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P07975

- HEMA_INCJH

UniProt

P07975 - HEMA_INCJH

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Protein

Hemagglutinin-esterase-fusion glycoprotein

Gene
HE
Organism
Influenza C virus (strain C/Johannesburg/1/1966)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711Nucleophile1 Publication
Active sitei366 – 3661Charge relay system1 Publication
Active sitei369 – 3691Charge relay system1 Publication

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

Protein family/group databases

TCDBi1.G.14.1.1. the influenza virus hemagglutinin/fusion pore-forming protein (influenza-h/fpp) family.

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/Johannesburg/1/1966)
Taxonomic identifieri100673 [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 – 630616Extracellular Reviewed predictionAdd
BLAST
Transmembranei631 – 65121Helical; Reviewed predictionAdd
BLAST
Topological domaini652 – 6554Cytoplasmic Reviewed prediction

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
  4. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi71 – 711S → A: 96% loss of esterase activity. 1 Publication
Mutagenesisi261 – 2611D → A: 64% loss of esterase activity. 1 Publication
Mutagenesisi280 – 2801N → A: Complete loss of esterase activity. 1 Publication
Mutagenesisi368 – 3681H → A: Complete loss of esterase activity. 1 Publication
Mutagenesisi369 – 3691H → A: Complete loss of esterase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1414Add
BLAST
Chaini15 – 446432Hemagglutinin-esterase-fusion glycoprotein chain 1PRO_0000039152Add
BLAST
Chaini447 – 655209Hemagglutinin-esterase-fusion glycoprotein chain 2PRO_0000039153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi20 ↔ 583Interchain (between HEF1 and HEF2 chains)
Glycosylationi26 – 261N-linked (GlcNAc...); by host
Glycosylationi61 – 611N-linked (GlcNAc...); by host
Disulfide bondi120 ↔ 165
Disulfide bondi140 ↔ 188
Glycosylationi144 – 1441N-linked (GlcNAc...); by host
Disulfide bondi210 ↔ 252
Disulfide bondi229 ↔ 316
Disulfide bondi237 ↔ 289
Disulfide bondi346 ↔ 352
Glycosylationi395 – 3951N-linked (GlcNAc...); by host

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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer of disulfide-linked HEF1-HEF2.

Structurei

Secondary structure

1
655
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 257
Beta strandi39 – 4810
Beta strandi59 – 6911
Beta strandi71 – 733
Helixi80 – 834
Helixi88 – 925
Beta strandi94 – 963
Helixi102 – 1076
Beta strandi110 – 1123
Beta strandi118 – 1203
Beta strandi122 – 1265
Helixi130 – 1323
Helixi134 – 1363
Helixi146 – 16015
Beta strandi164 – 1696
Beta strandi186 – 1883
Beta strandi194 – 1974
Turni205 – 2084
Beta strandi214 – 2207
Beta strandi222 – 2243
Beta strandi230 – 24011
Helixi244 – 2507
Beta strandi256 – 2605
Beta strandi262 – 2643
Beta strandi266 – 2716
Turni272 – 2743
Beta strandi286 – 2949
Beta strandi296 – 3038
Beta strandi314 – 3174
Beta strandi325 – 3284
Helixi341 – 3477
Beta strandi352 – 3554
Beta strandi364 – 3663
Helixi372 – 3776
Helixi378 – 3825
Beta strandi386 – 3894
Beta strandi392 – 3943
Beta strandi399 – 4035
Beta strandi407 – 4126
Turni419 – 4213
Beta strandi424 – 4329
Beta strandi452 – 4543
Beta strandi459 – 4624
Beta strandi469 – 4746
Turni488 – 4903
Helixi491 – 51020
Beta strandi519 – 5213
Helixi528 – 56942
Turni573 – 5753
Turni588 – 5903
Helixi593 – 5997

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FLCX-ray3.20A/C/E15-446[»]
B/D/F447-621[»]
ProteinModelPortaliP07975.
SMRiP07975. Positions 15-441, 450-611.

Miscellaneous databases

EvolutionaryTraceiP07975.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni15 – 4026Fusion domain-1Add
BLAST
Regioni41 – 151111Esterase domain-1Add
BLAST
Regioni151 – 310160N-acetyl-9-O-acetylneuraminic acid bindingAdd
BLAST
Regioni311 – 36555Esterase domain-2Add
BLAST
Regioni366 – 651286Fusion domain-2Add
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.

