P09612 · GP_BUNL7
- ProteinEnvelopment polyprotein
- GeneGP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1441 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 473-474 | Cleavage; by host signal peptidase | ||||
Sequence: AT |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | host cell endoplasmic reticulum membrane | |
Cellular Component | host cell Golgi membrane | |
Cellular Component | membrane | |
Cellular Component | virion membrane | |
Biological Process | fusion of virus membrane with host endosome membrane | |
Biological Process | modulation by virus of host process | |
Biological Process | symbiont entry into host cell | |
Biological Process | virion attachment to host cell |
Keywords
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEnvelopment polyprotein
- Alternative names
- Cleaved into 3 chains
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Polyploviricotina > Ellioviricetes > Bunyavirales > Peribunyaviridae > Orthobunyavirus > Orthobunyavirus lacrosseense
- Virus hosts
Accessions
- Primary accessionP09612
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 14-200 | Lumenal | ||||
Sequence: SPVYQRCFQDGAIVKQNPSKEAVTEVCLKDDVSMIKTEARYVKNATGVFSNNVAIRKWLVSDWHDCRPKKIVGGHINVIEVGDDLSLHTESYVCSADCTIGVDKETAQVRLQTDTTNHFEIAGTTVKSGWFKSTTYITLDQTCEHLKVSCAPKSVQFHACFNQHMSCVRFLHRTILPGSIANSICQN | ||||||
Transmembrane | 201-221 | Helical | ||||
Sequence: IEIIILVTLTLLIFILLSILS | ||||||
Topological domain | 222-305 | Cytoplasmic | ||||
Sequence: KTYICYLLMPIFIPIAYMYGVIYNKSCKKCKLCGLVYHPFTECGTHCVCGARYDTSDRMKLHRASGLCPGYKSLRAARVMCKSK | ||||||
Transmembrane | 306-326 | Helical | ||||
Sequence: GPASILSIITAVLVLTFVTPI | ||||||
Topological domain | 327-365 | Lumenal | ||||
Sequence: NSMVLGESKETFELEELPDDMLEMALRINSYYFTCILNY | ||||||
Transmembrane | 366-386 | Helical | ||||
Sequence: AVSWGLIIAGLLVGLIFKKYQ | ||||||
Topological domain | 387-452 | Cytoplasmic | ||||
Sequence: HRFLNIYAMYCEECNMYHDKSGLKRHGDFTNKCRQCTCGQYEDATGLITHRKTYNCLVQYKAKWMM | ||||||
Transmembrane | 453-473 | Helical | ||||
Sequence: NFLIIYIFLILIKDSAIVGQA | ||||||
Topological domain | 474-1395 | Lumenal | ||||
