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P03437

- HEMA_I68A0

UniProt

P03437 - HEMA_I68A0

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Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Aichi/2/1968 H3N2)
Status
Reviewed - Annotation score: 5 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei345 – 3462Cleavage; by host

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/Aichi/2/1968 H3N2)
Taxonomic identifieri387139 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Cetacea (whales) [TaxID: 9721]
Homo sapiens (Human) [TaxID: 9606]
Phocidae (true seals) [TaxID: 9709]
Sus scrofa (Pig) [TaxID: 9823]

Subcellular locationi

Virion membrane Curated; Single-pass type I membrane protein Curated. 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 530514ExtracellularSequence AnalysisAdd
BLAST
Transmembranei531 – 55121HelicalSequence AnalysisAdd
BLAST
Topological domaini552 – 56615CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
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 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 344328Hemagglutinin HA1 chainPRO_0000038885Add
BLAST
Chaini346 – 566221Hemagglutinin HA2 chainPRO_0000038886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...); by host
Disulfide bondi30 ↔ 482Interchain (between HA1 and HA2 chains)
Glycosylationi38 – 381N-linked (GlcNAc...); by host
Glycosylationi54 – 541N-linked (GlcNAc...); by host
Disulfide bondi68 ↔ 293
Disulfide bondi80 ↔ 92
Glycosylationi97 – 971N-linked (GlcNAc...); by host
Disulfide bondi113 ↔ 155
Glycosylationi181 – 1811N-linked (GlcNAc...); by host
Disulfide bondi297 ↔ 321
Glycosylationi301 – 3011N-linked (GlcNAc...); by host
Disulfide bondi489 ↔ 493
Glycosylationi499 – 4991N-linked (GlcNAc...); by host
Lipidationi555 – 5551S-palmitoyl cysteine; by hostBy similarity
Lipidationi562 – 5621S-palmitoyl cysteine; by hostBy similarity
Lipidationi565 – 5651S-palmitoyl cysteine; by hostBy 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.1 Publication
Palmitoylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HA1-HA2.

Protein-protein interaction databases

DIPiDIP-45342N.
IntActiP03437. 1 interaction.

Structurei

Secondary structure

1
566
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 359Combined sources
Beta strandi40 – 423Combined sources
Beta strandi50 – 534Combined sources
Beta strandi55 – 573Combined sources
Beta strandi65 – 728Combined sources
Beta strandi74 – 763Combined sources
Helixi82 – 876Combined sources
Helixi90 – 956Combined sources
Beta strandi101 – 1055Combined sources
Helixi121 – 13111Combined sources
Beta strandi136 – 1383Combined sources
Turni144 – 1463Combined sources
Beta strandi152 – 1576Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi180 – 1856Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi192 – 2009Combined sources
Helixi204 – 2118Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi217 – 2215Combined sources
Beta strandi226 – 2294Combined sources
Beta strandi245 – 2539Combined sources
Beta strandi258 – 2658Combined sources
Beta strandi267 – 2704Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi296 – 2994Combined sources
Beta strandi302 – 3043Combined sources
Beta strandi307 – 3115Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi331 – 3333Combined sources
Beta strandi337 – 3393Combined sources
Turni352 – 3543Combined sources
Beta strandi366 – 3738Combined sources
Beta strandi376 – 3827Combined sources
Helixi383 – 44967Combined sources
Beta strandi455 – 4573Combined sources
Helixi458 – 47013Combined sources
Helixi472 – 4743Combined sources
Beta strandi475 – 4773Combined sources
Beta strandi479 – 4846Combined sources
Helixi491 – 4999Combined sources
Helixi504 – 51512Combined sources
Turni516 – 5194Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EO8X-ray2.80A17-344[»]
B346-520[»]
1FYTX-ray2.60C322-334[»]
1HA0X-ray2.80A25-518[»]
1HGGX-ray2.90A/C/E17-344[»]
B/D/F346-520[»]
1HTMX-ray2.50A/C/E17-43[»]
B/D/F383-520[»]
1J8HX-ray2.40C322-334[»]
1QU1X-ray1.90A/B/C/D/E/F376-530[»]
2HMGX-ray3.00A/C/E17-344[»]
B/D/F346-520[»]
2VIRX-ray3.25C44-325[»]
2VISX-ray3.25C44-325[»]
2VITX-ray3.25C44-325[»]
2VIUX-ray2.50A17-344[»]
B346-520[»]
2YPGX-ray2.85A/C/E17-344[»]
B/D/F346-520[»]
3EYMX-ray2.80A/C/E25-345[»]
B/D/F346-517[»]
3HMGX-ray2.90A/C/E17-344[»]
B/D/F346-520[»]
3S4SX-ray2.40C/F322-334[»]
3S5LX-ray2.10C/F322-334[»]
3VUNX-ray3.00A/C/E17-345[»]
B/D/F346-520[»]
4C56X-ray2.90F/L322-334[»]
4HMGX-ray3.00A/C/E17-344[»]
B/D/F346-520[»]
5HMGX-ray3.20A/C/E17-344[»]
B/D/F346-520[»]
ProteinModelPortaliP03437.
SMRiP03437. Positions 17-520.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03437.

