P09612 · GP_BUNL7

Function

function

Glycoprotein C and Glycoprotein N interact with each other and are present at the surface of the virion. They are able to attach the virion to a cell receptor and to promote fusion of membranes after endocytosis of the virion (By similarity).

Features

Showing features for site.

114412004006008001,0001,2001,400
TypeIDPosition(s)Description
Site473-474Cleavage; by host signal peptidase

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componenthost cell endoplasmic reticulum membrane
Cellular Componenthost cell Golgi membrane
Cellular Componentmembrane
Cellular Componentvirion membrane
Biological Processfusion of virus membrane with host endosome membrane
Biological Processmodulation by virus of host process
Biological Processsymbiont entry into host cell
Biological Processvirion attachment to host cell

Keywords

Protein family/group databases

    • 1.G.20.1.4the hantavirus gc envelope fusion glycoprotein (gc-efg) family

Names & Taxonomy

Protein names

  • Recommended name
    Envelopment polyprotein
  • Alternative names
    • M polyprotein
  • Cleaved into 3 chains

Gene names

    • Name
      GP

Organism names

Accessions

  • Primary accession
    P09612

Subcellular Location

Glycoprotein C

Virion membrane
; Single-pass type I membrane protein
Host Golgi apparatus membrane
; Single-pass type I membrane protein
Host endoplasmic reticulum membrane
; Single-pass type I membrane protein
Note: Glycoprotein C alone is retained in the membrane of the endoplasmic reticulum, but not transported to the Golgi. Coexpression of Glycoprotein C and Glycoprotein N results in efficient transport of Glycoprotein C to the Golgi complex, indicating thattheir interaction is essential for proper targeting to this organelle, where virion budding occurs (By similarity).

Glycoprotein N

Virion membrane
; Single-pass type I membrane protein
Host Golgi apparatus membrane
; Single-pass type I membrane protein
Note: Glycoprotein N is retained in the Golgi complex through a Golgi retention signal, which resides in the Glycoprotein N transmembrane region.

Non-structural protein M

Host Golgi apparatus membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain14-200Lumenal
Transmembrane201-221Helical
Topological domain222-305Cytoplasmic
Transmembrane306-326Helical
Topological domain327-365Lumenal
Transmembrane366-386Helical
Topological domain387-452Cytoplasmic
Transmembrane453-473Helical
Topological domain474-1395Lumenal
Transmembrane1396-1416Helical
Topological domain1417-1441Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-13
ChainPRO_000003679014-1441Envelopment polyprotein
ChainPRO_000003679122-299Glycoprotein N
Glycosylation57N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000036792300-473Non-structural protein M
ChainPRO_0000036793474-1441Glycoprotein C
Glycosylation490N-linked (GlcNAc...) asparagine; by host
Glycosylation1177N-linked (GlcNAc...) asparagine; by host

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins including nonstructural protein NSm, glycoprotein C, and glycoprotein N.

Keywords

PTM databases

Interaction

Subunit

Glycoprotein C and Glycoprotein N interact with each other.

Structure

3D structure databases

Family & Domains

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,441
  • Mass (Da)
    162,541
  • Last updated
    1996-02-01 v3
  • Checksum
    50973CE30973C55B
MIRMLVLIVVTAASPVYQRCFQDGAIVKQNPSKEAVTEVCLKDDVSMIKTEARYVKNATGVFSNNVAIRKWLVSDWHDCRPKKIVGGHINVIEVGDDLSLHTESYVCSADCTIGVDKETAQVRLQTDTTNHFEIAGTTVKSGWFKSTTYITLDQTCEHLKVSCAPKSVQFHACFNQHMSCVRFLHRTILPGSIANSICQNIEIIILVTLTLLIFILLSILSKTYICYLLMPIFIPIAYMYGVIYNKSCKKCKLCGLVYHPFTECGTHCVCGARYDTSDRMKLHRASGLCPGYKSLRAARVMCKSKGPASILSIITAVLVLTFVTPINSMVLGESKETFELEELPDDMLEMALRINSYYFTCILNYAVSWGLIIAGLLVGLIFKKYQHRFLNIYAMYCEECNMYHDKSGLKRHGDFTNKCRQCTCGQYEDATGLITHRKTYNCLVQYKAKWMMNFLIIYIFLILIKDSAIVGQATGTDFTTCLETESINWNCTGPFLNLGNCQKQQKKEPYTNIATQLKGLKAISVLDIPIITSIPDDIAGALRYIEEKEDFHVQLTTEYAMLSKYCDYYTQFSDNSGYSQTTWRVYLRSHDFEACILYPNQHFCKCVKNGEKCSSSNWDFANGMKNYYSGKQAKFDKDLNLALTALHHAFRGTSSAYIAAMLSKKSNDDLIAYTNKIKAKFPGNALLKAIIDYIAYMKGLPEMANFKYDEFWDELLYKPNPAKASNLARGKESSYNFKLAISSKSIKTCKNVKDVACLSPRSGAIYSSIIACGEPNGPSVYRKPSGGVFQSSTDRSIYCLLDSHCLEEFEAISQEELDAVKKSKCWEIEYPDVRPLQESDGAKSCRMKDSGNCNVATNRWPVMQCENDKFYYSELQKDYDKTQDIGHYCLSPGCTTIRYPINPKHISNCNWQVSRSSIAKIDVHNVEDIEQYKKAITQKLQTSLSLFKYAKTKNLPHIRPIYKYITMKETETAEGIESAYIESEVPALAGTSVGFKINSKEGKHLLDVIAYVKSASYSSVYAKLYSTGPTSGINTKHDELCTGPCPANINHQVGWLTFARERTSSWGCEEFGCLAVSDGCVFGSCQDIIKEELSVYRKETEEVTNVELCLTFSDKTYCTNLNPVTPIITDLFEVQFKTVETYSLPRIVAVQNHEIKIGQINDLGVYSKGCGNVQKVNGTVYGNGVPRFDYLCHLASRKEVIVRKCFDNDYQACKFLQSPASYRLEEDSGTVTIIDYKKILGTIKMKAILGDVKYKTFADSVDITAEGSCAGCINCFQNIHCELTLHTTIEASCPIKSSCTVFHDRILVTPNEHKYALKIVCTEKPGNTLTIKVCNTRIEASMALVDAKPIIELAPVDQTAYIREKDERCKTWMCRVRDEGLQVILEPFKNLFGSYIGIFYTFIISIIALLVIIYVLLPICFKLRDTLRKHDDAYKREMKIR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict40in Ref. 2

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D10370
EMBL· GenBank· DDBJ
BAA01201.1
EMBL· GenBank· DDBJ
Genomic RNA
J02231
EMBL· GenBank· DDBJ
-Genomic RNA No translation available.

Similar Proteins

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