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P17005

- HEMA_INCNA

UniProt

P17005 - HEMA_INCNA

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Protein

Hemagglutinin-esterase-fusion glycoprotein

Gene
HE
Organism
Influenza C virus (strain C/Nara/1982)
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei57 – 571Nucleophile By similarity
Active sitei352 – 3521Charge relay system By similarity
Active sitei355 – 3551Charge relay system By 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/Nara/1982)
Taxonomic identifieri203232 [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 domaini1 – 616616Extracellular Reviewed predictionAdd
BLAST
Transmembranei617 – 63721Helical; Reviewed predictionAdd
BLAST
Topological domaini638 – 6414Cytoplasmic 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Hemagglutinin-esterase-fusion glycoprotein chain 1PRO_0000039158Add
BLAST
Chaini433 – 641209Hemagglutinin-esterase-fusion glycoprotein chain 2PRO_0000039159Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 569Interchain (between HEF1 and HEF2 chains) By similarity
Glycosylationi12 – 121N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi47 – 471N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi106 ↔ 151 By similarity
Disulfide bondi126 ↔ 174 By similarity
Glycosylationi130 – 1301N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi196 ↔ 238 By similarity
Disulfide bondi215 ↔ 302 By similarity
Disulfide bondi223 ↔ 275 By similarity
Disulfide bondi332 ↔ 338 By similarity
Glycosylationi381 – 3811N-linked (GlcNAc...); by host Reviewed prediction

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

ProteinModelPortaliP17005.
SMRiP17005. Positions 436-597.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2626Fusion domain-1 By similarityAdd
BLAST
Regioni27 – 137111Esterase domain-1 By similarityAdd
BLAST
Regioni137 – 296160N-acetyl-9-O-acetylneuraminic acid binding By similarityAdd
BLAST
Regioni297 – 35155Esterase domain-2 By similarityAdd
BLAST
Regioni352 – 637286Fusion domain-2 By similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

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: Fragment.

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

P17005-1 [UniParc]FASTAAdd to Basket

« Hide

EKIKICLQKQ VNSSFSLHNG FGGNLYATEE KRMFELVKPK AGASVLNQST    50
WIGFGDSRTD KSNPNFPRSA DVSVKTANKF RSLTGGSLML SMFGPPGKVD 100
YLYQGCGKHK VFYEGVNWSP HAAIDCYRKN WTDIKLNFQK NIYELASQSH 150
CMSLVNALDK TIPLQATAGV AGNCNNSFLK NPALYTQEVT PPXXKCGKEN 200
LAFFTLPTQF GTYECRLHLV ASCYFIYDSK EVYNKRGCDN YFQVIYDSSG 250
KVVGGLDNRV SPYTGNSGDT PTMQCDMIQL KPGRYSVRSS PRFLLMPERS 300
YCFDMKEKGP VTAVQSIWGK DRKSDYAVDQ ACLSTPGCML IQKQKPYTGE 350
ADDHHGDQEM RELLSGLDYE ARCISQSGWV NETSPFTEEY LLPPKFGRCP 400
LAAKEESIPK IPDGLLIPTS GTDTTVTKPK SRIFGIDDLI IGLLFVAIVE 450
AGIGGYLLGS RKESGGGVTK ESAEKGFEKI GNDIQILRSS TNIAIEKLND 500
RISHDEQAIR DLTLEIENAR SEALLGELGI IRALLVGNIS IGLQESLWEL 550
ASEITNRAGD LAVEISPGCW IIDNNICDQS CQNFIFKFNE TAPVPTIPPL 600
DTKIDLQSDP FYWGSSLGLA ITAAISLAAL VISGIAICRT K 641
Length:641
Mass (Da):70,561
Last modified:August 1, 1990 - v1
Checksum:iFA2477DFF44B3319
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M25362 Genomic RNA. Translation: AAA43790.1.
PIRiB32665. HMIVEB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M25362 Genomic RNA. Translation: AAA43790.1 .
PIRi B32665. HMIVEB.

3D structure databases

ProteinModelPortali P17005.
SMRi P17005. Positions 436-597.
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. "Antigenic and genetic characterization of three influenza C strains isolated in the Kinki district of Japan in 1982-1983."
    Adachi K., Kitame F., Sugawara K., Nishimura H., Nakamura K.
    Virology 172:125-133(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiHEMA_INCNA
AccessioniPrimary (citable) accession number: P17005
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 89 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

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