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Q9WFX3

- HEMA_I18A0

UniProt

Q9WFX3 - HEMA_I18A0

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Protein
Hemagglutinin
Gene
HA
Organism
Influenza A virus (strain A/Brevig Mission/1/1918 H1N1) (Influenza A virus (strain A/South Carolina/1/1918 H1N1))
Status
Reviewed - Annotation score: 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei344 – 3452Cleavage; by host By similarity

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

Hemagglutinin

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Hemagglutinin
Cleaved into the following 2 chains:
Gene namesi
Name:HA
OrganismiInfluenza A virus (strain A/Brevig Mission/1/1918 H1N1) (Influenza A virus (strain A/South Carolina/1/1918 H1N1))
Taxonomic identifieri88776 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000008430: Genome

Subcellular locationi

Virion membrane; Single-pass type I membrane protein Reviewed prediction. Host apical cell membrane; Single-pass type I membrane protein
Note: Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 529512Extracellular Reviewed prediction
Add
BLAST
Transmembranei530 – 55021Helical; Reviewed prediction
Add
BLAST
Topological domaini551 – 56616Cytoplasmic Reviewed prediction
Add
BLAST

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 membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 343326Hemagglutinin HA1 chain
PRO_0000310563Add
BLAST
Chaini345 – 566222Hemagglutinin HA2 chain
PRO_0000310564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 481Interchain (between HA1 and HA2 chains) By similarity
Glycosylationi27 – 271N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi28 – 281N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi40 – 401N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi59 ↔ 292 By similarity
Disulfide bondi72 ↔ 84 By similarity
Glycosylationi104 – 1041N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi107 ↔ 153 By similarity
Disulfide bondi296 ↔ 320 By similarity
Glycosylationi304 – 3041N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi488 ↔ 492 By similarity
Glycosylationi498 – 4981N-linked (GlcNAc...); by host Reviewed prediction
Lipidationi555 – 5551S-palmitoyl cysteine; by host By similarity
Lipidationi562 – 5621S-palmitoyl cysteine; by host By similarity
Lipidationi565 – 5651S-palmitoyl cysteine; by host By similarity

Post-translational modificationi

In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in lungs by Clara cells By similarity.
Palmitoylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HA1-HA2 By similarity.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 258
Beta strandi31 – 333
Beta strandi39 – 446
Beta strandi46 – 483
Beta strandi56 – 616
Beta strandi67 – 704
Helixi74 – 796
Helixi82 – 876
Beta strandi94 – 985
Beta strandi108 – 1103
Helixi115 – 1228
Beta strandi125 – 13410
Turni136 – 1383
Beta strandi143 – 1475
Beta strandi150 – 1556
Beta strandi158 – 1603
Beta strandi163 – 1675
Beta strandi171 – 1733
Beta strandi178 – 1836
Beta strandi186 – 1883
Beta strandi190 – 1989
Helixi202 – 2098
Beta strandi216 – 2194
Beta strandi224 – 2274
Beta strandi237 – 2393
Beta strandi240 – 25112
Beta strandi256 – 2638
Beta strandi265 – 2684
Beta strandi270 – 2767
Beta strandi282 – 2843
Beta strandi289 – 2979
Beta strandi301 – 3033
Beta strandi308 – 3103
Beta strandi316 – 3205
Beta strandi330 – 3323
Beta strandi336 – 3383
Turni341 – 3466
Turni351 – 3533
Beta strandi358 – 3603
Beta strandi365 – 3728
Beta strandi375 – 3806
Helixi382 – 40221
Beta strandi406 – 4094
Helixi416 – 4183
Helixi419 – 47052
Helixi471 – 4733
Beta strandi474 – 4763
Beta strandi478 – 4869
Helixi490 – 4978
Helixi503 – 51311

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RD8X-ray3.00A/C/E18-344[»]
B/D/F345-520[»]
1RUZX-ray2.90H/J/L14-339[»]
I/K/M345-504[»]
2WRGX-ray3.00H/J/L18-343[»]
I/K/M345-566[»]
3GBNX-ray2.20A18-344[»]
B345-520[»]
3LZFX-ray2.80A18-344[»]
B345-520[»]
3R2XX-ray3.10A18-344[»]
B345-520[»]
4EEFX-ray2.70A/C/E18-344[»]
B/D/F345-520[»]
4GXUX-ray3.29A/C/E/G/I/K18-344[»]
B/D/F/H/J/L345-520[»]
4GXXX-ray1.80A/C/E18-344[»]
B/D/F345-520[»]
4JUGX-ray2.70A/C/E/G/I/K18-339[»]
B/D/F/H/J/L345-514[»]
4JUHX-ray2.80A/C/E18-339[»]
B/D/F345-514[»]
4JUJX-ray3.01A/C/E18-339[»]
B/D/F345-514[»]
4PY8X-ray2.91A18-344[»]
B345-520[»]
ProteinModelPortaliQ9WFX3.
SMRiQ9WFX3. Positions 18-519.