Sequence: TGTDFTTCLETESINWNCTGPFLNLGNCQKQQKKEPYTNIATQLKGLKAISVLDIPIITSIPDDIAGALRYIEEKEDFHVQLTTEYAMLSKYCDYYTQFSDNSGYSQTTWRVYLRSHDFEACILYPNQHFCKCVKNGEKCSSSNWDFANGMKNYYSGKQAKFDKDLNLALTALHHAFRGTSSAYIAAMLSKKSNDDLIAYTNKIKAKFPGNALLKAIIDYIAYMKGLPEMANFKYDEFWDELLYKPNPAKASNLARGKESSYNFKLAISSKSIKTCKNVKDVACLSPRSGAIYSSIIACGEPNGPSVYRKPSGGVFQSSTDRSIYCLLDSHCLEEFEAISQEELDAVKKSKCWEIEYPDVRPLQESDGAKSCRMKDSGNCNVATNRWPVMQCENDKFYYSELQKDYDKTQDIGHYCLSPGCTTIRYPINPKHISNCNWQVSRSSIAKIDVHNVEDIEQYKKAITQKLQTSLSLFKYAKTKNLPHIRPIYKYITMKETETAEGIESAYIESEVPALAGTSVGFKINSKEGKHLLDVIAYVKSASYSSVYAKLYSTGPTSGINTKHDELCTGPCPANINHQVGWLTFARERTSSWGCEEFGCLAVSDGCVFGSCQDIIKEELSVYRKETEEVTNVELCLTFSDKTYCTNLNPVTPIITDLFEVQFKTVETYSLPRIVAVQNHEIKIGQINDLGVYSKGCGNVQKVNGTVYGNGVPRFDYLCHLASRKEVIVRKCFDNDYQACKFLQSPASYRLEEDSGTVTIIDYKKILGTIKMKAILGDVKYKTFADSVDITAEGSCAGCINCFQNIHCELTLHTTIEASCPIKSSCTVFHDRILVTPNEHKYALKIVCTEKPGNTLTIKVCNTRIEASMALVDAKPIIELAPVDQTAYIREKDERCKTWMCRVRDEGLQVILEPFKNLFGSY | ||||||
Transmembrane | 1396-1416 | Helical | ||||
Sequence: IGIFYTFIISIIALLVIIYVL | ||||||
Topological domain | 1417-1441 | Cytoplasmic | ||||
Sequence: LPICFKLRDTLRKHDDAYKREMKIR |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-13 | |||||
Sequence: MIRMLVLIVVTAA | ||||||
Chain | PRO_0000036790 | 14-1441 | Envelopment polyprotein | |||
Sequence: SPVYQRCFQDGAIVKQNPSKEAVTEVCLKDDVSMIKTEARYVKNATGVFSNNVAIRKWLVSDWHDCRPKKIVGGHINVIEVGDDLSLHTESYVCSADCTIGVDKETAQVRLQTDTTNHFEIAGTTVKSGWFKSTTYITLDQTCEHLKVSCAPKSVQFHACFNQHMSCVRFLHRTILPGSIANSICQNIEIIILVTLTLLIFILLSILSKTYICYLLMPIFIPIAYMYGVIYNKSCKKCKLCGLVYHPFTECGTHCVCGARYDTSDRMKLHRASGLCPGYKSLRAARVMCKSKGPASILSIITAVLVLTFVTPINSMVLGESKETFELEELPDDMLEMALRINSYYFTCILNYAVSWGLIIAGLLVGLIFKKYQHRFLNIYAMYCEECNMYHDKSGLKRHGDFTNKCRQCTCGQYEDATGLITHRKTYNCLVQYKAKWMMNFLIIYIFLILIKDSAIVGQATGTDFTTCLETESINWNCTGPFLNLGNCQKQQKKEPYTNIATQLKGLKAISVLDIPIITSIPDDIAGALRYIEEKEDFHVQLTTEYAMLSKYCDYYTQFSDNSGYSQTTWRVYLRSHDFEACILYPNQHFCKCVKNGEKCSSSNWDFANGMKNYYSGKQAKFDKDLNLALTALHHAFRGTSSAYIAAMLSKKSNDDLIAYTNKIKAKFPGNALLKAIIDYIAYMKGLPEMANFKYDEFWDELLYKPNPAKASNLARGKESSYNFKLAISSKSIKTCKNVKDVACLSPRSGAIYSSIIACGEPNGPSVYRKPSGGVFQSSTDRSIYCLLDSHCLEEFEAISQEELDAVKKSKCWEIEYPDVRPLQESDGAKSCRMKDSGNCNVATNRWPVMQCENDKFYYSELQKDYDKTQDIGHYCLSPGCTTIRYPINPKHISNCNWQVSRSSIAKIDVHNVEDIEQYKKAITQKLQTSLSLFKYAKTKNLPHIRPIYKYITMKETETAEGIESAYIESEVPALAGTSVGFKINSKEGKHLLDVIAYVKSASYSSVYAKLYSTGPTSGINTKHDELCTGPCPANINHQVGWLTFARERTSSWGCEEFGCLAVSDGCVFGSCQDIIKEELSVYRKETEEVTNVELCLTFSDKTYCTNLNPVTPIITDLFEVQFKTVETYSLPRIVAVQNHEIKIGQINDLGVYSKGCGNVQKVNGTVYGNGVPRFDYLCHLASRKEVIVRKCFDNDYQACKFLQSPASYRLEEDSGTVTIIDYKKILGTIKMKAILGDVKYKTFADSVDITAEGSCAGCINCFQNIHCELTLHTTIEASCPIKSSCTVFHDRILVTPNEHKYALKIVCTEKPGNTLTIKVCNTRIEASMALVDAKPIIELAPVDQTAYIREKDERCKTWMCRVRDEGLQVILEPFKNLFGSYIGIFYTFIISIIALLVIIYVLLPICFKLRDTLRKHDDAYKREMKIR | ||||||
