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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711NucleophileBy similarity
Active sitei366 – 3661Charge relay systemBy similarity
Active sitei369 – 3691Charge relay systemBy 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

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
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 – 1414By 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 hostSequence Analysis
Glycosylationi61 – 611N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi120 ↔ 165By similarity
Disulfide bondi140 ↔ 188By similarity
Glycosylationi144 – 1441N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi210 ↔ 252By similarity
Disulfide bondi229 ↔ 316By similarity
Disulfide bondi237 ↔ 289By similarity
Glycosylationi395 – 3951N-linked (GlcNAc...); by hostSequence Analysis

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.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini15 – 630616ExtracellularSequence AnalysisAdd
BLAST
Topological domaini652 – 6554CytoplasmicSequence Analysis

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei631 – 65121HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

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

        10         20         30         40         50
MFFSLLLMLG LTEAEKIKIC LQKQVNSSFS LHNGFGGNLY ATEEKRMFEL
60 70 80 90 100
VKPKAGASVL NQSTWIGFGD SRTDKSNSAF PRSADVSAKT ADKFRSLSGG
110 120 130 140 150
SLMLSMFGPP GKVDYLYQGC GKHKVFYEGV NWSPHAAINC YRKNWTDIKL
160 170 180 190 200
NFQKNIYELA SQSHCMSLVN ALDKTIPLQA TAGVAKNCNN SFLKNPALYT
210 220 230 240 250
QEVNPSVEKC GKENLAFFTL PTQFGTYECK LHLVASCYFI YDSKEVYNKR
260 270 280 290 300
GCDNYFQVIY DSSGKVVGGL DNRVSPYTGN SGDTPTMQCD MLQLKPGRYS
310 320 330 340 350
VRSSPRFLLM PERSYCFDMK EKGPVTAVQS IWGKGRESDH AVDQACLSTP
360 370 380 390 400
GCMLIQKQKP YIGEADDHHG DQEMRELLSG LDYEARCISQ SGWVNETSPF
410 420 430 440 450
TEEYLLPPKF GRCPLAAKEE SIPKIPDGLL IPTSGTDTTV TKPKSRIFGI
460 470 480 490 500
DDLIIGLLFV AIVEAGIGGY LLGSRKVSGG GVTKESAEKG FEKIGNDIQI
510 520 530 540 550
LRSSTNIAIE KLNDRISHDE QAIRDLTLEI ENARSEALLG ELGIIRALLV
560 570 580 590 600
GNISIGLQES LWELASEITN RAGDLAVEVS PGCWVIDNNI CDQSCQNFIF
610 620 630 640 650
KFNETAPVPT IPPLDTKIDL QSDPFYWGSS LGLAITAAIS LAALVISGIA

ICRTK
Length:655
Mass (Da):71,956
Last modified:December 12, 2006 - v2
Checksum:i81869FEDA9CD8943
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2093VEK → EEI in AAA43782. (PubMed:3855244)Curated
Sequence conflicti214 – 2141N → Y in AAA43782. (PubMed:3855244)Curated
Sequence conflicti263 – 2631S → Y in AAA43782. (PubMed:3855244)Curated
Sequence conflicti324 – 3241P → L in AAA43782. (PubMed:3855244)Curated
Sequence conflicti346 – 3461C → Y in AAA43782. (PubMed:3855244)Curated
Sequence conflicti458 – 4581L → F in AAA43782. (PubMed:3855244)Curated
Sequence conflicti477 – 4771V → E in AAA43782. (PubMed:3855244)Curated
Sequence conflicti637 – 6382AA → TP in AAA43782. (PubMed:3855244)Curated

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: October 29, 2014
This is version 59 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