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P03451

- HEMA_I57A0

UniProt

P03451 - HEMA_I57A0

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Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Japan/305/1957 H2N2)
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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei340 – 3412Cleavage; 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/Japan/305/1957 H2N2)
Taxonomic identifieri387161 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]

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.

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi519 – 5191S → A: No effect on palmitoylation. 1 Publication
Mutagenesisi520 – 5201S → A: No effect on palmitoylation. 1 Publication
Mutagenesisi551 – 5511C → A: Loss of palmitoylation. 1 Publication
Mutagenesisi558 – 5581C → A: Loss of palmitoylation. 1 Publication
Mutagenesisi561 – 5611C → A: Loss of palmitoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – 339324Hemagglutinin HA1 chainPRO_0000039010Add
BLAST
Chaini341 – 562222Hemagglutinin HA2 chainPRO_0000039011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi19 ↔ 477Interchain (between HA1 and HA2 chains)By similarity
Glycosylationi25 – 251N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi26 – 261N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi38 – 381N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi57 ↔ 288By similarity
Disulfide bondi70 ↔ 82By similarity
Disulfide bondi105 ↔ 149By similarity
Glycosylationi179 – 1791N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi180 – 1801N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi292 ↔ 316By similarity
Glycosylationi300 – 3001N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi484 ↔ 488By similarity
Glycosylationi494 – 4941N-linked (GlcNAc...); by hostSequence Analysis
Lipidationi551 – 5511S-palmitoyl cysteine; by host1 Publication
Lipidationi558 – 5581S-palmitoyl cysteine; by host1 Publication
Lipidationi561 – 5611S-palmitoyl cysteine; by host1 Publication

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.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HA1-HA2.

Protein-protein interaction databases

DIPiDIP-60235N.

Structurei

Secondary structure

1
562
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 238
Beta strandi37 – 426
Beta strandi44 – 463
Beta strandi65 – 684
Helixi72 – 776
Helixi80 – 867
Beta strandi94 – 963
Beta strandi101 – 1033
Beta strandi108 – 1103
Helixi113 – 1197
Beta strandi122 – 13211
Helixi134 – 1363
Beta strandi138 – 1414
Beta strandi146 – 1516
Beta strandi154 – 1563
Beta strandi161 – 1633
Beta strandi167 – 1693
Beta strandi174 – 1796
Beta strandi182 – 19413
Helixi198 – 2058
Beta strandi206 – 2094
Beta strandi212 – 2154
Beta strandi220 – 2234
Beta strandi239 – 2479
Beta strandi252 – 2598
Beta strandi261 – 27111
Beta strandi278 – 2803
Beta strandi289 – 2946
Beta strandi297 – 2993
Beta strandi303 – 3064
Beta strandi313 – 3153
Beta strandi326 – 3283
Turni347 – 3493
Beta strandi361 – 3677
Beta strandi373 – 3764
Helixi378 – 39720
Beta strandi403 – 4053
Helixi415 – 46652
Helixi467 – 4693
Beta strandi470 – 4723
Beta strandi474 – 4829
Helixi486 – 4938
Helixi499 – 51012

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FHUmodel-A/C/E16-335[»]
B/D/F341-500[»]
4HFUX-ray3.11A15-340[»]
B341-514[»]
4HG4X-ray3.20A/B/C/D/E/F/G/H/I15-340[»]
a/b/c/d/e/f/g/h/i341-514[»]
ProteinModelPortaliP03451.
SMRiP03451. Positions 16-335, 341-513.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini16 – 525510ExtracellularSequence AnalysisAdd
BLAST
Topological domaini547 – 56216CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei526 – 54621HelicalSequence AnalysisAdd
BLAST

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.

P03451-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAIIYLILLF TAVRGDQICI GYHANNSTEK VDTNLERNVT VTHAKDILEK
60 70 80 90 100
THNGKLCKLN GIPPLELGDC SIAGWLLGNP ECDRLLSVPE WSYIMEKENP
110 120 130 140 150
RDGLCYPGSF NDYEELKHLL SSVKHFEKVK ILPKDRWTQH TTTGGSRACA
160 170 180 190 200
VSGNPSFFRN MVWLTKEGSD YPVAKGSYNN TSGEQMLIIW GVHHPIDETE
210 220 230 240 250
QRTLYQNVGT YVSVGTSTLN KRSTPEIATR PKVNGQGGRM EFSWTLLDMW
260 270 280 290 300
DTINFESTGN LIAPEYGFKI SKRGSSGIMK TEGTLENCET KCQTPLGAIN
310 320 330 340 350
TTLPFHNVHP LTIGECPKYV KSEKLVLATG LRNVPQIESR GLFGAIAGFI
360 370 380 390 400
EGGWQGMVDG WYGYHHSNDQ GSGYAADKES TQKAFDGITN KVNSVIEKMN
410 420 430 440 450
TQFEAVGKEF GNLERRLENL NKRMEDGFLD VWTYNAELLV LMENERTLDF
460 470 480 490 500
HDSNVKNLYD KVRMQLRDNV KELGNGCFEF YHKCDDECMN SVKNGTYDYP
510 520 530 540 550
KYEEESKLNR NEIKGVKLSS MGVYQILAIY ATVAGSLSLA IMMAGISFWM
560
CSNGSLQCRI CI
Length:562
Mass (Da):63,119
Last modified:July 21, 1986 - v1
Checksum:i6B7FD0C038993630
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02127 Genomic RNA. Translation: AAA43185.1.
PIRiA04062. HMIV2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02127 Genomic RNA. Translation: AAA43185.1 .
PIRi A04062. HMIV2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FHU model - A/C/E 16-335 [» ]
B/D/F 341-500 [» ]
4HFU X-ray 3.11 A 15-340 [» ]
B 341-514 [» ]
4HG4 X-ray 3.20 A/B/C/D/E/F/G/H/I 15-340 [» ]
a/b/c/d/e/f/g/h/i 341-514 [» ]
ProteinModelPortali P03451.
SMRi P03451. Positions 16-335, 341-513.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60235N.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Cloning and DNA sequence of double-stranded copies of haemagglutinin genes from H2 and H3 strains elucidates antigenic shift and drift in human influenza virus."
    Gething M.-J., Bye J., Skehel J.J., Waterfield M.
    Nature 287:301-306(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion."
    Naeve C.W., Williams D.
    EMBO J. 9:3857-3866(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-551; CYS-558 AND CYS-561, MUTAGENESIS OF SER-519; SER-520; CYS-551; CYS-558 AND CYS-561.
  3. "Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: role of hemagglutinin surface density."
    Ellens H., Bentz J., Mason D., Zhang F., White J.M.
    Biochemistry 29:9697-9707(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiHEMA_I57A0
AccessioniPrimary (citable) accession number: P03451
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 102 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