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P03465

- HEMA_INCCA

UniProt

P03465 - HEMA_INCCA

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Protein

Hemagglutinin-esterase-fusion glycoprotein

Gene

HE

Organism
Influenza C virus (strain C/California/1978)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Binds to the N-acetyl-9-O-acetylneuraminic acid residues on the cell surface, bringing about the attachment of the virus particle to the cell. 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 induce an irreversible conformational change in HEF2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Displays a receptor-destroying activity which is a neuraminidate-O-acetyl esterase. This activity cleaves off any receptor on the cell surface, which would otherwise prevent virions release. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell (By similarity).By similarity

Catalytic activityi

N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711NucleophileBy similarity
Active sitei365 – 3651Charge relay systemBy similarity
Active sitei368 – 3681Charge relay systemBy similarity

GO - Molecular functioni

  1. sialate O-acetylesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  2. fusion of virus membrane with host plasma membrane Source: InterPro
  3. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin, Hydrolase

Keywords - Biological processi

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 entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Hemagglutinin-esterase-fusion glycoprotein (EC:3.1.1.53)
Short name:
HEF
Cleaved into the following 2 chains:
Gene namesi
Name:HE
OrganismiInfluenza C virus (strain C/California/1978)
Taxonomic identifieri203224 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus C
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini15 – 629615ExtracellularSequence AnalysisAdd
BLAST
Transmembranei630 – 65021HelicalSequence AnalysisAdd
BLAST
Topological domaini651 – 6544CytoplasmicSequence Analysis

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 – 1414By similarityAdd
BLAST
Chaini15 – 444430Hemagglutinin-esterase-fusion glycoprotein chain 1PRO_0000039144Add
BLAST
Chaini446 – 654209Hemagglutinin-esterase-fusion glycoprotein chain 2PRO_0000039145Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi20 ↔ 582Interchain (between HEF1 and HEF2 chains)By similarity
Glycosylationi26 – 261N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi61 – 611N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi119 ↔ 164By similarity
Disulfide bondi139 ↔ 187By similarity
Glycosylationi143 – 1431N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi209 ↔ 251By similarity
Disulfide bondi228 ↔ 315By similarity
Disulfide bondi236 ↔ 288By similarity
Disulfide bondi345 ↔ 351By similarity
Glycosylationi394 – 3941N-linked (GlcNAc...); by hostSequence Analysis

Post-translational modificationi

In natural infection, inactive HEF is matured into HEF1 and HEF2 outside the cell by one or more trypsin-like, arginine-specific endoprotease.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HEF1-HEF2.By similarity

Structurei

3D structure databases

ProteinModelPortaliP03465.
SMRiP03465. Positions 15-440, 449-610.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni15 – 4026Fusion domain-1By similarityAdd
BLAST
Regioni41 – 150110Esterase domain-1By similarityAdd
BLAST
Regioni150 – 309160N-acetyl-9-O-acetylneuraminic acid bindingBy similarityAdd
BLAST
Regioni310 – 36455Esterase domain-2By similarityAdd
BLAST
Regioni365 – 650286Fusion domain-2By similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.90.20.10. 1 hit.
InterProiIPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
IPR013829. Hemagglutn_stalk.
IPR014831. Hemagglutn_stalk_influenz-C.
[Graphical view]
PfamiPF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
PF08720. Hema_stalk. 1 hit.
[Graphical view]
SUPFAMiSSF49818. SSF49818. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03465-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MFFSLLLMLG LTEAEKIKIC LQKQVNSSFS LHNGFGGNLY ATEEKRMFEL
60 70 80 90 100
VKPKAGASVL NQSTWIGFGD SRTDQSNSAF PRSLMSAKTA DKFRSLSGGS
110 120 130 140 150
LMLSMFGPPG KVDYLYQGCG KHKVFYEGVN WSPHAAIDCY RKNWTDIKLN
160 170 180 190 200
FQKSIYELAS QSHCMSLVNA LDKTIPLQVT KGVAKNCNNS FLKNPALYTQ
210 220 230 240 250
EVKPLEQICG EENLAFFTLP TQFGTYECKL HLVASCYFIY DSKEVYNKRG
260 270 280 290 300
CGNYFQVIYD SSGKVVGGLD NRVSPYTGNS GDTPTMQCDM LQLKPGRYSV
310 320 330 340 350
RSSPRFLLMP ERSYCFDMKE KGPVTAVQSI WGKGRKSDYA VDQACLSTPG
360 370 380 390 400
CMLIQKQKPY IGEADDHHGD QEMRELLSGL DYEARCISQS GWVNETSPFT
410 420 430 440 450
EEYLLPPKFG RCPLAAKEES IPKIPDGLLI PTSGTDTTVT KPKSRIFGID
460 470 480 490 500
DLIIGLLFVA IVEAGIGGYL LGSRKESGGG VTKESAEKGF EKIGNDIQIL
510 520 530 540 550
RSSTNIAIEK LNDRISHDEQ AIRDLTLEIE NARSEALLGE LGIIRALLVG
560 570 580 590 600
NISIGLQESL WELASEITNR AGDLAVEVSP GCWIIDNNIC DQSCQNFIFK
610 620 630 640 650
FNETAPVPTI PPLDTKIDLQ SDPFYWGSSL GLAITAANLM AALVISGIAI

CRTK
Length:654
Mass (Da):72,085
Last modified:July 21, 1986 - v1
Checksum:i7F4C28D9EFD2E429
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01689 Genomic RNA. Translation: AAA43791.1.
PIRiA04076. HMIVC8.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01689 Genomic RNA. Translation: AAA43791.1 .
PIRi A04076. HMIVC8.

3D structure databases

ProteinModelPortali P03465.
SMRi P03465. Positions 15-440, 449-610.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.90.20.10. 1 hit.
InterProi IPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
IPR013829. Hemagglutn_stalk.
IPR014831. Hemagglutn_stalk_influenz-C.
[Graphical view ]
Pfami PF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
PF08720. Hema_stalk. 1 hit.
[Graphical view ]
SUPFAMi SSF49818. SSF49818. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Influenza C virus hemagglutinin: comparison with influenza A and B virus hemagglutinins."
    Nakada S., Creager R.S., Krystal M., Aaronson R.P., Palese P.
    J. Virol. 50:118-124(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiHEMA_INCCA
AccessioniPrimary (citable) accession number: P03465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3