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P03452

- HEMA_I34A1

UniProt

P03452 - HEMA_I34A1

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Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
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
Sitei343 – 3442Cleavage; by hostBy 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: Reactome
  4. intracellular transport of viral protein in host cell Source: Reactome
  5. receptor-mediated endocytosis of virus by host cell Source: Reactome
  6. uncoating of virus Source: Reactome
  7. viral entry into host cell Source: Reactome
  8. viral genome packaging Source: Reactome
  9. viral life cycle Source: Reactome
  10. viral process Source: Reactome
  11. viral release from host cell Source: Reactome
  12. viral transcription Source: Reactome
  13. virion assembly Source: Reactome
  14. 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

Enzyme and pathway databases

ReactomeiREACT_6145. Influenza Life Cycle.
REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
REACT_6212. Budding.
REACT_6215. Transport of HA trimer, NA tetramer and M2 tetramer from the endoplasmic reticulum to the Golgi Apparatus.
REACT_6235. Packaging of Eight RNA Segments.
REACT_6277. Assembly of Viral Components at the Budding Site.
REACT_6321. Uncoating of the Influenza Virion.
REACT_6326. Release.
REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemagglutinin
Cleaved into the following 2 chains:
Gene namesi
Name:HA
OrganismiInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Taxonomic identifieri211044 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000009255: Genome

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 domaini18 – 528511ExtracellularSequence AnalysisAdd
BLAST
Transmembranei529 – 54921HelicalSequence AnalysisAdd
BLAST
Topological domaini550 – 56516CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endocytic vesicle membrane Source: Reactome
  2. endoplasmic reticulum membrane Source: Reactome
  3. endosome lumen Source: Reactome
  4. extracellular region Source: Reactome
  5. Golgi membrane Source: Reactome
  6. host cell plasma membrane Source: UniProtKB-KW
  7. integral component of membrane Source: UniProtKB-KW
  8. plasma membrane Source: Reactome
  9. 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 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 342325Hemagglutinin HA1 chainPRO_0000039034Add
BLAST
Chaini344 – 565222Hemagglutinin HA2 chainPRO_0000039035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 480Interchain (between HA1 and HA2 chains)By similarity
Glycosylationi27 – 271N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi28 – 281N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi40 – 401N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi59 ↔ 291By similarity
Disulfide bondi72 ↔ 84By similarity
Disulfide bondi107 ↔ 152By similarity
Glycosylationi285 – 2851N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi295 ↔ 319By similarity
Glycosylationi303 – 3031N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi487 ↔ 491By similarity
Glycosylationi497 – 4971N-linked (GlcNAc...); by hostSequence Analysis
Lipidationi554 – 5541S-palmitoyl cysteine; by hostBy similarity
Lipidationi561 – 5611S-palmitoyl cysteine; by hostBy similarity
Lipidationi564 – 5641S-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 (By similarity).By similarity
Palmitoylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HA1-HA2.

Protein-protein interaction databases

IntActiP03452. 8 interactions.
MINTiMINT-3375119.

Structurei

Secondary structure

1
565
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 257Combined sources
Beta strandi39 – 446Combined sources
Beta strandi46 – 483Combined sources
Beta strandi56 – 616Combined sources
Beta strandi67 – 704Combined sources
Helixi74 – 796Combined sources
Helixi82 – 876Combined sources
Beta strandi94 – 985Combined sources
Beta strandi107 – 1104Combined sources
Helixi115 – 1228Combined sources
Beta strandi125 – 13410Combined sources
Turni136 – 1383Combined sources
Beta strandi149 – 1546Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi162 – 1665Combined sources
Beta strandi170 – 1723Combined sources
Beta strandi177 – 1826Combined sources
Beta strandi185 – 19713Combined sources
Helixi201 – 2088Combined sources
Beta strandi215 – 2184Combined sources
Beta strandi223 – 2264Combined sources
Beta strandi242 – 2509Combined sources
Beta strandi255 – 2628Combined sources
Beta strandi264 – 27512Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi288 – 29710Combined sources
Beta strandi300 – 3023Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi315 – 3195Combined sources
Beta strandi329 – 3313Combined sources
Turni350 – 3523Combined sources
Beta strandi364 – 3674Combined sources
Beta strandi376 – 3794Combined sources
Helixi381 – 40121Combined sources
Beta strandi405 – 4084Combined sources
Helixi418 – 46952Combined sources
Beta strandi472 – 4754Combined sources
Beta strandi477 – 4859Combined sources
Helixi491 – 4966Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RU7X-ray2.30A/C/E/G/I/K18-338[»]
B/D/F/H/J/L344-503[»]
1RVXX-ray2.20A/C/E/G/I/K14-338[»]
B/D/F/H/J/L344-503[»]
1RVZX-ray2.25A/C/E/G/I/K14-338[»]
B/D/F/H/J/L344-503[»]
ProteinModelPortaliP03452.
SMRiP03452. Positions 18-339, 344-518.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03452.

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.

