P25067 · CO8A2_HUMAN
- ProteinCollagen alpha-2(VIII) chain
- GeneCOL8A2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids703 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also a component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis (By similarity).
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 | basement membrane | |
Cellular Component | collagen trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | extracellular matrix | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Molecular Function | extracellular matrix structural constituent | |
Molecular Function | extracellular matrix structural constituent conferring tensile strength | |
Molecular Function | protein-macromolecule adaptor activity | |
Biological Process | angiogenesis | |
Biological Process | camera-type eye morphogenesis | |
Biological Process | cell-cell adhesion | |
Biological Process | endothelial cell proliferation | |
Biological Process | extracellular matrix organization |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCollagen alpha-2(VIII) chain
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP25067
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Corneal dystrophy, Fuchs endothelial, 1 (FECD1)
- Note
- DescriptionA corneal disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition.
- See alsoMIM:136800
Natural variants in FECD1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_017895 | 304 | R>Q | in FECD1; dbSNP:rs369487110 | |
VAR_017896 | 357 | G>R | in FECD1; uncertain significance; dbSNP:rs199786966 | |
VAR_017897 | 434 | R>H | in FECD1; dbSNP:rs201235688 | |
VAR_017898 | 455 | Q>K | in FECD1 and PPCD2; dbSNP:rs80358191 | |
VAR_017899 | 575 | P>L | in FECD1; uncertain significance; dbSNP:rs145553904 |
Corneal dystrophy, posterior polymorphous, 2 (PPCD2)
- Note
- DescriptionA rare mild subtype of posterior corneal dystrophy characterized by alterations of Descemet membrane presenting as vesicles, opacities or band-like lesions on slit-lamp examination and specular microscopy. Affected patient typically are asymptomatic.
- See alsoMIM:609140
Natural variants in PPCD2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_017898 | 455 | Q>K | in FECD1 and PPCD2; dbSNP:rs80358191 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_017893 | 3 | in dbSNP:rs115156902 | |||
Sequence: G → R | ||||||
Natural variant | VAR_017894 | 155 | in dbSNP:rs75864656 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_017895 | 304 | in FECD1; dbSNP:rs369487110 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_017896 | 357 | in FECD1; uncertain significance; dbSNP:rs199786966 | |||
Sequence: G → R | ||||||
Natural variant | VAR_017897 | 434 | in FECD1; dbSNP:rs201235688 | |||
Sequence: R → H | ||||||
Natural variant | VAR_017898 | 455 | in FECD1 and PPCD2; dbSNP:rs80358191 | |||
Sequence: Q → K | ||||||
Natural variant | VAR_021387 | 502 | in dbSNP:rs117860804 | |||
Sequence: T → M | ||||||
Natural variant | VAR_017899 | 575 | in FECD1; uncertain significance; dbSNP:rs145553904 | |||
Sequence: P → L | ||||||
Natural variant | VAR_017900 | 645 | in dbSNP:rs200767854 | |||
Sequence: T → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 892 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-28 | |||||
Sequence: MLGTLTPLSSLLLLLLVLVLGCGPRASS | ||||||
Chain | PRO_0000005835 | 29-703 | Collagen alpha-2(VIII) chain | |||
Sequence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|
Post-translational modification
Proteolytically cleaved by neutrophil elastase, in vitro.
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed primarily in the subendothelium of large blood vessels. Also expressed in arterioles and venules in muscle, heart, kidney, spleen, umbilical cord, liver and lung and is also found in connective tissue layers around hair follicles, around nerve bundles in muscle, in the dura of the optic nerve, in cornea and sclera, and in the perichondrium of cartilaginous tissues. In the kidney, expressed in mesangial cells, glomerular endothelial cells, and tubular epithelial cells. Also expressed in mast cells, and in astrocytes during the repair process. Expressed in Descemet's membrane.
