Q0VF58 · COJA1_MOUSE
- ProteinCollagen alpha-1(XIX) chain
- GeneCol19a1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1136 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
May act as a cross-bridge between fibrils and other extracellular matrix molecules. Involved in skeletal myogenesis in the developing esophagus. May play a role in organization of the pericellular matrix or the sphinteric smooth muscle.
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 | collagen trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | extracellular matrix structural constituent conferring tensile strength | |
Biological Process | cell adhesion | |
Biological Process | cell differentiation | |
Biological Process | extracellular matrix organization | |
Biological Process | skeletal muscle tissue development |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCollagen alpha-1(XIX) chain
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ0VF58
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice show severe signs of malnourishment and the majority die within the first three weeks of postnatal life. Newborn homozygotes do not show gross anatomical abnormalities, except for smaller size of the internal organs. However, necroscopy of the mice that survive past the weaning stage reveals a dilated esophagus (megaesophagus) with retention of ingesta immediately above the diaphragm level. Mutant mice also exhibit an additional defect, namely impaired smooth-to-skeletal muscle cell transdifferentiation in the abdominal segment of the esophagus. Heterozygotes by comparison are morphologically normal, viable and fertile.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 99 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MRHTGSWKLWTWVTTFLLPACTC | ||||||
Chain | PRO_0000284731 | 24-1136 | Collagen alpha-1(XIX) chain | |||
Sequence: LTVRDKPETTCPTLRTERYQDDRNKSELSGFDLGESFALRHAFCEGDKTCFKLGSVLLIRDTVKIFPKGLPEEYAIAVMFRVRRSTKKERWFLWKILNQQNMAQISVVIDGTKKVVEFMFRGAEGDLLNYVFKNRELRPLFDRQWHKLGIGVQSRVLSLYMDCNLIASRHTEEKNSVDFQGRTIIAARASDGKPVDIELHQLRIYCNANFLAEESCCNLSPTKCPEQDDFGSTTSSWGTSNTGKMSSYLPGKQELKDTCQCIPNKEEAGLPGTLRSIGHKGDKGEPGEHGLDGTPGLPGQKGEQGLEGIKGEIGEKGEPGAKGDSGLDGLNGQDGLKGDSGPQGPPGPKGDKGDMGPPGPPALTGSIGIQGPQGPPGKEGQRGRRGKTGPPGNPGPPGPPGPPGLQGLQQPFGGYFNKGTGEHGASGPKGEKGDTGLPGFPGSVGPKGHKGEPGEPLTKGEKGDRGEPGLLGPQGIKGEPGDPGPPGLLGSPGLKGQQGPAGSMGPRGPPGDVGLPGEHGIPGKQGVKGEKGDPGGRLGPPGLPGLKGDAGPPGISLPGKPGLDGNPGSPGPRGPKGERGLPGLHGSPGDTGPPGVGIPGRTGSQGPAGEPGIQGPRGLPGLPGTPGMPGNDGAPGKDGKPGLPGPPGDPIALPLLGDIGALLKNFCGNCQANVPGLKSIKGDDGSTGEPGKYDPAARKGDVGPRGPPGFPGREGPKGSKGERGYPGIHGEKGDEGLQGIPGLSGAPGPTGPPGLTGRTGHPGPTGAKGDKGSEGPPGKPGPPGPPGVPLNEGNGMSSLYKIQGGVNVPGYPGPPGPPGPKGDPGPVGEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGISGKPGAPGPPGVPGEQGERGPIGDTGFPGPEGPSGKPGINGKDGLPGAQGIMGKPGDRGPKGERGDQGIPGDRGPQGERGKPGLTGMKGAIGPVGPAGSKGSTGPPGHQGPPGNPGIPGTPADAVSFEEIKHYINQEVLRIFEERMAVFLSQLKLPAAMLSAQAHGRPGPPGKDGLPGPPGDPGPQGYRGQKGERGEPGIGLPGSPGLPGSSAVGLPGSPGAPGPQGPPGPSGRCNPEDCLYPAPPPHQQAGGK | ||||||
Glycosylation | 47 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
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
Developmental stage
Expressed in the myotome of somites from 9.5 dpc. In muscular tissues, expression is transient and is confined to a few sites of the developing embryo, such as limbs, tongue, and smooth muscle layers of stomach and esophagus. Also detected in skin at 16.5 dpc and in cerebral cortex and hippocampus of the newborn brain. In adult, expression is only observed in cerebrum, cerebellum, eyes, and testis. In CNS, expression gradually increases following birth. Also expressed in embryonic fibroblasts and to a lesser extent in adult fibroblasts.
