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Q91IJ0

- Q91IJ0_9INFA

UniProt

Q91IJ0 - Q91IJ0_9INFA

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Protein
Submitted name: Hemagglutinin
Gene
N/A
Organism
Influenza A virus (A/Hong Kong/1035/1998(H1N1))
Status
Unreviewed - 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 By similarity.UniRule annotationSAAS annotations

GO - Biological processi

  1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  3. fusion of virus membrane with host plasma membrane Source: InterPro
  4. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

HemagglutininUniRule annotationSAAS annotations

Keywords - Biological processi

Clathrin- and caveolin-independent endocytosis of virus by hostSAAS annotations, Clathrin-mediated endocytosis of virus by hostSAAS annotations, Fusion of virus membrane with host endosomal membraneSAAS annotations, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cellSAAS annotations, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Submitted name:
HemagglutininImported
OrganismiInfluenza A virus (A/Hong Kong/1035/1998(H1N1))Imported
Taxonomic identifieri164325 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A

Subcellular locationi

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
  4. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membraneSAAS annotations, Host membrane, Membrane, Viral envelope proteinUniRule annotationSAAS annotations, Virion

PTM / Processingi

Keywords - PTMi

Disulfide bondSAAS annotations

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HA1-HA2 By similarity.UniRule annotationSAAS annotations

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LWANMR-A/B/C344-366[»]
ProteinModelPortaliQ91IJ0.
SMRiQ91IJ0. Positions 18-339, 344-518.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helixSAAS annotations

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

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MKAKLLVLLC TFTATYADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL    50
EDRHNGKLCL LKGIAPLQLG NCSVAGWILG NPECELLISK ESWSYIVETP 100
NPENGTCYPG YFADYEELRE QLSSVSSFER FEIFPKESSW PNHTVTGVSA 150
SCSHNGKSSF YRNLLWLTEK NGLYPNLSKS YVNNKEKEVL VLWGVHNPSN 200
IGDQRAIYHT ENAYVSVVSS HYSRRFTPEI AKRPKVRDQE GRINYYWTLL 250
EPGDTIIFEA NGNLIAPWYA FALSRGFGSG IITSNAPMDE CDAKCQTPQG 300
AINSSLPFQN VHPVTIGECP KYVRSAKLRM VTGLRNIPSI QSRGLFGAIA 350
GFIEGGWTGM IDGWYGYHHQ NEQGSGYAAD QKSTQNAING ITNKVNSVIE 400
KMNTQFTAVG KEFNKLERRM ENLNKKVDDG FLDIWTYNAE LLVLLENERT 450
LDFHDSNVKN LYEKVKSQLK NNAKEIGNGC FEFYHKCNNE CMESVKNGTY 500
DYPKYSEESK LNREKIDGVK LESMGVYQIL AIYSTVASSL VLLVSLGAIS 550
FWMCSNGSLQ CRICI 565
Length:565
Mass (Da):63,392
Last modified:December 1, 2001 - v1
Checksum:iC4870EDBCEEAA3CF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF386777 Genomic RNA. Translation: AAK70453.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF386777 Genomic RNA. Translation: AAK70453.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LWA NMR - A/B/C 344-366 [» ]
ProteinModelPortali Q91IJ0.
SMRi Q91IJ0. Positions 18-339, 344-518.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.10.77.10. 1 hit.
3.90.20.10. 1 hit.
3.90.209.20. 1 hit.
InterProi IPR008980. 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 ]
Pfami PF00509. Hemagglutinin. 1 hit.
[Graphical view ]
PRINTSi PR00330. HEMAGGLUTN1.
PR00329. HEMAGGLUTN12.
SUPFAMi SSF49818. SSF49818. 1 hit.
ProtoNeti Search...

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: February 19, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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