260 270 280 290 300
LEPGDTIIFE ANGNLIAPWY RFALSRGFGS GIIISNASMD ECDAKCQTPQ
310 320 330 340 350
GAINSSLPFQ NVHPVTIGEC PKYVRSKKLR MVTGLRNIPS IQSRGLFGAI
360 370 380 390 400
AGFIEGGWTG MIDGWYGYHH QNEQGSGYAA DQKSTQNAIN GITNKVNSVI
410 420 430 440 450
EKMNTQFTAV GKEFNKLEKR IENLNKKVDD GFLDIWTYNA ELLVLLENER
460 470 480 490 500
TLDFHDSNVK TLYEKVKNQL KNNAKEIGNG CFEFYHKCNN ECMESVKNGT
510 520 530 540 550
YDYPKYSEES KLNREKIDGV KLESMGVYQI LAIYSTVASS LVLLVSLGAA
560
SFWMCSNGSL QCRICI
Length:566
Mass (Da):63,833
Last modified:May 1, 1999 - v1
Checksum:i2270269582E8969A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085413 mRNA Translation: AAD05215.1

Similar proteinsi

Entry informationi

Entry nameiQ9YTC2_9INFA
AccessioniPrimary (citable) accession number: Q9YTC2
Entry historyiIntegrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: April 25, 2018
This is version 111 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health