Gene expression databases
Interaction
Subunit
Oligomer; disulfide-linked.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 47-231 | Laminin G-like | ||||
Sequence: NKSELSGFDLGESFALRHAFCEGDKTCFKLGSVLLIRDTVKIFPKGLPEEYAIAVMFRVRRSTKKERWFLWKILNQQNMAQISVVIDGTKKVVEFMFRGAEGDLLNYVFKNRELRPLFDRQWHKLGIGVQSRVLSLYMDCNLIASRHTEEKNSVDFQGRTIIAARASDGKPVDIELHQLRIYCNA | ||||||
Compositional bias | 252-271 | Polar residues | ||||
Sequence: DFGSTTSSWGTSNTGKMSSY | ||||||
Region | 252-272 | Disordered | ||||
Sequence: DFGSTTSSWGTSNTGKMSSYL | ||||||
Region | 289-348 | Triple-helical region 1 (COL1) | ||||
Sequence: EEAGLPGTLRSIGHKGDKGEPGEHGLDGTPGLPGQKGEQGLEGIKGEIGEKGEPGAKGDS | ||||||
Region | 289-673 | Disordered | ||||
Sequence: EEAGLPGTLRSIGHKGDKGEPGEHGLDGTPGLPGQKGEQGLEGIKGEIGEKGEPGAKGDSGLDGLNGQDGLKGDSGPQGPPGPKGDKGDMGPPGPPALTGSIGIQGPQGPPGKEGQRGRRGKTGPPGNPGPPGPPGPPGLQGLQQPFGGYFNKGTGEHGASGPKGEKGDTGLPGFPGSVGPKGHKGEPGEPLTKGEKGDRGEPGLLGPQGIKGEPGDPGPPGLLGSPGLKGQQGPAGSMGPRGPPGDVGLPGEHGIPGKQGVKGEKGDPGGRLGPPGLPGLKGDAGPPGISLPGKPGLDGNPGSPGPRGPKGERGLPGLHGSPGDTGPPGVGIPGRTGSQGPAGEPGIQGPRGLPGLPGTPGMPGNDGAPGKDGKPGLPGPPGDP | ||||||
Domain | 292-346 | Collagen-like 1 | ||||
Sequence: GLPGTLRSIGHKGDKGEPGEHGLDGTPGLPGQKGEQGLEGIKGEIGEKGEPGAKG | ||||||
Compositional bias | 331-345 | Basic and acidic residues | ||||
Sequence: GIKGEIGEKGEPGAK | ||||||
Domain | 347-388 | Collagen-like 2 | ||||
Sequence: DSGLDGLNGQDGLKGDSGPQGPPGPKGDKGDMGPPGPPALTG | ||||||
Region | 367-426 | Triple-helical region 2 (COL2) | ||||
Sequence: GPPGPKGDKGDMGPPGPPALTGSIGIQGPQGPPGKEGQRGRRGKTGPPGNPGPPGPPGPP | ||||||
Domain | 389-430 | Collagen-like 3 | ||||
Sequence: SIGIQGPQGPPGKEGQRGRRGKTGPPGNPGPPGPPGPPGLQG | ||||||
Compositional bias | 413-429 | Pro residues | ||||
Sequence: PPGNPGPPGPPGPPGLQ | ||||||
Region | 442-682 | Triple-helical region 3 (COL3) | ||||
Sequence: GTGEHGASGPKGEKGDTGLPGFPGSVGPKGHKGEPGEPLTKGEKGDRGEPGLLGPQGIKGEPGDPGPPGLLGSPGLKGQQGPAGSMGPRGPPGDVGLPGEHGIPGKQGVKGEKGDPGGRLGPPGLPGLKGDAGPPGISLPGKPGLDGNPGSPGPRGPKGERGLPGLHGSPGDTGPPGVGIPGRTGSQGPAGEPGIQGPRGLPGLPGTPGMPGNDGAPGKDGKPGLPGPPGDPIALPLLGDI | ||||||
Compositional bias | 475-489 | Basic and acidic residues | ||||
Sequence: EPGEPLTKGEKGDRG | ||||||
Domain | 519-577 | Collagen-like 4 | ||||
Sequence: GQQGPAGSMGPRGPPGDVGLPGEHGIPGKQGVKGEKGDPGGRLGPPGLPGLKGDAGPPG | ||||||
Domain | 578-618 | Collagen-like 5 | ||||
Sequence: ISLPGKPGLDGNPGSPGPRGPKGERGLPGLHGSPGDTGPPG | ||||||
Domain | 620-673 | Collagen-like 6 | ||||
Sequence: GIPGRTGSQGPAGEPGIQGPRGLPGLPGTPGMPGNDGAPGKDGKPGLPGPPGDP | ||||||
Region | 694-812 | Triple-helical region 4 (COL4) | ||||
Sequence: QANVPGLKSIKGDDGSTGEPGKYDPAARKGDVGPRGPPGFPGREGPKGSKGERGYPGIHGEKGDEGLQGIPGLSGAPGPTGPPGLTGRTGHPGPTGAKGDKGSEGPPGKPGPPGPPGVP | ||||||
Region | 699-1005 | Disordered | ||||
Sequence: GLKSIKGDDGSTGEPGKYDPAARKGDVGPRGPPGFPGREGPKGSKGERGYPGIHGEKGDEGLQGIPGLSGAPGPTGPPGLTGRTGHPGPTGAKGDKGSEGPPGKPGPPGPPGVPLNEGNGMSSLYKIQGGVNVPGYPGPPGPPGPKGDPGPVGEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGISGKPGAPGPPGVPGEQGERGPIGDTGFPGPEGPSGKPGINGKDGLPGAQGIMGKPGDRGPKGERGDQGIPGDRGPQGERGKPGLTGMKGAIGPVGPAGSKGSTGPPGHQGPPGNPGIPGTPAD | ||||||
