Q9YIB4 (CO1A1_CYNPY) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 52.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Collagen alpha-1(I) chain Alternative name(s): Alpha-1 type I collagen | ||
| Gene names |
| ||
| Organism | Cynops pyrrhogaster (Japanese common newt) | ||
| Taxonomic identifier | 8330 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Caudata › Salamandroidea › Salamandridae › Cynops![]() |
Protein attributes
| Sequence length | 1450 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Type I collagen is a member of group I collagen (fibrillar forming collagen) By similarity. |
| Subunit structure | Trimers of one alpha 2(I) and two alpha 1(I) chains By similarity. |
| Subcellular location | Secreted › extracellular space › extracellular matrix By similarity. |
| Domain | The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity. |
| Post-translational modification | Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains By similarity. |
| Sequence similarities | Belongs to the fibrillar collagen family. Contains 1 fibrillar collagen NC1 domain. Contains 1 VWFC domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Extracellular matrix Secreted |
| Domain | Collagen Repeat Signal |
| Ligand | Calcium Metal-binding |
| PTM | Disulfide bond Glycoprotein Hydroxylation Pyrrolidone carboxylic acid |
| Gene Ontology (GO) | |
| Cellular_component | collagen Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | extracellular matrix structural constituent Inferred from electronic annotation. Source: InterPro metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | ||||||||
| Propeptide | 23 – 148 | 126 | N-terminal propeptide By similarity | PRO_0000286160 | |||||||
| Chain | 149 – 1202 | 1054 | Collagen alpha-1(I) chain | PRO_0000286161 | |||||||
| Propeptide | 1203 – 1450 | 248 | C-terminal propeptide By similarity | PRO_0000286162 | |||||||
Regions | |||||||||||
| Domain | 31 – 90 | 60 | VWFC | ||||||||
| Domain | 1215 – 1450 | 236 | Fibrillar collagen NC1 | ||||||||
Sites | |||||||||||
| Metal binding | 1263 | 1 | Calcium By similarity | ||||||||
| Metal binding | 1265 | 1 | Calcium By similarity | ||||||||
| Metal binding | 1266 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 1268 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 1271 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 149 | 1 | Pyrrolidone carboxylic acid By similarity | ||||||||
| Glycosylation | 1351 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 1245 ↔ 1277 | By similarity | |||||||||
| Disulfide bond | 1251 | Interchain (with C-1268) By similarity | |||||||||
| Disulfide bond | 1268 | Interchain (with C-1251) By similarity | |||||||||
| Disulfide bond | 1285 ↔ 1448 | By similarity | |||||||||
| Disulfide bond | 1356 ↔ 1401 | By similarity | |||||||||
Sequences
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References
| [1] | "Expression of genes of type I and type II collagen in the formation and development of the blastema of regenerating newt limb." Asahina K., Obara M., Yoshizato K. Dev. Dyn. 216:59-71(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Regenerating forelimb blastema. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB015438 mRNA. Translation: BAA36973.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1Q7D based on UniProtKB Q15201. |
| ProteinModelPortal | Q9YIB4. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG004933. |
Family and domain databases | |
| InterPro | IPR008160. Collagen. IPR000885. Fib_collagen_C. IPR001007. VWF_C. [Graphical view] |
| Pfam | PF01410. COLFI. 1 hit. PF01391. Collagen. 12 hits. PF00093. VWC. 1 hit. [Graphical view] |
| ProDom | PD002078. Fib_collagen_C. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00038. COLFI. 1 hit. SM00214. VWC. 1 hit. [Graphical view] |
| PROSITE | PS51461. NC1_FIB. 1 hit. PS01208. VWFC_1. 1 hit. PS50184. VWFC_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CO1A1_CYNPY | ||||||||
| Accession | Primary (citable) accession number: Q9YIB4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
