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P26562

- HEMA_I76A4

UniProt

P26562 - HEMA_I76A4

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Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Duck/Alberta/35/1976 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei344 – 3452Cleavage; 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: 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/Duck/Alberta/35/1976 H1N1)
Taxonomic identifieri352520 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
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 domaini18 – 529512ExtracellularSequence AnalysisAdd
BLAST
Transmembranei530 – 55021HelicalSequence AnalysisAdd
BLAST
Topological domaini551 – 56616CytoplasmicSequence 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 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 343326Hemagglutinin HA1 chainPRO_0000038910Add
BLAST
Chaini345 – 566222Hemagglutinin HA2 chainPRO_0000038911Add
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 hostSequence Analysis
Glycosylationi28 – 281N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi40 – 401N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi59 ↔ 292By similarity
Disulfide bondi72 ↔ 84By similarity
Glycosylationi104 – 1041N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi107 ↔ 153By similarity
Disulfide bondi296 ↔ 320By similarity
Glycosylationi304 – 3041N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi488 ↔ 492By similarity
Glycosylationi498 – 4981N-linked (GlcNAc...); by hostSequence Analysis
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 (By similarity).By similarity
Palmitoylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HA1-HA2.

Structurei

Secondary structure

1
566
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
Helixi74 – 796Combined sources
Helixi82 – 843Combined sources
Turni85 – 873Combined sources
Beta strandi96 – 983Combined sources
Helixi115 – 1217Combined sources
Beta strandi123 – 13412Combined sources
Helixi136 – 1394Combined sources
Beta strandi150 – 1556Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi178 – 1836Combined sources
Beta strandi186 – 19813Combined sources
Helixi202 – 2098Combined sources
Beta strandi216 – 2205Combined sources
Beta strandi223 – 2275Combined sources
Beta strandi242 – 25110Combined sources
Beta strandi256 – 2638Combined sources
Beta strandi265 – 27612Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi289 – 2935Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi307 – 3104Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi330 – 3323Combined sources
Turni351 – 3533Combined sources
Beta strandi365 – 3684Combined sources
Helixi382 – 40120Combined sources
Helixi419 – 47052Combined sources
Helixi471 – 4733Combined sources
Beta strandi474 – 4785Combined sources
Beta strandi481 – 4866Combined sources
Helixi490 – 4989Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WRHX-ray3.00H/J/L18-343[»]
I/K/M345-566[»]
ProteinModelPortaliP26562.
SMRiP26562. Positions 18-519.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26562.

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.

P26562-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEAKLFVLFC TFTVLKADTI CVGYHANNST DTVDTVLEKN VTVTHSVNLL
60 70 80 90 100
EDSHNGKLCS LNGIAPLQLG KCNVAGWLLG NPECDLLLTA NSWSYIIETS
110 120 130 140 150
NSENGTCYPG EFIDYEELRE QLSSISSFEK FEIFPKASSW PNHETTKGVT
160 170 180 190 200
AACSYSGASS FYRNLLWITK KGTSYPKLSK SYTNNKGKEV LVLWGVHHPP
210 220 230 240 250
SVSEQQSLYQ NADAYVSVGS SKYNRRFAPE IAARPEVRGQ AGRMNYYWTL
260 270 280 290 300
LDQGDTITFE ATGNLIAPWY AFALNKGSDS GIITSDAPVH NCDTRCQTPH
310 320 330 340 350
GALNSSLPFQ NVHPITIGEC PKYVKSTKLR MATGLRNVPS IQSRGLFGAI
360 370 380 390 400
AGFIEGGWTG MIDGWYGYHH QNEQGSGYAA DQKSTQNAID GITSKVNSVI
410 420 430 440 450
EKMNTQFTAV GKEFNNLERR IENLNKKVDD GFLDVWTYNA ELLVLLENER
460 470 480 490 500
TLDFHDSNVR NLYEKVKSQL RNNAKEIGNG CFEFYHKCDD ECMESVKNGT
510 520 530 540 550
YDYPKYSEES KLNREEIDGV KLESMGVYQI LAIYSTVASS LVLLVSWGAI
560
SFWMCSNGSL QCRICI
Length:566
Mass (Da):63,072
Last modified:February 1, 1996 - v2
Checksum:i9B7ADCA0E9BCA819
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651A → P in AAB52910. (PubMed:8892928)Curated
Sequence conflicti125 – 1251I → V in AAB52910. (PubMed:8892928)Curated
Sequence conflicti236 – 2361E → K in AAB52910. (PubMed:8892928)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10477 Genomic RNA. Translation: BAA01280.1.
U47310 mRNA. Translation: AAB52910.1.
PIRiA36257. HMIVD1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10477 Genomic RNA. Translation: BAA01280.1 .
U47310 mRNA. Translation: AAB52910.1 .
PIRi A36257. HMIVD1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WRH X-ray 3.00 H/J/L 18-343 [» ]
I/K/M 345-566 [» ]
ProteinModelPortali P26562.
SMRi P26562. Positions 18-519.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P26562.

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. "Molecular analysis of the haemagglutinin gene of an avian H1N1 influenza virus."
    Austin F.J., Kawaoka Y., Webster R.G.
    J. Gen. Virol. 71:2471-2474(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Emergence of avian H1N1 influenza viruses in pigs in China."
    Guan Y., Shortridge K.F., Krauss S., Li P.H., Kawaoka Y., Webster R.G.
    J. Virol. 70:8041-8046(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-344.

Entry informationi

Entry nameiHEMA_I76A4
AccessioniPrimary (citable) accession number: P26562
Secondary accession number(s): O09652
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 97 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

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