Domain | 722-777 | Collagen-like 7 | ||||
Sequence: KGDVGPRGPPGFPGREGPKGSKGERGYPGIHGEKGDEGLQGIPGLSGAPGPTGPPG | ||||||
Compositional bias | 739-753 | Basic and acidic residues | ||||
Sequence: PKGSKGERGYPGIHG | ||||||
Domain | 778-810 | Collagen-like 8 | ||||
Sequence: LTGRTGHPGPTGAKGDKGSEGPPGKPGPPGPPG | ||||||
Region | 827-1006 | Triple-helical region 5 (COL5) | ||||
Sequence: GGVNVPGYPGPPGPPGPKGDPGPVGEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGISGKPGAPGPPGVPGEQGERGPIGDTGFPGPEGPSGKPGINGKDGLPGAQGIMGKPGDRGPKGERGDQGIPGDRGPQGERGKPGLTGMKGAIGPVGPAGSKGSTGPPGHQGPPGNPGIPGTPADA | ||||||
Compositional bias | 833-848 | Pro residues | ||||
Sequence: GYPGPPGPPGPKGDPG | ||||||
Domain | 833-891 | Collagen-like 9 | ||||
Sequence: GYPGPPGPPGPKGDPGPVGEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGISGKPGAPGP | ||||||
Motif | 946-948 | Cell attachment site | ||||
Sequence: RGD | ||||||
Region | 1043-1136 | Disordered | ||||
Sequence: SAQAHGRPGPPGKDGLPGPPGDPGPQGYRGQKGERGEPGIGLPGSPGLPGSSAVGLPGSPGAPGPQGPPGPSGRCNPEDCLYPAPPPHQQAGGK | ||||||
Region | 1048-1105 | Triple-helical region 6 (COL6) | ||||
Sequence: GRPGPPGKDGLPGPPGDPGPQGYRGQKGERGEPGIGLPGSPGLPGSSAVGLPGSPGAP |
Domain
The numerous interruptions in the triple helix may make this molecule either elastic or flexible.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,136
- Mass (Da)114,197
- Last updated2007-04-17 v2
- ChecksumC480216027D70B43
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8WHV4 | F8WHV4_MOUSE | Col19a1 | 1069 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 110 | in Ref. 1; BAA23578 | ||||
Sequence: K → Q | ||||||
Compositional bias | 252-271 | Polar residues | ||||
Sequence: DFGSTTSSWGTSNTGKMSSY | ||||||
Sequence conflict | 315 | in Ref. 1; BAA23578 and 3; AAI18971 | ||||
Sequence: D → N | ||||||
Compositional bias | 331-345 | Basic and acidic residues | ||||
Sequence: GIKGEIGEKGEPGAK | ||||||
Compositional bias | 413-429 | Pro residues | ||||
Sequence: PPGNPGPPGPPGPPGLQ | ||||||
Compositional bias | 475-489 | Basic and acidic residues | ||||
Sequence: EPGEPLTKGEKGDRG | ||||||
Sequence conflict | 528 | in Ref. 1; BAA23578 | ||||
Sequence: G → K | ||||||
Sequence conflict | 597 | in Ref. 1; BAA23578 | ||||
Sequence: G → E | ||||||
Sequence conflict | 717 | in Ref. 1; BAA23578 and 3; AAI18971 | ||||
Sequence: D → E | ||||||
Compositional bias | 739-753 | Basic and acidic residues | ||||
Sequence: PKGSKGERGYPGIHG | ||||||
Compositional bias | 833-848 | Pro residues | ||||
Sequence: GYPGPPGPPGPKGDPG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB000636 EMBL· GenBank· DDBJ | BAA23578.1 EMBL· GenBank· DDBJ | mRNA | ||
AC116998 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC130201 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC161879 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC118970 EMBL· GenBank· DDBJ | AAI18971.1 EMBL· GenBank· DDBJ | mRNA |