P10228 · GC_HHV11
- ProteinEnvelope glycoprotein C
- GenegC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids511 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Major attachment protein that mediates binding of the virus to cell surface heparan sulfate or chondroitin sulfate. Also plays several roles in host immune evasion by inhibiting the host complement cascade activation, and by providing a shield against neutralizing antibodies that interfere with gB-gD, gB-gH/gL or gD-gH/gL interactions (By similarity).
Miscellaneous
There are seven external glycoproteins in HSV-1 and 2: gH, gB, gC, gG, gD, gI, and gE.
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 | membrane | |
Cellular Component | virion membrane | |
Molecular Function | complement binding | |
Biological Process | adhesion receptor-mediated virion attachment to host cell | |
Biological Process | symbiont entry into host cell | |
Biological Process | symbiont-mediated suppression of host complement activation | |
Biological Process | virus-mediated perturbation of host defense response |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameEnvelope glycoprotein C
Gene names
Organism names
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Peploviricota > Herviviricetes > Herpesvirales > Orthoherpesviridae > Alphaherpesvirinae > Simplexvirus > Simplexvirus humanalpha1 > Human herpesvirus 1
- Virus hosts
Accessions
- Primary accessionP10228
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Virion membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 25-480 | Virion surface | ||||
Sequence: GSETASTGPTITAGAVTNASEAPTSGSPGSAASPEVTPTSTPNPNNVTQNKTTPTEPASPPTTPKPTSTPKSPPTSTPDPKPKNNTTPAKSGRPTKPPGPVWCDRRDPLARYGSRVQIRCRFRNSTRMEFRLQIWRYSMGPSPPIAPAPDLEEVLTNITAPPGGLLVYDSAPNLTDPHVLWAEGAGPGADPPLYSVTGPLPTQRLIIGEVTPATQGMYYLAWGRMDSPHEYGTWVRVRMFRPPSLTLQPHAVMEGQPFKATCTAAAYYPRNPVEFVWFEDDHQVFNPGQIDTQTHEHPDGFTTVSTVTSEAVGGQVPPRTFTCQMTWHRDSVTFSRRNATGLALVLPRPTITMEFGVRIVVCTAGCVPEGVTFAWFLGDDPSPAAKSAVTAQESCDHPGLATVRSTLPISYDYSEYICRLTGYPAGIPVLEHHGSHQPPPRDPTERQVIEAIEWVG | ||||||
Transmembrane | 481-497 | Helical | ||||
Sequence: IGIGVLAAGVLVVTAIV | ||||||
Topological domain | 498-511 | Cytoplasmic | ||||
Sequence: YVVRTSQSRQRHRR |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MAPGRVGLAVVLWSLLWLGAGVSG | ||||||
Chain | PRO_0000038197 | 25-511 | Envelope glycoprotein C | |||
Sequence: GSETASTGPTITAGAVTNASEAPTSGSPGSAASPEVTPTSTPNPNNVTQNKTTPTEPASPPTTPKPTSTPKSPPTSTPDPKPKNNTTPAKSGRPTKPPGPVWCDRRDPLARYGSRVQIRCRFRNSTRMEFRLQIWRYSMGPSPPIAPAPDLEEVLTNITAPPGGLLVYDSAPNLTDPHVLWAEGAGPGADPPLYSVTGPLPTQRLIIGEVTPATQGMYYLAWGRMDSPHEYGTWVRVRMFRPPSLTLQPHAVMEGQPFKATCTAAAYYPRNPVEFVWFEDDHQVFNPGQIDTQTHEHPDGFTTVSTVTSEAVGGQVPPRTFTCQMTWHRDSVTFSRRNATGLALVLPRPTITMEFGVRIVVCTAGCVPEGVTFAWFLGDDPSPAAKSAVTAQESCDHPGLATVRSTLPISYDYSEYICRLTGYPAGIPVLEHHGSHQPPPRDPTERQVIEAIEWVGIGIGVLAAGVLVVTAIVYVVRTSQSRQRHRR | ||||||
Glycosylation | 42 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 70 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 74 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 108 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 127↔144 | |||||
Sequence: CDRRDPLARYGSRVQIRC | ||||||
Glycosylation | 148 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 181 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 197 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 286↔347 | |||||
Sequence: CTAAAYYPRNPVEFVWFEDDHQVFNPGQIDTQTHEHPDGFTTVSTVTSEAVGGQVPPRTFTC | ||||||
Glycosylation | 362 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 386↔442 | |||||
Sequence: CTAGCVPEGVTFAWFLGDDPSPAAKSAVTAQESCDHPGLATVRSTLPISYDYSEYIC | ||||||
Disulfide bond | 390↔419 | |||||
Sequence: CVPEGVTFAWFLGDDPSPAAKSAVTAQESC |
Keywords
- PTM
PTM databases
Interaction
Subunit
Interacts with host complement component C3b; this interaction inhibits host immune response by disregulating complement cascade.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 42-80 | Polar residues | ||||
Sequence: NASEAPTSGSPGSAASPEVTPTSTPNPNNVTQNKTTPTE | ||||||
Region | 42-130 | Disordered | ||||
Sequence: NASEAPTSGSPGSAASPEVTPTSTPNPNNVTQNKTTPTEPASPPTTPKPTSTPKSPPTSTPDPKPKNNTTPAKSGRPTKPPGPVWCDRR | ||||||
Compositional bias | 81-105 | Pro residues | ||||
Sequence: PASPPTTPKPTSTPKSPPTSTPDPK | ||||||
Region | 137-151 | Heparin-binding domain | ||||
Sequence: GSRVQIRCRFRNSTR | ||||||
Domain | 267-359 | Ig-like | ||||
Sequence: PSLTLQPHAVMEGQPFKATCTAAAYYPRNPVEFVWFEDDHQVFNPGQIDTQTHEHPDGFTTVSTVTSEAVGGQVPPRTFTCQMTWHRDSVTFS |
Sequence similarities
Belongs to the herpesviridae glycoprotein C family.
Keywords
- Domain
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing & Alternative initiation.
P10228-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NamegC
- NoteMembrane-bound gC.
- Length511
- Mass (Da)54,998
- Last updated1989-07-01 v1
- Checksum874BE474DC7D71C5
P10228-2
- NamegCsec
- NoteSecreted.
- Differences from canonical
- 472-511: VIEAIEWVGIGIGVLAAGVLVVTAIVYVVRTSQSRQRHRR → VILGRSRTTHGVEQNASP
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 42-80 | Polar residues | ||||
Sequence: NASEAPTSGSPGSAASPEVTPTSTPNPNNVTQNKTTPTE | ||||||
Compositional bias | 81-105 | Pro residues | ||||
Sequence: PASPPTTPKPTSTPKSPPTSTPDPK | ||||||
Alternative sequence | VSP_040892 | 472-511 | in isoform gCsec | |||
Sequence: VIEAIEWVGIGIGVLAAGVLVVTAIVYVVRTSQSRQRHRR → VILGRSRTTHGVEQNASP |
Keywords
- Coding sequence diversity
- Technical term