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Protein

Hemagglutinin-esterase-fusion glycoprotein

Gene

HE

Organism
Influenza C virus (strain C/Taylor/1233/1947)
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 sitei353Charge relay systemUniRule annotation1
Active sitei356Charge 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/Taylor/1233/1947)
Taxonomic identifieri11567 [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 domaini1 – 617ExtracellularUniRule annotationAdd BLAST617
Transmembranei618 – 638HelicalUniRule annotationAdd BLAST21
Topological domaini639 – 642CytoplasmicUniRule 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
ChainiPRO_00004407661 – 433Hemagglutinin-esterase-fusion glycoprotein chain 1UniRule annotationAdd BLAST433
ChainiPRO_0000039169434 – 642Hemagglutinin-esterase-fusion glycoprotein chain 2UniRule annotationAdd BLAST209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi13N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi48N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi131N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi176N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi197 ↔ 239UniRule annotation
Disulfide bondi216 ↔ 303UniRule annotation
Disulfide bondi224 ↔ 276UniRule annotation
Glycosylationi382N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi539N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi590N-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

ProteinModelPortaliP07974.
SMRiP07974.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni83 – 297N-acetyl-9-O-acetylneuraminic acid bindingUniRule annotationAdd BLAST215
Regioni297 – 351Esterase domain-2UniRule annotationAdd BLAST55
Regioni352 – 637Fusion domain-2UniRule annotationAdd BLAST286

Sequence similaritiesi

Belongs to the influenza viruses hemagglutinin family.UniRule annotation

Keywords - Domaini

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.
IPR036514. SGNH_hydro_sf.
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: Fragment.

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

P07974-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AEKIKICLQK QVNSSFSLHN GFGGNLYATE EKRMFELVKP KAGASVLNQS
60 70 80 90 100
TWIGFGDSRT DKSNSAFPRS ADVSEKTADK FRSLSGGSLM LSMFGPPGKV
110 120 130 140 150
DYLYQGCGKH KVFYEGVNWS PHAAINCYRK NWTDIKLNFQ KNIYELASQS
160 170 180 190 200
HCMSLVNALD KTIPLQVTAG VAKNCNNSFL KNPALYTQEV NPSKEICGKE
210 220 230 240 250
NLAFFTLPTQ FGTYECKLHL VASCYFIYDS KEVYNKRGCD NYFQVIYDSS
260 270 280 290 300
GKVVGGLDNR VSPYTGNTGD TPTMQCDMLQ LKPGRYSVRS SPRFLLMPER
310 320 330 340 350
SYCFDMKEKG LVTAVQSVWG KGRESDHAVD QAYLSTPGCM LIQKQKPYIG
360 370 380 390 400
EADDHHGDQE MRELLSGLDY EARCISQSGW VNETSPFTEE YLLPPKFGRC
410 420 430 440 450
PLAAKEESIP KIPDGLLIPT SGTDTIVTKP KSRIFGIDDL IIGLLFVAIV
460 470 480 490 500
EAGIGGYLLG SRKESGGGVT KESAEKGFEK IGNDIQILRS STNIAIEKLN
510 520 530 540 550
DRITHDEQAI RDLTLEIENA RSEALLGELG IIRALLVGNI SIGLQESLWE
560 570 580 590 600
LASEITNRAG DLAVEVSPGC WIIDNNICDQ SCQNFIFKFN ETAPVPTIPP
610 620 630 640
LDTKIDLQSD PFYWGSSLGL AITTPISLAA LVISGIAICR TK
Length:642
Mass (Da):70,762
Last modified:August 1, 1988 - v1
Checksum:i591F15F288835411
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11637 Genomic RNA. Translation: AAA43795.1.

Similar proteinsi

Entry informationi

Entry nameiHEMA_INCTA
AccessioniPrimary (citable) accession number: P07974
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 25, 2017
This is version 99 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