Miscellaneous databases

EvolutionaryTraceiQ9WFX3.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WFX3-1 [UniParc]FASTAAdd to Basket

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MEARLLVLLC AFAATNADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL    50
EDSHNGKLCK LKGIAPLQLG KCNIAGWLLG NPECDLLLTA SSWSYIVETS 100
NSENGTCYPG DFIDYEELRE QLSSVSSFEK FEIFPKTSSW PNHETTKGVT 150
AACSYAGASS FYRNLLWLTK KGSSYPKLSK SYVNNKGKEV LVLWGVHHPP 200
TGTDQQSLYQ NADAYVSVGS SKYNRRFTPE IAARPKVRDQ AGRMNYYWTL 250
LEPGDTITFE ATGNLIAPWY AFALNRGSGS GIITSDAPVH DCNTKCQTPH 300
GAINSSLPFQ NIHPVTIGEC PKYVRSTKLR MATGLRNIPS IQSRGLFGAI 350
AGFIEGGWTG MIDGWYGYHH QNEQGSGYAA DQKSTQNAID GITNKVNSVI 400
EKMNTQFTAV GKEFNNLERR IENLNKKVDD GFLDIWTYNA ELLVLLENER 450
TLDFHDSNVR NLYEKVKSQL KNNAKEIGNG CFEFYHKCDD ACMESVRNGT 500
YDYPKYSEES KLNREEIDGV KLESMGVYQI LAIYSTVASS LVLLVSLGAI 550
SFWMCSNGSL QCRICI 566
Length:566
Mass (Da):62,866
Last modified:November 13, 2007 - v2
Checksum:i5A292C3386E0F96B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF117241 Genomic RNA. Translation: AAD17229.1.
AF116575 mRNA. Translation: AAD17218.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF117241 Genomic RNA. Translation: AAD17229.1 .
AF116575 mRNA. Translation: AAD17218.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RD8 X-ray 3.00 A/C/E 18-344 [» ]
B/D/F 345-520 [» ]
1RUZ X-ray 2.90 H/J/L 14-339 [» ]
I/K/M 345-504 [» ]
2WRG X-ray 3.00 H/J/L 18-343 [» ]
I/K/M 345-566 [» ]
3GBN X-ray 2.20 A 18-344 [» ]
B 345-520 [» ]
3LZF X-ray 2.80 A 18-344 [» ]
B 345-520 [» ]
3R2X X-ray 3.10 A 18-344 [» ]
B 345-520 [» ]
4EEF X-ray 2.70 A/C/E 18-344 [» ]
B/D/F 345-520 [» ]
4GXU X-ray 3.29 A/C/E/G/I/K 18-344 [» ]
B/D/F/H/J/L 345-520 [» ]
4GXX X-ray 1.80 A/C/E 18-344 [» ]
B/D/F 345-520 [» ]
4JUG X-ray 2.70 A/C/E/G/I/K 18-339 [» ]
B/D/F/H/J/L 345-514 [» ]
4JUH X-ray 2.80 A/C/E 18-339 [» ]
B/D/F 345-514 [» ]
4JUJ X-ray 3.01 A/C/E 18-339 [» ]
B/D/F 345-514 [» ]
4PY8 X-ray 2.91 A 18-344 [» ]
B 345-520 [» ]
ProteinModelPortali Q9WFX3.
SMRi Q9WFX3. Positions 18-519.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q9WFX3.

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. "Initial genetic characterization of the 1918 'Spanish' influenza virus."
    Taubenberger J.K., Reid A.H., Krafft A.E., Bijwaard K.E., Fanning T.G.
    Science 275:1793-1796(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: A/South Carolina/1/1918.
  2. "Origin and evolution of the 1918 'Spanish' influenza virus hemagglutinin gene."
    Reid A.H., Fanning T.G., Hultin J.V., Taubenberger J.K.
    Proc. Natl. Acad. Sci. U.S.A. 96:1651-1656(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], NUCLEOTIDE SEQUENCE [MRNA] OF 1-406.
    Strain: A/South Carolina/1/1918.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 14-339.
    Strain: A/South Carolina/1/1918.
  4. "Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus."
    Stevens J., Corper A.L., Basler C.F., Taubenberger J.K., Palese P., Wilson I.A.
    Science 303:1866-1870(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-344.
    Strain: A/South Carolina/1/1918.

Entry informationi

Entry nameiHEMA_I18A0
AccessioniPrimary (citable) accession number: Q9WFX3
Secondary accession number(s): O10424
, O10425, O10426, Q9WFZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Major glycoprotein, comprises over 80% of the envelope proteins present in virus particle.
The extent of infection into host organism is determined by HA. Influenza viruses bud from the apical surface of polarized epithelial cells (e.g. bronchial epithelial cells) into lumen of lungs and are therefore usually pneumotropic. The reason is that HA is cleaved by tryptase clara which is restricted to lungs. However, HAs of H5 and H7 pantropic avian viruses subtypes can be cleaved by furin and subtilisin-type enzymes, allowing the virus to grow in other organs than lungs.
The influenza A genome consist of 8 RNA segments. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains. The mechanism of variation can be the result of point mutations or the result of genetic reassortment between segments of two different strains.
South Carolina isolate has been sequenced from formalid fixed-lung tissues of a 21-year-old male which died in 1918 at Ft. Jackson, SC. Brevig Mission isolate has been sequenced from lung tissues of an Inuit woman buried in the permafrost in a gravesite near Brevig Mission, Alaska. This sample was recovered by John Hultin, retired pathologist.

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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