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Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (A/Viet Nam/1203/2004(H5N1))
Status
Unreviewed-Annotation score: Annotation score: 3 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).SAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei237 – 2371Galactose; via carbonyl oxygenCombined sources

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
Gene namesi
Name:HAImported
OrganismiInfluenza A virus (A/Viet Nam/1203/2004(H5N1))Imported
Taxonomic identifieri284218 [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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi20 ↔ 483Interchain (with C-483 in Q5EP31)Combined sources
Glycosylationi27 – 271N-linked (GlcNAc...)Combined sources
Glycosylationi39 – 391N-linked (GlcNAc...)Combined sources
Disulfide bondi58 ↔ 290Combined sources
Disulfide bondi71 ↔ 83Combined sources
Disulfide bondi106 ↔ 151Combined sources
Glycosylationi181 – 1811N-linked (GlcNAc...)Combined sources
Disulfide bondi294 ↔ 318Combined sources
Disulfide bondi490 ↔ 494Combined sources

Keywords - PTMi

Disulfide bondSAAS annotation

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HA1-HA2.UniRule annotationSAAS annotation

Protein-protein interaction databases

DIPiDIP-60227N.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BH2X-ray2.12A17-340[»]
B347-513[»]
4BH3X-ray2.00A17-340[»]
B347-513[»]
4BH4X-ray1.90A17-340[»]
B347-513[»]
4N5ZX-ray2.95A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c17-346[»]
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.

Q5EP31-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKIVLLFAI VSLVKSDQIC IGYHANNSTE QVDTIMEKNV TVTHAQDILE
60 70 80 90 100
KKHNGKLCDL DGVKPLILRD CSVAGWLLGN PMCDEFINVP EWSYIVEKAN
110 120 130 140 150
PVNDLCYPGD FNDYEELKHL LSRINHFEKI QIIPKSSWSS HEASLGVSSA
160 170 180 190 200
CPYQGKSSFF RNVVWLIKKN STYPTIKRSY NNTNQEDLLV LWGIHHPNDA
210 220 230 240 250
AEQTKLYQNP TTYISVGTST LNQRLVPRIA TRSKVNGQSG RMEFFWTILK
260 270 280 290 300
PNDAINFESN GNFIAPEYAY KIVKKGDSTI MKSELEYGNC NTKCQTPMGA
310 320 330 340 350
INSSMPFHNI HPLTIGECPK YVKSNRLVLA TGLRNSPQRE RRRKKRGLFG
360 370 380 390 400
AIAGFIEGGW QGMVDGWYGY HHSNEQGSGY AADKESTQKA IDGVTNKVNS
410 420 430 440 450
IIDKMNTQFE AVGREFNNLE RRIENLNKKM EDGFLDVWTY NAELLVLMEN
460 470 480 490 500
ERTLDFHDSN VKNLYDKVRL QLRDNAKELG NGCFEFYHKC DNECMESVRN
510 520 530 540 550
GTYDYPQYSE EARLKREEIS GVKLESIGIY QILSIYSTVA SSLALAIMVA
560
GLSLWMCSNG SLQCRICI
Length:568
Mass (Da):64,461
Last modified:March 15, 2005 - v1
Checksum:i1987CB02AB9C06CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY818135 Genomic RNA. Translation: AAW80717.1.
EF541403 Viral cRNA. Translation: ABP51977.1.
HM006759 Viral cRNA. Translation: ADD97095.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY818135 Genomic RNA. Translation: AAW80717.1.
EF541403 Viral cRNA. Translation: ABP51977.1.
HM006759 Viral cRNA. Translation: ADD97095.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BH2X-ray2.12A17-340[»]
B347-513[»]
4BH3X-ray2.00A17-340[»]
B347-513[»]
4BH4X-ray1.90A17-340[»]
B347-513[»]
4N5ZX-ray2.95A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c17-346[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60227N.

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. "Evolution of H5N1 avian influenza viruses in Asia."
    World Health Organization Global Influenza Program Surveillance Network
    Emerg. Infect. Dis. 11:1515-1521(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Viet Nam/1203/2004Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Viet Nam/1203/2004Imported.
  3. Smith C.
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Viet Nam/1203/2004Imported.
  4. "Acquisition of virulence mutations in avian H5N1 influenza virus during a single passage in ferrets."
    Butler J., Middleton D., Klippel J., Rockman S., Brown L., Sapats S.
    Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Viet Nam/1203/2004Imported.
  5. "Receptor binding by a ferret-transmissible H5 avian influenza virus."
    Xiong X., Coombs P.J., Martin S.R., Liu J., Xiao H., McCauley J.W., Locher K., Walker P.A., Collins P.J., Kawaoka Y., Skehel J.J., Gamblin S.J.
    Nature 497:392-396(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 17-340 AND 347-513 IN COMPLEX WITH GALACTOSE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-27; ASN-39 AND ASN-181.
  6. "Hemagglutinin receptor specificity and structural analyses of respiratory droplet-transmissible H5N1 viruses."
    de Vries R.P., Zhu X., McBride R., Rigter A., Hanson A., Zhong G., Hatta M., Xu R., Yu W., Kawaoka Y., de Haan C.A., Wilson I.A., Paulson J.C.
    J. Virol. 88:768-773(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 17-346, DISULFIDE BONDS, GLYCOSYLATION AT ASN-39 AND ASN-181.

Entry informationi

Entry nameiQ5EP31_9INFA
AccessioniPrimary (citable) accession number: Q5EP31
Entry historyi
Integrated into UniProtKB/TrEMBL: March 15, 2005
Last sequence update: March 15, 2005
Last modified: June 24, 2015
This is version 78 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.