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.

P03437-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTIIALSYI FCLALGQDLP GNDNSTATLC LGHHAVPNGT LVKTITDDQI
60 70 80 90 100
EVTNATELVQ SSSTGKICNN PHRILDGIDC TLIDALLGDP HCDVFQNETW
110 120 130 140 150
DLFVERSKAF SNCYPYDVPD YASLRSLVAS SGTLEFITEG FTWTGVTQNG
160 170 180 190 200
GSNACKRGPG SGFFSRLNWL TKSGSTYPVL NVTMPNNDNF DKLYIWGIHH
210 220 230 240 250
PSTNQEQTSL YVQASGRVTV STRRSQQTII PNIGSRPWVR GLSSRISIYW
260 270 280 290 300
TIVKPGDVLV INSNGNLIAP RGYFKMRTGK SSIMRSDAPI DTCISECITP
310 320 330 340 350
NGSIPNDKPF QNVNKITYGA CPKYVKQNTL KLATGMRNVP EKQTRGLFGA
360 370 380 390 400
IAGFIENGWE GMIDGWYGFR HQNSEGTGQA ADLKSTQAAI DQINGKLNRV
410 420 430 440 450
IEKTNEKFHQ IEKEFSEVEG RIQDLEKYVE DTKIDLWSYN AELLVALENQ
460 470 480 490 500
HTIDLTDSEM NKLFEKTRRQ LRENAEEMGN GCFKIYHKCD NACIESIRNG
510 520 530 540 550
TYDHDVYRDE ALNNRFQIKG VELKSGYKDW ILWISFAISC FLLCVVLLGF
560
IMWACQRGNI RCNICI
Length:566
Mass (Da):63,416
Last modified:July 21, 1986 - v1
Checksum:iE395659C23CAFECA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141A → P in AAA43239. 1 PublicationCurated
Sequence conflicti15 – 151L → I in BAF37221. (PubMed:15331693)Curated
Sequence conflicti160 – 1601G → S in BAF37221. (PubMed:15331693)Curated
Sequence conflicti198 – 1981I → V in BAF37221. (PubMed:15331693)Curated
Sequence conflicti240 – 2401R → G in BAF37221. (PubMed:15331693)Curated
Sequence conflicti477 – 4771E → D in BAF37221. (PubMed:15331693)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02090 Genomic RNA. Translation: AAA43178.1.
V01085 Genomic RNA. Translation: CAA24269.1.
M55059 Genomic RNA. Translation: AAA43239.1.
AB284320 Genomic RNA. Translation: BAF37221.1.
PIRiA93231. HMIVHA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02090 Genomic RNA. Translation: AAA43178.1 .
V01085 Genomic RNA. Translation: CAA24269.1 .
M55059 Genomic RNA. Translation: AAA43239.1 .
AB284320 Genomic RNA. Translation: BAF37221.1 .
PIRi A93231. HMIVHA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EO8 X-ray 2.80 A 17-344 [» ]
B 346-520 [» ]
1FYT X-ray 2.60 C 322-334 [» ]
1HA0 X-ray 2.80 A 25-518 [» ]
1HGG X-ray 2.90 A/C/E 17-344 [» ]
B/D/F 346-520 [» ]
1HTM X-ray 2.50 A/C/E 17-43 [» ]
B/D/F 383-520 [» ]
1J8H X-ray 2.40 C 322-334 [» ]
1QU1 X-ray 1.90 A/B/C/D/E/F 376-530 [» ]
2HMG X-ray 3.00 A/C/E 17-344 [» ]
B/D/F 346-520 [» ]
2VIR X-ray 3.25 C 44-325 [» ]
2VIS X-ray 3.25 C 44-325 [» ]
2VIT X-ray 3.25 C 44-325 [» ]
2VIU X-ray 2.50 A 17-344 [» ]
B 346-520 [» ]
2YPG X-ray 2.85 A/C/E 17-344 [» ]
B/D/F 346-520 [» ]
3EYM X-ray 2.80 A/C/E 25-345 [» ]
B/D/F 346-517 [» ]
3HMG X-ray 2.90 A/C/E 17-344 [» ]
B/D/F 346-520 [» ]
3S4S X-ray 2.40 C/F 322-334 [» ]
3S5L X-ray 2.10 C/F 322-334 [» ]
3VUN X-ray 3.00 A/C/E 17-345 [» ]
B/D/F 346-520 [» ]
4C56 X-ray 2.90 F/L 322-334 [» ]
4HMG X-ray 3.00 A/C/E 17-344 [» ]
B/D/F 346-520 [» ]
5HMG X-ray 3.20 A/C/E 17-344 [» ]
B/D/F 346-520 [» ]
ProteinModelPortali P03437.
SMRi P03437. Positions 17-520.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-45342N.
IntActi P03437. 1 interaction.

