Hemagglutinin-neuraminidase - Sendai virus (strain Harris) (SeV)

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P03425 (HN_SENDH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Hemagglutinin-neuraminidase
Short name=HN protein
EC=3.2.1.18

Gene names

Name:

Organism

Sendai virus (strain Harris) (SeV)

Taxonomic identifier

11196 [NCBI]

Taxonomic lineage

Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Respirovirus ›

Virus host

Cavia cutleri (Guinea pig) [TaxID: 10144]
Cricetidae sp. (Hamster) [TaxID: 36483]
Mus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]

Protein attributes

Sequence length	576 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion By similarity. Neuraminidase activity ensures the efficient spread of the virus by dissociating the mature virions from the neuraminic acid containing glycoproteins By similarity.
Catalytic activity	Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Subunit structure	Homotetramer; composed of disulfide-linked homodimers. Interacts with F protein trimer By similarity.
Subcellular location	Virion membrane; Single-pass type II membrane protein Potential. Host cell membrane; Single-pass type II membrane protein Potential. Note: Folded in the endoplasmic reticulum By similarity.
Post-translational modification	N-glycosylated; glycans consist of a mixture of high mannose-type oligosaccharides and of complex-type oligosaccharides By similarity.
Sequence similarities	Belongs to the paramyxoviruses hemagglutinin-neuraminidase family.

Ontologies

Keywords
Biological process	Host-virus interaction Viral attachment to host cell Virus entry into host cell
Cellular component	Host cell membrane Host membrane Membrane Viral envelope protein Virion
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Hemagglutinin Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological_process	viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell Inferred from electronic annotation. Source: UniProtKB-KW viral infectious cycle Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: UniProtKB-KW virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	exo-alpha-(2->3)-sialidase activity Inferred from electronic annotation. Source: EC exo-alpha-(2->6)-sialidase activity Inferred from electronic annotation. Source: EC exo-alpha-(2->8)-sialidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 576

576

Hemagglutinin-neuraminidase

PRO_0000142638

Regions

Topological domain

1 – 37

Intravirion By similarity

Transmembrane

38 – 58

Helical; By similarity

Topological domain

59 – 576

518

Virion surface By similarity

Region

10 – 14

Incorporation in virion By similarity

Region

59 – 140

Involved in interaction with F protein By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...); by host By similarity

Glycosylation

499

N-linked (GlcNAc...); by host By similarity

Glycosylation

511

N-linked (GlcNAc...); by host By similarity

Disulfide bond

129

Interchain Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P03425 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 01CD8067E038FC5B
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FASTA

576

63,515

        10         20         30         40         50         60 
MDGDRGKRDS YWSTSPSGST TKLASGWERS SKVDTWLLIL SFTQWALSIA TVIICIIISA 

        70         80         90        100        110        120 
RQGYSTKEYS MTVEALNMSS REVKESLTSL IRQEVIARAV NIQSSVQTGI PVLLNKNSRD 

       130        140        150        160        170        180 
VIQMIDKSCS RQELTQLCES TIAVHHAEGI APLEPHSFWR CPVGEPYLSS DPKISLLLGP 

       190        200        210        220        230        240 
SLLSGSTTIS GCVRLPSLSI GEAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMFPD 

       250        260        270        280        290        300 
LNPVVSHTYD INDNRKSCSV VATGTRGYQL CSMPTVDERT DYSSDGIEDL VLDVLDLKGS 

       310        320        330        340        350        360 
TKSHRYRNSE VDLDHPFSAL YPSVGNGIAT EGSLIFLGYG GLTTPLQGDT KCRTQGCQQV 

       370        380        390        400        410        420 
SQDTCNEALK ITWLGGKQVV NVIIRVNDYL SERPKIRVTT IPITQNYLGA EGRLLKLGDR 

       430        440        450        460        470        480 
VYIYTRSSGW HSQLQIGVLD VSHPLTINWT PHEALSRPGN KECNWYNTCP KECISGVYTD 

       490        500        510        520        530        540 
AYPLSPDAAN VATVTLYANT SRVNPTIMYS NTTNIINMLR IKDVQLEVAY TTISSCITHF 

       550        560        570 
GKGYCFHIIE INQKSLNTLQ PMLFKTSIPK LCKAES

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References

[1]	"Sequence determination of the Sendai virus HN gene and its comparison to the influenza virus glycoproteins." Blumberg B.M., Giorgi C., Roux L., Raju R., Dowling P., Chollet A., Kolakofsky D. Cell 41:269-278(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M12397 Genomic RNA. Translation: AAA47810.1.
PIR	HNNZS. A00877.
3D structure databases
ProteinModelPortal	P03425.
SMR	P03425. Positions 144-573.
ModBase	Search...
Protein family/group databases
CAZy	GH83. Glycoside Hydrolase Family 83.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.120.10.10. 1 hit.
InterPro	IPR000665. Hemagglutn-neuramid. IPR016285. Hemagglutn-neuramid_paramyxo. IPR011040. Sialidases. [Graphical view]
Pfam	PF00423. HN. 1 hit. [Graphical view]
PIRSF	PIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAM	SSF50939. Sialidase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HN_SENDH

Accession

Primary (citable) accession number: P03425

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents