P08124 · COL1_CAEEL
- ProteinCuticle collagen 1
- Genesqt-3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids301 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Secreted collagen that forms part of the nematode cuticle, which functions as an exoskeleton and a barrier to protect the worm from its environment (PubMed:37721936).
Secretion and subsequent incorporation into the cuticle is likely mediated by bli-4, which probably cleaves at the N-terminal consensus furin cleavage site (PubMed:37721936).
Secretion and subsequent incorporation into the cuticle is likely mediated by bli-4, which probably cleaves at the N-terminal consensus furin cleavage site (PubMed:37721936).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 289-290 | Cleavage; by dpy-31 | ||||
Sequence: LD |
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 and cuticulin-based cuticle extracellular matrix | |
Cellular Component | collagen trimer | |
Cellular Component | extracellular region | |
Molecular Function | structural constituent of cuticle | |
Biological Process | collagen and cuticulin-based cuticle development | |
Biological Process | cuticle development involved in collagen and cuticulin-based cuticle molting cycle |
Names & Taxonomy
Protein names
- Recommended nameCuticle collagen 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionP08124
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 79-82 | Forms large puncta; fails to secrete and incorporate into the cuticle. | ||||
Sequence: RTTR → ATTA | ||||||
Mutagenesis | 288 | In e2809, e2889 and e2896; abnormal left-twisted body. | ||||
Sequence: A → V | ||||||
Mutagenesis | 290 | In 2901; abnormal left-handed rolling. | ||||
Sequence: D → G | ||||||
Mutagenesis | 291 | In e2888, e2890 and sc8; abnormal left-twisted body. At the restrictive temperature of 25 degrees Celsius, lethal in a dpy-31 (ju345) mutant background. | ||||
Sequence: G → E | ||||||
Mutagenesis | 297 | In e2911; slightly shorter and stouter. | ||||
Sequence: D → G | ||||||
Mutagenesis | 299 | In e2906; temperature sensitive mutant. At the restrictive temperature of 15 degrees Celsius, lethal at the embryonic or early larval stages. At the permissive temperature of 25 degrees Celsius, slightly shorter and stouter. | ||||
Sequence: T → A |
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-37 | |||||
Sequence: METDGRLKAYKFVAYAAVGFSIAAVASVLLTLPMVYS | ||||||
Chain | PRO_0000006420 | 38-301 | Cuticle collagen 1 | |||
Sequence: YVSHVRQQMHHEINFCKGSAKDIFAEVNYMKANAGPVPPRNRTTRQAYGGPEVNPAPNLQCEGCCLPGPPGPAGAPGKPGKPGRPGAPGTPGTPGKPPVAPCEPTTPPPCKPCPQGPPGPPGPPGAPGDPGEAGTPGRPGTDAAPGSPGPRGPPGPAGEAGAPGPAGEPGTPAISEPLTPGAPGEPGDSGPPGPPGPPGAPGNDGPPGPPGPKGAPGPDGPPGVDGQSGPPGPPGPAGTPGEKGICPKYCALDGGVFFEDGTRR |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 79-82 | Furin-like endopeptidase recognition region | ||||
Sequence: RTTR | ||||||
Region | 105-134 | Triple-helical region | ||||
Sequence: GPPGPAGAPGKPGKPGRPGAPGTPGTPGKP | ||||||
Compositional bias | 109-167 | Pro residues | ||||
Sequence: PAGAPGKPGKPGRPGAPGTPGTPGKPPVAPCEPTTPPPCKPCPQGPPGPPGPPGAPGDP | ||||||
Region | 109-284 | Disordered | ||||
Sequence: PAGAPGKPGKPGRPGAPGTPGTPGKPPVAPCEPTTPPPCKPCPQGPPGPPGPPGAPGDPGEAGTPGRPGTDAAPGSPGPRGPPGPAGEAGAPGPAGEPGTPAISEPLTPGAPGEPGDSGPPGPPGPPGAPGNDGPPGPPGPKGAPGPDGPPGVDGQSGPPGPPGPAGTPGEKGICP | ||||||
Region | 153-179 | Triple-helical region | ||||
Sequence: GPPGPPGPPGAPGDPGEAGTPGRPGTD | ||||||
Compositional bias | 183-197 | Pro residues | ||||
Sequence: GSPGPRGPPGPAGEA | ||||||
Region | 183-209 | Triple-helical region | ||||
Sequence: GSPGPRGPPGPAGEAGAPGPAGEPGTP | ||||||
Region | 218-283 | Triple-helical region | ||||
Sequence: GAPGEPGDSGPPGPPGPPGAPGNDGPPGPPGPKGAPGPDGPPGVDGQSGPPGPPGPAGTPGEKGIC | ||||||
Compositional bias | 221-277 | Pro residues | ||||
Sequence: GEPGDSGPPGPPGPPGAPGNDGPPGPPGPKGAPGPDGPPGVDGQSGPPGPPGPAGTP |
Sequence similarities
Belongs to the cuticular collagen family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length301
- Mass (Da)29,177
- Last updated2008-07-22 v2
- Checksum4A75B65540E50360
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H2L2C4 | H2L2C4_CAEEL | sqt-3 | 235 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 57-61 | in Ref. 1; CAA23463 and 2; AAA27988 | ||||
Sequence: Missing | ||||||
Compositional bias | 109-167 | Pro residues | ||||
Sequence: PAGAPGKPGKPGRPGAPGTPGTPGKPPVAPCEPTTPPPCKPCPQGPPGPPGPPGAPGDP | ||||||
Compositional bias | 183-197 | Pro residues | ||||
Sequence: GSPGPRGPPGPAGEA | ||||||
Compositional bias | 221-277 | Pro residues | ||||
Sequence: GEPGDSGPPGPPGPPGAPGNDGPPGPPGPKGAPGPDGPPGVDGQSGPPGPPGPAGTP | ||||||
Sequence conflict | 261 | in Ref. 1; CAA23463 and 2; AAA27988 | ||||
Sequence: V → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
V00147 EMBL· GenBank· DDBJ | CAA23463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
J01047 EMBL· GenBank· DDBJ | AAA27988.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z74472 EMBL· GenBank· DDBJ | CAA98942.1 EMBL· GenBank· DDBJ | Genomic DNA |