Chemistry

BindingDBi P03437.
ChEMBLi CHEMBL1932897.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P03437.

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. "Antigenic drift between the haemagglutinin of the Hong Kong influenza strains A/Aichi/2/68 and A/Victoria/3/75."
    Verhoeyen M., Fang R., Jou W.M., Devos R., Huylebroeck D., Saman E., Fiers W.
    Nature 286:771-776(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Shift and drift in influenza viruses."
    Min J.W., Verhoeyen M., Fang R.-X., Devos R., Huylebroeck D., Fiers W.
    (In) Carlile M.J., Collins J.F., Moseley B.E.B. (eds.); Symposium of the Society for General Microbiology, pp.285-311, Cambridge University Press, New York (1981)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin."
    Abe Y., Takashita E., Sugawara K., Matsuzaki Y., Muraki Y., Hongo S.
    J. Virol. 78:9605-9611(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  4. "Human mucus protease inhibitor in airway fluids is a potential defensive compound against infection with influenza A and Sendai viruses."
    Beppu Y., Imamura Y., Tashiro M., Towatari T., Ariga H., Kido H.
    J. Biochem. 121:309-316(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE.
  5. "Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3-A resolution."
    Wilson I.A., Skehel J.J., Wiley D.C.
    Nature 289:366-373(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  6. "Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid."
    Weis W.I., Brown J.H., Cusack S.C., Paulson J.C., Skehel J.J., Wiley D.C.
    Nature 333:426-431(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
  7. "The structure of a membrane fusion mutant of the influenza virus haemagglutinin."
    Weis W.I., Cusack S.C., Brown J.H., Daniels R.S., Skehel J.J., Wiley D.C.
    EMBO J. 9:17-24(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF A MUTANT WITH GLY-457.
  8. "Refinement of the influenza virus hemagglutinin by simulated annealing."
    Weis W.I., Bruenger A.T., Skehel J.J., Wiley D.C.
    J. Mol. Biol. 212:737-761(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
  9. "Structure of influenza haemagglutinin at the pH of membrane fusion."
    Bullough P.A., Hughson F.M., Skehel J.J., Wiley D.C.
    Nature 371:37-43(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  10. "Antigen distortion allows influenza virus to escape neutralization."
    Fleury D., Wharton S.A., Skehel J.J., Knossow M., Bizebard T.
    Nat. Struct. Biol. 5:119-123(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS).

Entry informationi

Entry nameiHEMA_I68A0
AccessioniPrimary (citable) accession number: P03437
Secondary accession number(s): A0PC85, Q67132
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 123 of the entry and version 1 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.

Keywords - Technical termi

3D-structure

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