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H6QM93 (H6QM93_9INFA) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 14. 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·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. RuleBase RU003324 SAAS SAAS000149

Subunit structure

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

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
   DomainSignal EMBL AFC35438.1
Transmembrane
Transmembrane helix SAAS SAAS000149
   Molecular functionHemagglutinin RuleBase RU003324 SAAS SAAS000149
   PTMDisulfide bond SAAS SAAS000149
   Technical term3D-structure PDB 4I78 PDB 4H32
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential EMBL AFC35438.1
Chain19 – 564546 Potential EMBL AFC35438.1
PRO_5000868406
Chain19 – 342324HA1 EMBL AFC35438.1
PRO_5000868407
Chain343 – 564222HA2 EMBL AFC35438.1
PRO_5000868408

Amino acid modifications

Glycosylation311N-linked (GlcNAc...)
Glycosylation1281N-linked (GlcNAc...) PDB 4I78 PDB 4H32

Sequences

Sequence LengthMass (Da)Tools
H6QM93 [UniParc].

Last modified April 18, 2012. Version 1.
Checksum: E71DFB048B81F12F

FASTA56463,584
        10         20         30         40         50         60 
MELIILLILL NPYTFVLGDR ICIGYQANQN NQTVNTLLEQ NVPVTGAQEI LETNHNGKLC 

        70         80         90        100        110        120 
SLNGVPPLDL QSCTLAGWLL GNPNCDNLLE AEEWSYIKIN ENAPDDLCFP GNFENLQDLL 

       130        140        150        160        170        180 
LEMSGVQNFT KVKLFNPQSM TGVTTNNVDQ TCPFEGKPSF YRNLNWIQGN SGLPFNIEIK 

       190        200        210        220        230        240 
NPTSNPLLLL WGIHNTKDAA QQRNLYGNDY SYTIFNFGEK SEEFRPDIGQ RDEIKAHQDR 

       250        260        270        280        290        300 
IDYYWGSLPA QSTLRIESTG NLIAPEYGFY YKRKEGKGGL MKSKLPISDC STKCQTPLGA 

       310        320        330        340        350        360 
LNSTLPFQNV HQQTIGNCPK YVKATSLMLA TGLRNNPQME GRGLFGAIAG FIEGGWQGMI 

       370        380        390        400        410        420 
DGWYGYHHEN QEGSGYAADK EATQKAVDAI TNKVNSIIDK MNSQFESNIK EFNRLELRIQ 

       430        440        450        460        470        480 
HLSDRVDDAL LDIWSYNTEL LVLLENERTL DFHDANVKNL FEKVKAQLKD NAIDEGNGCF 

       490        500        510        520        530        540 
LLLHKCNNSC MDDIKNGTYK YMDYREESHI EKQKIDGVKL TDYSRYYTMT LYSTIASSVV 

       550        560 
LGSLIIAAFL WGCQKGSIQC KICI 

« Hide

References

[1]"A distinct lineage of influenza A virus from bats."
Tong S., Li Y., Rivailler P., Conrardy C., Alvarez Castillo D.A., Chen L.-M., Recuenco S., Ellison J.A., Davis C.T., York I.A., Turmelle A.S., Moran D., Rogers S., Shi M., Tao Y., Weil M.R., Tang K., Rowe L.A. expand/collapse author list , Sammons S., Xu X., Frace M., Lindblade K.A., Cox N.J., Anderson L.J., Rupprecht C., Donis R.O.
Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2012)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/little yellow-shouldered bat/Guatemala/060/2010 EMBL AFC35438.1.
[2]"Bat-derived influenza hemagglutinin H17 does not bind canonical avian or human receptors and most likely uses a unique entry mechanism."
Sun X., Shi Y., Lu X., He J., Gao F., Yan J., Qi J., Gao G.F.
Cell Rep. 3:769-778(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 19-337 AND 349-518, GLYCOSYLATION AT ASN-31 AND ASN-128.
[3]"Hemagglutinin homologue from H17N10 bat influenza virus exhibits divergent receptor-binding and pH-dependent fusion activities."
Zhu X., Yu W., McBride R., Li Y., Chen L.M., Donis R.O., Tong S., Paulson J.C., Wilson I.A.
Proc. Natl. Acad. Sci. U.S.A. 110:1458-1463(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.18 ANGSTROMS) OF 18-342 AND 343-516, GLYCOSYLATION AT ASN-128.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CY103892 Viral cRNA. Translation: AFC35438.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4H32X-ray2.70A/C/E/G/I/K19-337[»]
B/D/F/H/J/L349-518[»]
4I78X-ray3.18A/B18-342[»]
C/D343-516[»]
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...

Entry information

Entry nameH6QM93_9INFA
AccessionPrimary (citable) accession number: H6QM93
Entry history
Integrated into UniProtKB/TrEMBL: April 18, 2012
Last sequence update: April 18, 2012
Last modified: February 19, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)