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Protein

Hemagglutinin-esterase-fusion glycoprotein

Gene

HE

Organism
Influenza C virus (strain C/California/1978)
Status
Reviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei71NucleophileUniRule annotation1
Active sitei365Charge relay systemUniRule annotation1
Active sitei368Charge relay systemUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHemagglutinin, Hydrolase
Biological processFusion 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-esterase-fusion glycoproteinUniRule annotation (EC:3.1.1.53UniRule annotation)
Short name:
HEFUniRule annotation
Cleaved into the following 2 chains:
Hemagglutinin-esterase-fusion glycoprotein chain 1UniRule annotation
Short name:
HEF1UniRule annotation
Hemagglutinin-esterase-fusion glycoprotein chain 2UniRule annotation
Short name:
HEF2UniRule annotation
Gene namesi
Name:HEUniRule annotation
OrganismiInfluenza C virus (strain C/California/1978)
Taxonomic identifieri203224 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus C
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Subcellular locationi

  • Virion membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host cell membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini15 – 629ExtracellularUniRule annotationAdd BLAST615
Transmembranei630 – 650HelicalUniRule annotationAdd BLAST21
Topological domaini651 – 654CytoplasmicUniRule annotation4

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 14UniRule annotationAdd BLAST14
ChainiPRO_000044055215 – 654Hemagglutinin-esterase-fusion glycoproteinUniRule annotationAdd BLAST640
ChainiPRO_000044055315 – 445Hemagglutinin-esterase-fusion glycoprotein chain 1UniRule annotationAdd BLAST431
ChainiPRO_0000440554446 – 654Hemagglutinin-esterase-fusion glycoprotein chain 2UniRule annotationAdd BLAST209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi20 ↔ 582Interchain (between HEF1 and HEF2 chains)UniRule annotation
Glycosylationi26N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi61N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi143N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi188N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi209 ↔ 251UniRule annotation
Disulfide bondi228 ↔ 315UniRule annotation
Disulfide bondi236 ↔ 288UniRule annotation
Glycosylationi394N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi551N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi602N-linked (GlcNAc...) asparagine; by hostUniRule annotation1

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.UniRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HEF1-HEF2.UniRule annotation

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliP03465.
SMRiP03465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni15 – 40Fusion domain-1UniRule annotationAdd BLAST26
Regioni41 – 157Esterase domain-1UniRule annotationAdd BLAST117
Regioni157 – 309N-acetyl-9-O-acetylneuraminic acid bindingUniRule annotationAdd BLAST153
Regioni309 – 363Esterase domain-2UniRule annotationAdd BLAST55
Regioni364 – 654Fusion domain-2UniRule annotationAdd BLAST291

Sequence similaritiesi

Belongs to the influenza viruses hemagglutinin family.UniRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

HAMAPiMF_04072. INFV_HEMA. 1 hit.
InterProiView protein in InterPro
IPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
IPR014831. Hemagglutn_stalk_influenz-C.
IPR013830. SGNH_hydro.
PfamiView protein in Pfam
PF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
PF08720. Hema_stalk. 1 hit.
SUPFAMiSSF49818. SSF49818. 1 hit.
SSF52266. SSF52266. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P03465-1 [UniParc]FASTAAdd to basket

« Hide

        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

PIRiA04076. HMIVC8.

Similar proteinsi

Entry informationi

Entry nameiHEMA_INCCA
AccessioniPrimary (citable) accession number: P03465
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: August 30, 2017
This is version 98 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families