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P17004

- HEMA_INCKY

UniProt

P17004 - HEMA_INCKY

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Protein

Hemagglutinin-esterase-fusion glycoprotein

Gene

HE

Organism
Influenza C virus (strain C/Kyoto/41/1982)
Status
Reviewed - Annotation score: 3 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 sitei57 – 571NucleophileBy similarity
Active sitei352 – 3521Charge relay systemBy similarity
Active sitei355 – 3551Charge 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/Kyoto/41/1982)
Taxonomic identifieri203233 [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 – 616616ExtracellularSequence AnalysisAdd
BLAST
Transmembranei617 – 63721HelicalSequence AnalysisAdd
BLAST
Topological domaini638 – 6414CytoplasmicSequence Analysis

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
Chaini1 – 432432Hemagglutinin-esterase-fusion glycoprotein chain 1PRO_0000039154Add
BLAST
Chaini433 – 641209Hemagglutinin-esterase-fusion glycoprotein chain 2PRO_0000039155Add
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 hostSequence Analysis
Glycosylationi47 – 471N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi106 ↔ 151By similarity
Disulfide bondi126 ↔ 174By similarity
Glycosylationi130 – 1301N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi196 ↔ 238By similarity
Disulfide bondi215 ↔ 302By similarity
Disulfide bondi223 ↔ 275By similarity
Disulfide bondi332 ↔ 338By similarity
Glycosylationi381 – 3811N-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

ProteinModelPortaliP17004.
SMRiP17004. Positions 436-597.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

P17004-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
EKIKICLQKQ VNSSFSLHNG FGGNLYATEE KRMFELVKPK AGASVLNQST
60 70 80 90 100
WIGFGDSRTD KSNPNFPRSA DVSVKTANKF RSLTGGSLML SMFGPPGKVD
110 120 130 140 150
YLYQGCGKHK VFYEGVNWSP HAAIDCYRKN WTDIKLNFQK NIYELASQSH
160 170 180 190 200
CMSLVNALDK TIPLQATAGV AGNCNNSFLK NPALYTQKVT PPXXKCGKEN
210 220 230 240 250
LAFFTLPTQF GTYECRLHLV ASCYFIYDSK EVYNKRGCDN YFQVIYDSSG
260 270 280 290 300
KVVGGLDNRV SPYTGNSGDT PTMQCDMIQL KPGRYSVRSS PRFLLMPERS
310 320 330 340 350
YCFDMKEKGP VTAVQSIWGK DRKSDYAVDQ ACLSTPGCML IQKQKPYTGE
360 370 380 390 400
ADDHHGDQEM RELLSGLDYE ARCISQSGWV NETSPFTEEY LLPPKFGRCP
410 420 430 440 450
LAAKEESIPK IPDGLLIPTS GTDTTVTKPK SRIFGIDDLI IGLLFVAIVE
460 470 480 490 500
AGIGGYLLGS RKESGGGVTK ESAEKGFEKI GNDIQILRSS TNIAIEKLND
510 520 530 540 550
RISHDEQAIR DLTLEIENAR SEALLGELGI IRALLVGNIS IGLQESLWEL
560 570 580 590 600
ASEITNRAGD LAVEISPGCW IIDNNICDQS CQNFIFKFNE TAPVPTIPPL
610 620 630 640
DTKIDLQSDP FYWGSSLGLA ITAAISLAAL VISGIAICRT K
Length:641
Mass (Da):70,560
Last modified:August 1, 1990 - v1
Checksum:iB8A09536CB11B62E
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25361 Genomic RNA. Translation: AAA43789.1.
PIRiA32665. HMIVEA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25361 Genomic RNA. Translation: AAA43789.1 .
PIRi A32665. HMIVEA.

3D structure databases

ProteinModelPortali P17004.
SMRi P17004. 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_INCKY
AccessioniPrimary (citable) accession number: P17004
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: October 29, 2014
This is version 91 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