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Q9YTC2 (Q9YTC2_9INFA) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 SAAS000149 RuleBase RU003324

Subunit structure

Homotrimer of disulfide-linked HA1-HA2 By similarity. SAAS SAAS000149 RuleBase RU003324

Subcellular location

Virion membrane; Single-pass type I membrane protein. Host apical cell membrane; Single-pass type I membrane protein By similarity SAAS SAAS000149.

Sequence similarities

Belongs to the influenza viruses hemagglutinin family. RuleBase RU003324

Ontologies

Keywords
   Biological processClathrin- and caveolin-independent endocytosis of virus by host SAAS SAAS000149
Clathrin-mediated endocytosis of virus by host SAAS SAAS000149
Fusion of virus membrane with host endosomal membrane SAAS SAAS000149
Fusion of virus membrane with host membrane
Host-virus interaction
Viral attachment to host cell SAAS SAAS000149
Viral penetration into host cytoplasm
Virus endocytosis by host
Virus entry into host cell
   Cellular componentHost cell membrane SAAS SAAS000149
Host membrane
Membrane
Viral envelope protein RuleBase RU003324 SAAS SAAS000149
Virion
   DomainTransmembrane
Transmembrane helix SAAS SAAS000149
   Molecular functionHemagglutinin SAAS SAAS000149 RuleBase RU003324
   PTMDisulfide bond SAAS SAAS000149
   Technical term3D-structure PDB 2KXA
Gene Ontology (GO)
   Biological_processclathrin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host endosome membrane

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host plasma membrane

Inferred from electronic annotation. Source: InterPro

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q9YTC2 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 2270269582E8969A

FASTA56663,833
        10         20         30         40         50         60 
MKEKLLVLLC ALSATDADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDSHNGKLCR 

        70         80         90        100        110        120 
LKGIAPLQLG KCSIAGWILG NPECELLFSK KSWSYIAETP NSENGICYPG YFSDYEELRE 

       130        140        150        160        170        180 
QLSSVSSFER FEIFPKESSW PKHSVNKGVT KSCSHKGKSS FYRNLLWLTE KNGSYPNLSK 

       190        200        210        220        230        240 
SYVNNKEKEV LVLWGVHHPS NIENQKTIYR KETAYVSVVS SHYNRRFTPE ITRRPKVRDQ 

       250        260        270        280        290        300 
EGRINYYWTL LEPGDTIIFE ANGNLIAPWY RFALSRGFGS GIIISNASMD ECDAKCQTPQ 

       310        320        330        340        350        360 
GAINSSLPFQ NVHPVTIGEC PKYVRSKKLR MVTGLRNIPS IQSRGLFGAI AGFIEGGWTG 

       370        380        390        400        410        420 
MIDGWYGYHH QNEQGSGYAA DQKSTQNAIN GITNKVNSVI EKMNTQFTAV GKEFNKLEKR 

       430        440        450        460        470        480 
IENLNKKVDD GFLDIWTYNA ELLVLLENER TLDFHDSNVK TLYEKVKNQL KNNAKEIGNG 

       490        500        510        520        530        540 
CFEFYHKCNN ECMESVKNGT YDYPKYSEES KLNREKIDGV KLESMGVYQI LAIYSTVASS 

       550        560 
LVLLVSLGAA SFWMCSNGSL QCRICI 

« Hide

References

[1]Brown I.H.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/swine/Scotland/410440/94 EMBL AAD05215.1.
[2]"The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface."
Lorieau J.L., Louis J.M., Bax A.
Proc. Natl. Acad. Sci. U.S.A. 107:11341-11346(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 345-367.
[3]"Multiple genetic reassortment of avian and human influenza A viruses in European pigs, resulting in the emergence of an H1N2 virus of novel genotype."
Brown I.H., Harris P.A., McCauley J.W., Alexander D.J.
J. Gen. Virol. 79:0-0(0001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/swine/Scotland/410440/94 EMBL AAD05215.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF085413 mRNA. Translation: AAD05215.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KXANMR-A345-367[»]
ProteinModelPortalQ9YTC2.
SMRQ9YTC2. Positions 18-340, 345-519.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.10.77.10. 1 hit.
3.90.20.10. 1 hit.
3.90.209.20. 1 hit.
InterProIPR008980. 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]
PfamPF00509. Hemagglutinin. 1 hit.
[Graphical view]
PRINTSPR00330. HEMAGGLUTN1.
PR00329. HEMAGGLUTN12.
SUPFAMSSF49818. SSF49818. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9YTC2.

Entry information

Entry nameQ9YTC2_9INFA
AccessionPrimary (citable) accession number: Q9YTC2
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)