Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9WCD9

- HEMA_I30A0

UniProt

Q9WCD9 - HEMA_I30A0

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Swine/Iowa/15/1930 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).By similarity

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/Swine/Iowa/15/1930 H1N1)
Taxonomic identifieri380342 [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 (By similarity).By similarity

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_5000055153Add
BLAST
Chaini345 – 566222Hemagglutinin HA2 chainPRO_5000055154Add
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.By similarity

Structurei

Secondary structure

1
566
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 257
Beta strandi39 – 446
Beta strandi46 – 483
Beta strandi58 – 614
Beta strandi67 – 704
Helixi74 – 796
Helixi82 – 898
Beta strandi96 – 983
Helixi115 – 1228
Beta strandi125 – 1317
Turni136 – 1383
Beta strandi150 – 1556
Beta strandi158 – 1603
Beta strandi163 – 1675
Beta strandi178 – 1836
Beta strandi186 – 1883
Beta strandi190 – 1989
Helixi202 – 2098
Beta strandi216 – 2194
Beta strandi224 – 2274
Beta strandi240 – 25112
Beta strandi256 – 2638
Beta strandi265 – 2684
Beta strandi271 – 2766
Beta strandi282 – 2843
Beta strandi289 – 2935
Beta strandi295 – 2984
Beta strandi301 – 3033
Beta strandi308 – 3103
Beta strandi316 – 3205
Beta strandi330 – 3323

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RUYX-ray2.70H/J/L18-339[»]
ProteinModelPortaliQ9WCD9.
SMRiQ9WCD9. Positions 345-519.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WCD9.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 529512ExtracellularSequence AnalysisAdd
BLAST
Topological domaini551 – 56616CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei530 – 55021HelicalSequence 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.

Q9WCD9 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKAILLVLLC AFAATNADTL CIGYHANNST DTVDTVLEKN VTVTHSVNLL
60 70 80 90 100
EDSHNGKLCR LGGIAPLQLG KCNIAGXXLG NPECDLLLTV SSWSYIVETS
110 120 130 140 150
NSDNGTCYPG DFIDYEELRE QLSSVSSFEK FEIFPKTSSW PNHETTRGVT
160 170 180 190 200
AACPYAGASS FYRNLLWLVK KENSYPKLSK SYVNNKGKEV LVLWGVHHPP
210 220 230 240 250
TSTDQQSLYQ NADAYVSVGS SKYDRRFTPE IAARPKVRGQ AGRMNYYWTL
260 270 280 290 300
LEPGDTITFE ATGNLVAPRY AFALNRGSES GIITSDAPVH DCDTKCQTPH
310 320 330 340 350
GAINSSLPFQ NIHPVTIGEC PKYVKSTKLR MVTGLRNIPS IQSRGLFGAI
360 370 380 390 400
AGFIEGGWTG LIDGWYGYHH QNGQGSGYAA DQKSTQNAID GITNKVNSVI
410 420 430 440 450
EKMNTQFTVV GKEFNNLERR IKNLNKKVDD GFLDVWTYNA EMLVLLENER
460 470 480 490 500
TLDFHDSNVK NLYEKARSQL RNNAKEIGNG CFEFYHKCDD ACMESVRNGT
510 520 530 540 550
YDYPKYSEES KLNREEIDGV KLESMMVYQI LAIYSTVASS LVLLVSLGAI
560
SFWMCSNGSL QCRICI
Length:566
Mass (Da):62,868
Last modified:November 1, 1999 - v1
Checksum:iDF84450D8446B949
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF091308 mRNA. Translation: AAD25303.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF091308 mRNA. Translation: AAD25303.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RUY X-ray 2.70 H/J/L 18-339 [» ]
ProteinModelPortali Q9WCD9.
SMRi Q9WCD9. Positions 345-519.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q9WCD9.

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 basis for the generation in pigs of influenza A viruses with pandemic potential."
    Ito T., Couceiro J.N., Kelm S., Baum L.G., Krauss S., Castrucci M.R., Donatelli I., Kida H., Paulson J.C., Webster R.G., Kawaoka Y.
    J. Virol. 72:7367-7373(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiHEMA_I30A0
AccessioniPrimary (citable) accession number: Q9WCD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 80 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