SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P68762

- HEMA_INCAA

UniProt

P68762 - HEMA_INCAA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Hemagglutinin-esterase-fusion glycoprotein

Gene
HE
Organism
Influenza C virus (strain C/Ann Arbor/1/1950)
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 sitei71 – 711Nucleophile By similarity
Active sitei366 – 3661Charge relay system By similarity
Active sitei369 – 3691Charge 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/Ann Arbor/1/1950)
Taxonomic identifieri11553 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus C
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000008286: Genome

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1414 By similarityAdd
BLAST
Chaini15 – 446432Hemagglutinin-esterase-fusion glycoprotein chain 1PRO_0000039142Add
BLAST
Chaini447 – 655209Hemagglutinin-esterase-fusion glycoprotein chain 2PRO_0000039143Add
BLAST

Amino acid modifications

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

ProteinModelPortaliP68762.
SMRiP68762. Positions 15-441, 450-611.

Family & Domainsi

Region

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

P68762-1 [UniParc]FASTAAdd to Basket

« Hide

MFFSLLLMLG LTEAEKIKIC LQKQVNSSFS LHNGFGGNLY ATEEKRMFEL    50
VKPKAGASVL NQSTWIGFGD SRTDKSNSAF PRSADVSAKT ADKFRSLSGG 100
SLMLSMFGPP GKVDYLYQGC GKHKVFYEGV NWSPHAAINC YRKNWTDIKL 150
NFQKNIYELA SQSHCMSLVN ALDKTIPLQA TAGVAKNCNN SFLKNPALYT 200
QEVNPSVEKC GKENLAFFTL PTQFGTYECK LHLVASCYFI YDSKEVYNKR 250
GCDNYFQVIY DSSGKVVGGL DNRVSPYTGN SGDTPTMQCD MLQLKPGRYS 300
VRSSPRFLLM PERSYCFDMK EKGPVTAVQS IWGKGRESDH AVDQACLSTP 350
GCMLIQKQKP YIGEADDHHG DQEMRELLSG LDYEARCISQ SGWVNETSPF 400
TEEYLLPPKF GRCPLAAKEE SIPKIPDGLL IPTSGTDTTV TKPKSRIFGI 450
DDLIIGLLFV AIVEAGIGGY LLGSRKVSGG GVTKESAEKG FEKIGNDIQI 500
LRSSTNIAIE KLNDRISHDE QAIRDLTLEI ENARSEALLG ELGIIRALLV 550
GNISIGLQES LWELASEITN RAGDLAVEVS PGCWVIDNNI CDQSCQNFIF 600
KFNETAPVPT IPPLDTKIDL QSDPFYWGSS LGLAITAAIS LAALVISGIA 650
ICRTK 655
Length:655
Mass (Da):71,956
Last modified:December 12, 2006 - v2
Checksum:i81869FEDA9CD8943
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2093VEK → EEI in AAA43782. 1 Publication
Sequence conflicti214 – 2141N → Y in AAA43782. 1 Publication
Sequence conflicti263 – 2631S → Y in AAA43782. 1 Publication
Sequence conflicti324 – 3241P → L in AAA43782. 1 Publication
Sequence conflicti346 – 3461C → Y in AAA43782. 1 Publication
Sequence conflicti458 – 4581L → F in AAA43782. 1 Publication
Sequence conflicti477 – 4771V → E in AAA43782. 1 Publication
Sequence conflicti637 – 6382AA → TP in AAA43782. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB126194 Genomic RNA. Translation: BAD24940.1.
M11638 Genomic RNA. Translation: AAA43782.1.
RefSeqiYP_089655.1. NC_006310.1.

Genome annotation databases

GeneIDi3077359.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB126194 Genomic RNA. Translation: BAD24940.1 .
M11638 Genomic RNA. Translation: AAA43782.1 .
RefSeqi YP_089655.1. NC_006310.1.

3D structure databases

ProteinModelPortali P68762.
SMRi P68762. Positions 15-441, 450-611.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3077359.

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. "Identification of an amino acid residue on influenza C virus M1 protein responsible for formation of the cord-like structures of the virus."
    Muraki Y., Washioka H., Sugawara K., Matsuzaki Y., Takashita E., Hongo S.
    J. Gen. Virol. 85:1885-1893(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Noncumulative sequence changes in the hemagglutinin genes of influenza C virus isolates."
    Buonagurio D.A., Nakada S., Desselberger U., Krystal M., Palese P.
    Virology 146:221-232(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 14-655.

Entry informationi

Entry nameiHEMA_INCAA
AccessioniPrimary (citable) accession number: P68762
Secondary accession number(s): P07969, Q6I7C1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi