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Protein

Hemagglutinin

Gene
N/A
Organism
Influenza A virus (A/Hong Kong/1035/1998(H1N1))
Status
Unreviewed-Annotation score: Annotation score: 2 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
OrganismiInfluenza A virus (A/Hong Kong/1035/1998(H1N1))Imported
Taxonomic identifieri164325 [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

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
2LWANMR-A/B/C344-366[»]
ProteinModelPortaliQ91IJ0.
SMRiQ91IJ0. Positions 18-339, 344-518.
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.

Q91IJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAKLLVLLC TFTATYADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL
60 70 80 90 100
EDRHNGKLCL LKGIAPLQLG NCSVAGWILG NPECELLISK ESWSYIVETP
110 120 130 140 150
NPENGTCYPG YFADYEELRE QLSSVSSFER FEIFPKESSW PNHTVTGVSA
160 170 180 190 200
SCSHNGKSSF YRNLLWLTEK NGLYPNLSKS YVNNKEKEVL VLWGVHNPSN
210 220 230 240 250
IGDQRAIYHT ENAYVSVVSS HYSRRFTPEI AKRPKVRDQE GRINYYWTLL
260 270 280 290 300
EPGDTIIFEA NGNLIAPWYA FALSRGFGSG IITSNAPMDE CDAKCQTPQG
310 320 330 340 350
AINSSLPFQN VHPVTIGECP KYVRSAKLRM VTGLRNIPSI QSRGLFGAIA
360 370 380 390 400
GFIEGGWTGM IDGWYGYHHQ NEQGSGYAAD QKSTQNAING ITNKVNSVIE
410 420 430 440 450
KMNTQFTAVG KEFNKLERRM ENLNKKVDDG FLDIWTYNAE LLVLLENERT
460 470 480 490 500
LDFHDSNVKN LYEKVKSQLK NNAKEIGNGC FEFYHKCNNE CMESVKNGTY
510 520 530 540 550
DYPKYSEESK LNREKIDGVK LESMGVYQIL AIYSTVASSL VLLVSLGAIS
560
FWMCSNGSLQ CRICI
Length:565
Mass (Da):63,392
Last modified:December 1, 2001 - v1
Checksum:iC4870EDBCEEAA3CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF386777 Genomic RNA. Translation: AAK70453.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF386777 Genomic RNA. Translation: AAK70453.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LWANMR-A/B/C344-366[»]
ProteinModelPortaliQ91IJ0.
SMRiQ91IJ0. Positions 18-339, 344-518.
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. "Distinct host range of influenza H3N2 virus isolates in Vero and MDCK cells is determined by cell specific glycosylation pattern."
    Romanova J., Katinger D., Ferko B., Voglauer R., Mochalova L., Bovin N., Lim W., Katinger H., Egorov A.
    Virology 307:90-97(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Hong Kong/1035/98Imported.
  2. "pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR."
    Lorieau J.L., Louis J.M., Schwieters C.D., Bax A.
    Proc. Natl. Acad. Sci. U.S.A. 109:19994-19999(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 344-366.

Entry informationi

Entry nameiQ91IJ0_9INFA
AccessioniPrimary (citable) accession number: Q91IJ0
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: July 22, 2015
This is version 81 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.