Chain | PRO_0000036791 | 22-299 | Glycoprotein N | |||
Sequence: QDGAIVKQNPSKEAVTEVCLKDDVSMIKTEARYVKNATGVFSNNVAIRKWLVSDWHDCRPKKIVGGHINVIEVGDDLSLHTESYVCSADCTIGVDKETAQVRLQTDTTNHFEIAGTTVKSGWFKSTTYITLDQTCEHLKVSCAPKSVQFHACFNQHMSCVRFLHRTILPGSIANSICQNIEIIILVTLTLLIFILLSILSKTYICYLLMPIFIPIAYMYGVIYNKSCKKCKLCGLVYHPFTECGTHCVCGARYDTSDRMKLHRASGLCPGYKSLRAAR | ||||||
Glycosylation | 57 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Chain | PRO_0000036792 | 300-473 | Non-structural protein M | |||
Sequence: VMCKSKGPASILSIITAVLVLTFVTPINSMVLGESKETFELEELPDDMLEMALRINSYYFTCILNYAVSWGLIIAGLLVGLIFKKYQHRFLNIYAMYCEECNMYHDKSGLKRHGDFTNKCRQCTCGQYEDATGLITHRKTYNCLVQYKAKWMMNFLIIYIFLILIKDSAIVGQA | ||||||
Chain | PRO_0000036793 | 474-1441 | Glycoprotein C | |||
Sequence: TGTDFTTCLETESINWNCTGPFLNLGNCQKQQKKEPYTNIATQLKGLKAISVLDIPIITSIPDDIAGALRYIEEKEDFHVQLTTEYAMLSKYCDYYTQFSDNSGYSQTTWRVYLRSHDFEACILYPNQHFCKCVKNGEKCSSSNWDFANGMKNYYSGKQAKFDKDLNLALTALHHAFRGTSSAYIAAMLSKKSNDDLIAYTNKIKAKFPGNALLKAIIDYIAYMKGLPEMANFKYDEFWDELLYKPNPAKASNLARGKESSYNFKLAISSKSIKTCKNVKDVACLSPRSGAIYSSIIACGEPNGPSVYRKPSGGVFQSSTDRSIYCLLDSHCLEEFEAISQEELDAVKKSKCWEIEYPDVRPLQESDGAKSCRMKDSGNCNVATNRWPVMQCENDKFYYSELQKDYDKTQDIGHYCLSPGCTTIRYPINPKHISNCNWQVSRSSIAKIDVHNVEDIEQYKKAITQKLQTSLSLFKYAKTKNLPHIRPIYKYITMKETETAEGIESAYIESEVPALAGTSVGFKINSKEGKHLLDVIAYVKSASYSSVYAKLYSTGPTSGINTKHDELCTGPCPANINHQVGWLTFARERTSSWGCEEFGCLAVSDGCVFGSCQDIIKEELSVYRKETEEVTNVELCLTFSDKTYCTNLNPVTPIITDLFEVQFKTVETYSLPRIVAVQNHEIKIGQINDLGVYSKGCGNVQKVNGTVYGNGVPRFDYLCHLASRKEVIVRKCFDNDYQACKFLQSPASYRLEEDSGTVTIIDYKKILGTIKMKAILGDVKYKTFADSVDITAEGSCAGCINCFQNIHCELTLHTTIEASCPIKSSCTVFHDRILVTPNEHKYALKIVCTEKPGNTLTIKVCNTRIEASMALVDAKPIIELAPVDQTAYIREKDERCKTWMCRVRDEGLQVILEPFKNLFGSYIGIFYTFIISIIALLVIIYVLLPICFKLRDTLRKHDDAYKREMKIR | ||||||
Glycosylation | 490 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 1177 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N |
Post-translational modification
Specific enzymatic cleavages in vivo yield mature proteins including nonstructural protein NSm, glycoprotein C, and glycoprotein N.
Keywords
- PTM
PTM databases
Interaction
Subunit
Glycoprotein C and Glycoprotein N interact with each other.
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,441
- Mass (Da)162,541
- Last updated1996-02-01 v3
- Checksum50973CE30973C55B
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 40 | in Ref. 2 | ||||
Sequence: C → S |