P16729 · MCP_HCMVA
- ProteinMajor capsid protein
- GeneMCP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1370 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
function
Self-assembles to form an icosahedral capsid with a T=16 symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12 pentons (total of 162 capsomers). Hexons form the edges and faces of the capsid and are each composed of six MCP molecules. In contrast, one penton is found at each of the 12 vertices. Eleven of the pentons are MCP pentamers, while the last vertex is occupied by the portal complex. The capsid is surrounded by a layer of proteinaceous material designated the tegument which, in turn, is enclosed in an envelope of host cell-derived lipids containing virus-encoded glycoproteins.
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 nucleus | |
Cellular Component | T=16 icosahedral viral capsid | |
Molecular Function | structural molecule activity |
Names & Taxonomy
Protein names
- Recommended nameMajor capsid protein
- Short namesMCP
Gene names
Organism names
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Peploviricota > Herviviricetes > Herpesvirales > Orthoherpesviridae > Betaherpesvirinae > Cytomegalovirus > Cytomegalovirus humanbeta5 > Human cytomegalovirus
- Virus hosts
Accessions
- Primary accessionP16729
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000115711 | 1-1370 | Major capsid protein | |||
Sequence: MENWSALELLPKVGIPTDFLTHVKTSAGEEMFEALRIYYGDDPERYNIHFEAIFGTFCNRLEWVYFLTSGLAAAAHAIKFHDLNKLTTGKMLFHVQVPRVASGAGLPTSRQTTIMVTKYSEKSPITIPFELSAACLTYLRETFEGTILDKILNVEAMHTVLRALKNTADAMERGLIHSFLQTLLRKAPPYFVVQTLVENATLARQALNRIQRSNILQSFKAKMLATLFLLNRTRDRDYVLKFLTRLAEAATDSILDNPTTYTTSSGAKISGVMVSTANVMQIIMSLLSSHITKETVSAPATYGNFVLSPENAVTAISYHSILADFNSYKAHLTSGQPHLPNDSLSQAGAHSLTPLSMDVIRLGEKTVIMENLRRVYKNTDTKDPLERNVDLTFFFPVGLYLPEDRGYTTVESKVKLNDTVRNALPTTAYLLNRDRAVQKIDFVDALKTLCHPVLHEPAPCLQTFTERGPPSEPAMQRLLECRFQQEPMGGAARRIPHFYRVRREVPRTVNEMKQDFVVTDFYKVGNITLYTELHPFFDFTHCQENSETVALCTPRIVIGNLPDGLAPGPFHELRTWEIMEHMRLRPPPDYEETLRLFKTTVTSPNYPELCYLVDVLVHGNVDAFLLIRTFVARCIVNMFHTRQLLVFAHSYALVTLIAEHLADGALPPQLLFHYRNLVAVLRLVTRISALPGLNNGQLAEEPLSAYVNALHDHRLWPPFVTHLPRNMEGVQVVADRQPLNPANIEARHHGVSDVPRLGAMDADEPLFVDDYRATDDEWTLQKVFYLCLMPAMTNNRACGLGLNLKTLLVDLFYRPAFLLMPAATAVSTSGTTSKESTSGVTPEDSIAAQRQAVGEMLTELVEDVATDAHTPLLQACRELFLAVQFVGEHVKVLEVRAPLDHAQRQGLPDFISRQHVLYNGCCVVTAPKTLIEYSLPVPFHRFYSNPTICAALSDDIKRYVTEFPHYHRHDGGFPLPTAFAHEYHNWLRSPFSRYSATCPNVLHSVMTLAAMLYKISPVSLVLQTKAHIHPGFALTAVRTDTFEVDMLLYSGKSCTSVIINNPIVTKEERDISTTYHVTQNINTVDMGLGYTSNTCVAYVNRVRTDMGVRVQDLFRVFPMNVYRHDEVDRWIRHAAGVERPQLLDTETISMLTFGSMSERNAAATVHGQKAACELILTPVTMDVNYFKIPNNPRGRASCMLAVDPYDTEAATKAIYDHREADAQTFAATHNPWASQAGCLSDVLYNTRHRERLGYNSKFYSPCAQYFNTEEIIAANKTLFKTIDEYLLRAKDCIRGDTDTQYVCVEGTEQLIENPCRLTQEALPILSTTTLALMETKLKGGAGAFATSETHFGNYVVGEIIPLQQSMLFNS |
Interaction
Subunit
Homomultimer. Makes the hexons and eleven out of twelve pentons. Interacts with triplex proteins 1/TRX1 and 2/TRX2; adjacent capsomers are linked together in groups of three by triplexes, heterotrimeric complexes composed of one molecule of TRX1 and two molecules of TRX2. Interacts with scaffold protein; this interaction allows efficient MCP transport to the host nucleus. Interacts with capsid vertex component 2/CVC2. Interacts with the small capsomere-interacting protein/SCP.
Protein-protein interaction databases
Sequence
- Sequence statusComplete
- Length1,370
- Mass (Da)153,872
- Last updated1990-08-01 v1
- Checksum5EEFCEE4D7498E8D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X17403 EMBL· GenBank· DDBJ | CAA35360.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M25411 EMBL· GenBank· DDBJ | AAA51532.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK000394 EMBL· GenBank· DDBJ | DAA00183.1 EMBL· GenBank· DDBJ | Genomic DNA |