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Protein

Hemagglutinin-neuraminidase

Gene

HN

Organism
Mumps virus (strain SBL-1) (MuV)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).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 activityi

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin, Hydrolase

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Virus entry into host cell

Protein family/group databases

CAZyiGH83. Glycoside Hydrolase Family 83.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemagglutinin-neuraminidase (EC:3.2.1.18)
Gene namesi
Name:HN
OrganismiMumps virus (strain SBL-1) (MuV)
Taxonomic identifieri11173 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeRubulavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3434IntravirionSequence AnalysisAdd
BLAST
Transmembranei35 – 5521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini56 – 582527Virion surfaceSequence AnalysisAdd
BLAST

GO - Cellular componenti

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 – 582582Hemagglutinin-neuraminidasePRO_0000142605Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi284 – 2841N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi329 – 3291N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi400 – 4001N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi448 – 4481N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi507 – 5071N-linked (GlcNAc...); by hostSequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP19762.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR016285. Hemagglutn-neuramid.
IPR000665. Hemagglutn/HN.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00423. HN. 1 hit.
[Graphical view]
PIRSFiPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

P19762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPSKLFIMS DNATVAPGPV VNAAGKKTFR TCFRILVLSV QAVTLILVIV
60 70 80 90 100
TLGELIRMIN DQGLSNQLSS ITDKIRESAA VIASAVGVMN QVIHGVTVSL
110 120 130 140 150
PLQIEGNQNQ LLSTLATICT NRNQVSNCST NIPLVNDLRF INGINKFIIE
160 170 180 190 200
DYATHDFSIG NPLNMPSFIP TATSPNGCTR IPSFSLGKTH WCYTHNVINA
210 220 230 240 250
NCKDHTSSNQ YVSMGILVQT ASGYPMFKTL KIQYLSDGLN RKSCSIATVP
260 270 280 290 300
DGCAMYCYVS TQLEANDYAG SSPPTQKLTL LFYNDTITER TISPSGLEGN
310 320 330 340 350
WATLVPGVGS GIYFENKLIF PAYGGVLPNS TLGVKSAREF FRPVNPYNPC
360 370 380 390 400
SGPPQELDQR ALRSYFPRYF SSRRVQSAFL VCAWNQILVT NCELVVPSNN
410 420 430 440 450
QTLMGAEGRV LLINNRLLYY QRSTSWWPYE LLYEISFTFT NSGQSSVNMS
460 470 480 490 500
WIPIYSFTPP GSGNCSGKNV CPTVCVSGVY LDPWPLTPYS HQSGINRNFY
510 520 530 540 550
FTGALLNSST TRVNPTLYVS ALNNLKVLAP YGTQGLFASY TTTTCFQDTG
560 570 580
DASVYCVYIM ELASNIVGEF QILPVLARLT IT
Length:582
Mass (Da):63,885
Last modified:February 1, 1991 - v1
Checksum:i18F95300AA33DC7F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55065 Genomic RNA. Translation: AAA74751.1.
D00663 Genomic RNA. Translation: BAA00563.1.
PIRiA42758. HNNZSB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55065 Genomic RNA. Translation: AAA74751.1.
D00663 Genomic RNA. Translation: BAA00563.1.
PIRiA42758. HNNZSB.

3D structure databases

ProteinModelPortaliP19762.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH83. Glycoside Hydrolase Family 83.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR016285. Hemagglutn-neuramid.
IPR000665. Hemagglutn/HN.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00423. HN. 1 hit.
[Graphical view]
PIRSFiPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete nucleotide sequence of the hemagglutinin-neuraminidase (HN) mRNA of mumps virus and comparison of paramyxovirus HN proteins."
    Koevamees J., Norrby E., Elango N.
    Virus Res. 12:87-96(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Strain-variable editing during transcription of the P gene of mumps virus may lead to the generation of non-structural proteins NS1 (V) and NS2."
    Elliott G.D., Yeo R.P., Afzal M.A., Simpson E.J.B., Curran J.A., Rima B.K.
    J. Gen. Virol. 71:1555-1560(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-153.

Entry informationi

Entry nameiHN_MUMP1
AccessioniPrimary (citable) accession number: P19762
Secondary accession number(s): P33480
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 27, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.