Induction
Some up-regulation in diabetic nephropathy.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homotrimers, or heterotrimers in association with alpha 2(VIII) type collagens. Four homotrimers can form a tetrahedron stabilized by central interacting C-terminal NC1 trimers.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 29-76 | Nonhelical region (NC2) | ||||
Sequence: GGGAGGAAGYAPVKYIQPMQKGPVGPPFREGKGQYLEMPLPLLPMDLK | ||||||
Region | 70-544 | Disordered | ||||
Sequence: LLPMDLKGEPGPPGKPGPRGPPGPPGFPGKPGMGKPGLHGQPGPAGPPGFSRMGKAGPPGLPGKVGPPGQPGLRGEPGIRGDQGLRGPPGPPGLPGPSGITIPGKPGAQGVPGPPGFQGEPGPQGEPGPPGDRGLKGDNGVGQPGLPGAPGQGGAPGPPGLPGPAGLGKPGLDGLPGAPGDKGESGPPGVPGPRGEPGAVGPKGPPGVDGVGVPGAAGLPGPQGPSGAKGEPGTRGPPGLIGPTGYGMPGLPGPKGDRGPAGVPGLLGDRGEPGEDGEPGEQGPQGLGGPPGLPGSAGLPGRRGPPGPKGEAGPGGPPGVPGIRGDQGPSGLAGKPGVPGERGLPGAHGPPGPTGPKGEPGFTGRPGGPGVAGALGQKGDLGLPGQPGLRGPSGIPGLQGPAGPIGPQGLPGLKGEPGLPGPPGEGRAGEPGTAGPTGPPGVPGSPGITGPPGPPGPPGPPGAPGAFDETGIAGL | ||||||
Compositional bias | 74-100 | Pro residues | ||||
Sequence: DLKGEPGPPGKPGPRGPPGPPGFPGKP | ||||||
Region | 77-536 | Triple-helical region | ||||
Sequence: GEPGPPGKPGPRGPPGPPGFPGKPGMGKPGLHGQPGPAGPPGFSRMGKAGPPGLPGKVGPPGQPGLRGEPGIRGDQGLRGPPGPPGLPGPSGITIPGKPGAQGVPGPPGFQGEPGPQGEPGPPGDRGLKGDNGVGQPGLPGAPGQGGAPGPPGLPGPAGLGKPGLDGLPGAPGDKGESGPPGVPGPRGEPGAVGPKGPPGVDGVGVPGAAGLPGPQGPSGAKGEPGTRGPPGLIGPTGYGMPGLPGPKGDRGPAGVPGLLGDRGEPGEDGEPGEQGPQGLGGPPGLPGSAGLPGRRGPPGPKGEAGPGGPPGVPGIRGDQGPSGLAGKPGVPGERGLPGAHGPPGPTGPKGEPGFTGRPGGPGVAGALGQKGDLGLPGQPGLRGPSGIPGLQGPAGPIGPQGLPGLKGEPGLPGPPGEGRAGEPGTAGPTGPPGVPGSPGITGPPGPPGPPGPPGAPGAF | ||||||
Compositional bias | 220-234 | Pro residues | ||||
Sequence: GQGGAPGPPGLPGPA | ||||||
Compositional bias | 505-533 | Pro residues | ||||
Sequence: PTGPPGVPGSPGITGPPGPPGPPGPPGAP | ||||||
Region | 537-703 | Nonhelical region (NC1) | ||||
Sequence: DETGIAGLHLPNGGVEGAVLGKGGKPQFGLGELSAHATPAFTAVLTSPFPASGMPVKFDRTLYNGHSGYNPATGIFTCPVGGVYYFAYHVHVKGTNVWVALYKNNVPATYTYDEYKKGYLDQASGGAVLQLRPNDQVWVQMPSDQANGLYSTEYIHSSFSGFLLCPT | ||||||
Domain | 570-703 | C1q | ||||
Sequence: SAHATPAFTAVLTSPFPASGMPVKFDRTLYNGHSGYNPATGIFTCPVGGVYYFAYHVHVKGTNVWVALYKNNVPATYTYDEYKKGYLDQASGGAVLQLRPNDQVWVQMPSDQANGLYSTEYIHSSFSGFLLCPT |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length703
- Mass (Da)67,244
- Last updated2004-03-15 v2
- Checksum84BD7CBDBDECD466
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PP49 | E9PP49_HUMAN | COL8A2 | 638 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 74-100 | Pro residues | ||||
Sequence: DLKGEPGPPGKPGPRGPPGPPGFPGKP | ||||||
Sequence conflict | 88 | in Ref. 4; AAA62822 | ||||
Sequence: R → W | ||||||
Sequence conflict | 102 | in Ref. 4; AAA62822 | ||||
Sequence: M → H | ||||||
Sequence conflict | 133 | in Ref. 4; AAA62822 | ||||
Sequence: K → N | ||||||
Compositional bias | 220-234 | Pro residues | ||||
Sequence: GQGGAPGPPGLPGPA | ||||||
Sequence conflict | 347 | in Ref. 4; AAA62822 | ||||
Sequence: E → D | ||||||
Sequence conflict | 377-378 | in Ref. 4; AAA62822 | ||||
Sequence: PK → LR | ||||||
Compositional bias | 505-533 | Pro residues | ||||
Sequence: PTGPPGVPGSPGITGPPGPPGPPGPPGAP | ||||||
Sequence conflict | 506 | in Ref. 4; AAA62822 | ||||
Sequence: T → R | ||||||
Sequence conflict | 523 | in Ref. 4; AAA62822 | ||||
Sequence: P → L | ||||||
Sequence conflict | 529-531 | in Ref. 4; AAA62822 | ||||
Sequence: Missing | ||||||
Sequence conflict | 585 | in Ref. 4; AAA62822 | ||||
Sequence: F → L | ||||||
Sequence conflict | 677 | in Ref. 4; AAA62822 | ||||
Sequence: M → I |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK074129 EMBL· GenBank· DDBJ | BAB84955.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL138787 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471059 EMBL· GenBank· DDBJ | EAX07388.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M60832 EMBL· GenBank· DDBJ | AAA62822.1 EMBL· GenBank· DDBJ | Genomic DNA |