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Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Japan/305/1957 H2N2)
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 (strain A/Japan/305/1957 H2N2)Imported
Taxonomic identifieri387161 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000207860 Componenti: Genome

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
Transmembranei527 – 550HelicalUniRule annotationAdd BLAST24

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 bondi19Interchain (with C-477)Combined sources
Glycosylationi26N-linked (GlcNAc...)Combined sources1
Glycosylationi38N-linked (GlcNAc...)Combined sources1
Disulfide bondi57 ↔ 288Combined sources
Disulfide bondi70 ↔ 82UniRule annotationCombined sources
Disulfide bondi105 ↔ 149Combined sources
Glycosylationi179N-linked (GlcNAc...)Combined sources1
Disulfide bondi292 ↔ 316UniRule annotationCombined sources
Glycosylationi300N-linked (GlcNAc...)Combined sources1
Disulfide bondi477Interchain (with C-19)Combined sources
Disulfide bondi484 ↔ 488UniRule annotationCombined sources
Glycosylationi494N-linked (GlcNAc...)Combined sources1
Lipidationi551S-palmitoyl cysteine; by hostUniRule annotation1
Lipidationi558S-palmitoyl cysteine; by hostUniRule annotation1
Lipidationi561S-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
Sitei340 – 341Cleavage; 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
3KU3X-ray1.60A15-340[»]
B341-514[»]
3KU5X-ray1.73A15-340[»]
B341-514[»]
3KU6X-ray1.75A15-340[»]
B341-514[»]
3QQBX-ray1.97A15-340[»]
B341-514[»]
3QQEX-ray2.10A15-340[»]
B341-514[»]
3QQIX-ray1.65A/B61-279[»]
3QQOX-ray2.90A/C/E15-340[»]
B/D/F341-514[»]
4HF5X-ray3.00A15-340[»]
B341-514[»]
4HLZX-ray2.90A/C/E15-340[»]
B/D/F341-514[»]
SMRiC7S226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiC7S226.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili396 – 430Sequence 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.

C7S226-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIIYLILLF TAVRGDQICI GYHANNSTEK VDTILERNVT VTHAKDILEK
60 70 80 90 100
THNGKLCKLN GIPPLELGDC SIAGWLLGNP ECDRLLSVPE WSYIMEKENP
110 120 130 140 150
RDGLCYPGSF NDYEELKHLL SSVKHFEKVK ILPKDRWTQH TTTGGSRACA
160 170 180 190 200
VSGNPSFFRN MVWLTEKGSN YPVAKGSYNN TSGEQMLIIW GVHHPNDETE
210 220 230 240 250
QRTLYQNVGT YVSVGTSTLN KRSTPEIATR PKVNGQGGRM EFSWTLLDMW
260 270 280 290 300
DTINFESTGN LIAPEYGFKI SKRGSSGIMK TEGTLENCET KCQTPLGAIN
310 320 330 340 350
TTLPFHNVHP LTIGECPKYV KSEKLVLATG LRNVPQIESR GLFGAIAGFI
360 370 380 390 400
EGGWQGMVDG WYGYHHSNDQ GSGYAADKES TQKAFDGITN KVNSVIEKMN
410 420 430 440 450
TQFEAVGKEF SNLERRLENL NKKMEDGFLD VWTYNAELLV LMENERTLDF
460 470 480 490 500
HDSNVKNLYD KVRMQLRDNV KELGNGCFEF YHKCDDECMN SVKNGTYDYP
510 520 530 540 550
KYEEESKLNR NEIKGVKLSS MGVYQILAIY ATVAGSLSLA IMMAGISFWM
560
CSNGSLQCRI CI
Length:562
Mass (Da):63,120
Last modified:October 13, 2009 - v1
Checksum:iD4747A6A6733E733
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CY045804 Viral cRNA. Translation: ACV49600.1.

Similar proteinsi

Entry informationi

Entry nameiC7S226_I57A0
AccessioniPrimary (citable) accession number: C7S226
Entry historyiIntegrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: January 31, 2018
This is version 71 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, Complete proteomeImported