P03452-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKANLLVLLC ALAAADADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL
60 70 80 90 100
EDSHNGKLCR LKGIAPLQLG KCNIAGWLLG NPECDPLLPV RSWSYIVETP
110 120 130 140 150
NSENGICYPG DFIDYEELRE QLSSVSSFER FEIFPKESSW PNHNTNGVTA
160 170 180 190 200
ACSHEGKSSF YRNLLWLTEK EGSYPKLKNS YVNKKGKEVL VLWGIHHPPN
210 220 230 240 250
SKEQQNLYQN ENAYVSVVTS NYNRRFTPEI AERPKVRDQA GRMNYYWTLL
260 270 280 290 300
KPGDTIIFEA NGNLIAPMYA FALSRGFGSG IITSNASMHE CNTKCQTPLG
310 320 330 340 350
AINSSLPYQN IHPVTIGECP KYVRSAKLRM VTGLRNIPSI QSRGLFGAIA
360 370 380 390 400
GFIEGGWTGM IDGWYGYHHQ NEQGSGYAAD QKSTQNAING ITNKVNTVIE
410 420 430 440 450
KMNIQFTAVG KEFNKLEKRM ENLNKKVDDG FLDIWTYNAE LLVLLENERT
460 470 480 490 500
LDFHDSNVKN LYEKVKSQLK NNAKEIGNGC FEFYHKCDNE CMESVRNGTY
510 520 530 540 550
DYPKYSEESK LNREKVDGVK LESMGIYQIL AIYSTVASSL VLLVSLGAIS
560
FWMCSNGSLQ CRICI
Length:565
Mass (Da):63,353
Last modified:March 6, 2007 - v2
Checksum:i47F34821748F494E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101C → S in AAM75158. (PubMed:11779399)Curated
Sequence conflicti146 – 1461N → TK in CAA24272. (PubMed:7278968)Curated
Sequence conflicti155 – 1551E → A in CAA24272. (PubMed:7278968)Curated
Sequence conflicti199 – 1991P → S in CAA24272. (PubMed:7278968)Curated
Sequence conflicti203 – 2031E → D in CAA24272. (PubMed:7278968)Curated
Sequence conflicti207 – 2071L → I in CAA24272. (PubMed:7278968)Curated
Sequence conflicti207 – 2071L → I in AAM75158. (PubMed:11779399)Curated
Sequence conflicti268 – 2681M → R in CAA24272. (PubMed:7278968)Curated
Sequence conflicti308 – 3081Y → F in CAA24272. (PubMed:7278968)Curated
Sequence conflicti337 – 3371I → N in ABO21709. (PubMed:15163504)Curated
Sequence conflicti397 – 3971T → S in CAA24272. (PubMed:7278968)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01088 Genomic RNA. Translation: CAA24272.1.
AF389118 Genomic RNA. Translation: AAM75158.1.
EF467821 Genomic RNA. Translation: ABO21709.1.
CY009444 Genomic RNA. Translation: ABD77675.1.
J02144 Genomic RNA. Translation: AAA43194.1.
RefSeqiNP_040980.1. NC_002017.1.

Genome annotation databases

GeneIDi956529.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01088 Genomic RNA. Translation: CAA24272.1 .
AF389118 Genomic RNA. Translation: AAM75158.1 .
EF467821 Genomic RNA. Translation: ABO21709.1 .
CY009444 Genomic RNA. Translation: ABD77675.1 .
J02144 Genomic RNA. Translation: AAA43194.1 .
RefSeqi NP_040980.1. NC_002017.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RU7 X-ray 2.30 A/C/E/G/I/K 18-338 [» ]
B/D/F/H/J/L 344-503 [» ]
1RVX X-ray 2.20 A/C/E/G/I/K 14-338 [» ]
B/D/F/H/J/L 344-503 [» ]
1RVZ X-ray 2.25 A/C/E/G/I/K 14-338 [» ]
B/D/F/H/J/L 344-503 [» ]
ProteinModelPortali P03452.
SMRi P03452. Positions 18-339, 344-518.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P03452. 8 interactions.
MINTi MINT-3375119.

Chemistry

BindingDBi P03452.
ChEMBLi CHEMBL1075313.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 956529.

Enzyme and pathway databases

Reactomei REACT_6145. Influenza Life Cycle.
REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
REACT_6212. Budding.
REACT_6215. Transport of HA trimer, NA tetramer and M2 tetramer from the endoplasmic reticulum to the Golgi Apparatus.
REACT_6235. Packaging of Eight RNA Segments.
REACT_6277. Assembly of Viral Components at the Budding Site.
REACT_6321. Uncoating of the Influenza Virion.
REACT_6326. Release.
REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

EvolutionaryTracei P03452.

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. "Nucleotide sequence of the haemagglutinin gene of a human influenza virus H1 subtype."
    Winter G., Fields S., Brownlee G.G.
    Nature 292:72-75(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Efficient generation and growth of influenza virus A/PR/8/34 from eight cDNA fragments."
    de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F., Osterhaus A.D.M.E., Fouchier R.A.M.
    Virus Res. 103:155-161(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], REVERSE GENETICS.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate EE12/E1.
  5. "The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype)."
    Caton A.J., Brownlee G.G., Yewdell J.W., Gerhard W.
    Cell 31:417-427(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 18-343.

Entry informationi

Entry nameiHEMA_I34A1
AccessioniPrimary (citable) accession number: P03452
Secondary accession number(s): A4GXH4
, Q20N38, Q83964, Q8JUU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 6, 2007
Last modified: November 26, 2014
This is version 121 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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference 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