P07975-1 [UniParc]FASTAAdd to Basket

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MFFSLLLVLG LTEAEKIKIC LQKQVNSSFS LHNGFGGNLY ATEEKRMFEL    50
VKPKAGASVL NQSTWIGFGD SRTDKSNSAF PRSADVSAKT ADKFRFLSGG 100
SLMLSMFGPP GKVDYLYQGC GKHKVFYEGV NWSPHAAINC YRKNWTDIKL 150
NFQKNIYELA SQSHCMSLVN ALDKTIPLQV TAGTAGNCNN SFLKNPALYT 200
QEVKPSENKC GKENLAFFTL PTQFGTYECK LHLVASCYFI YDSKEVYNKR 250
GCDNYFQVIY DSFGKVVGGL DNRVSPYTGN SGDTPTMQCD MLQLKPGRYS 300
VRSSPRFLLM PERSYCFDMK EKGPVTAVQS IWGKGRESDY AVDQACLSTP 350
GCMLIQKQKP YIGEADDHHG DQEMRELLSG LDYEARCISQ SGWVNETSPF 400
TEKYLLPPKF GRCPLAAKEE SIPKIPDGLL IPTSGTDTTV TKPKSRIFGI 450
DDLIIGVLFV AIVETGIGGY LLGSRKESGG GVTKESAEKG FEKIGNDIQI 500
LKSSINIAIE KLNDRISHDE QAIRDLTLEI ENARSEALLG ELGIIRALLV 550
GNISIGLQES LWELASEITN RAGDLAVEVS PGCWIIDNNI CDQSCQNFIF 600
KFNETAPVPT IPPLDTKIDL QSDPFYWGSS LGLAITATIS LAALVISGIA 650
ICRTK 655
Length:655
Mass (Da):72,131
Last modified:August 1, 1988 - v1
Checksum:i52C78BFCC5A24AC8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961F → S.
Natural varianti263 – 2631F → S.
Natural varianti457 – 4571V → L.
Natural varianti465 – 4651T → A.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M17868 Genomic RNA. Translation: AAA43788.1.
AJ872181 Genomic RNA. Translation: CAI43342.1.
AY880247 mRNA. Translation: AAW73083.1.
PIRiS07412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M17868 Genomic RNA. Translation: AAA43788.1 .
AJ872181 Genomic RNA. Translation: CAI43342.1 .
AY880247 mRNA. Translation: AAW73083.1 .
PIRi S07412.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FLC X-ray 3.20 A/C/E 15-446 [» ]
B/D/F 447-621 [» ]
ProteinModelPortali P07975.
SMRi P07975. Positions 15-441, 450-611.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

TCDBi 1.G.14.1.1. the influenza virus hemagglutinin/fusion pore-forming protein (influenza-h/fpp) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P07975.

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. "Structure of the influenza C glycoprotein gene as determined from cloned DNA."
    Pfeifer J.B., Compans R.W.
    Virus Res. 1:281-296(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Use of influenza C virus glycoprotein HEF for generation of vesicular stomatitis virus pseudotypes."
    Hanika A., Larisch B., Steinmann E., Schwegmann-Wessels C., Herrler G., Zimmer G.
    J. Gen. Virol. 86:1455-1465(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA].
  3. "The catalytic triad of the influenza C virus glycoprotein HEF esterase: characterization by site-directed mutagenesis and functional analysis."
    Pleschka S., Klenk H.D., Herrler G.
    J. Gen. Virol. 76:2529-2537(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-71; ASP-261; ASN-280; HIS-368 AND HIS-369.
  4. "Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus."
    Rosenthal P.B., Zhang X., Formanowski F., Fitz W., Wong C.H., Meier-Ewert H., Skehel J.J., Wiley D.C.
    Nature 396:92-96(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 15-621 AND ACTIVE SITE.

Entry informationi

Entry nameiHEMA_INCJH
AccessioniPrimary (citable) accession number: P07975
Secondary accession number(s): Q5EI66, Q5JZY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 11, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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

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