Q5QNQ9 (CORA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 82.
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(XXVII) chain | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 1845 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 | Plays a role during the calcification of cartilage and the transition of cartilage to bone By similarity. |
| Subcellular location | Secreted › extracellular space › extracellular matrix. Note: Found on some small banded collagen fibrils and filamentous meshworks. Ref.4 |
| Tissue specificity | Highly expressed in cartilage, eye and ear. Ref.1 |
| Developmental stage | Expressed in E14.5 in several cartilaginous structures including anlagen of several bones and the developing lungs as well as in the eye, ear and colon. First detectable at E12.5. At E14.5 localizes to cartilage, developing dermis, cornea, the inner limiting membrane of the retina, and major arteries of the heart. At E18.5 appears restricted mainly to cartilage where expression continued into adulthood. Ref.1 Ref.5 |
| 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. |
| Sequence similarities | Belongs to the fibrillar collagen family. Contains 15 collagen-like domains. Contains 1 fibrillar collagen NC1 domain. Contains 1 laminin G-like domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Extracellular matrix Secreted |
| Domain | Collagen Repeat Signal |
| Ligand | Calcium Metal-binding |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | fibrillar collagen Inferred from direct assay Ref.5. Source: MGI |
| 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 – 39 | 39 | Potential | ||||||||
| Propeptide | 40 – 609 | 570 | N-terminal propeptide | PRO_0000314669 | |||||||
| Chain | 610 – 1606 | 997 | Collagen alpha-1(XXVII) chain | PRO_0000314670 | |||||||
| Propeptide | 1607 – 1845 | 239 | C-terminal propeptide | PRO_0000314671 | |||||||
Regions | |||||||||||
| Domain | 72 – 237 | 166 | Laminin G-like | ||||||||
| Domain | 610 – 664 | 55 | Collagen-like 1 | ||||||||
| Domain | 673 – 732 | 60 | Collagen-like 2 | ||||||||
| Domain | 742 – 801 | 60 | Collagen-like 3 | ||||||||
| Domain | 817 – 876 | 60 | Collagen-like 4 | ||||||||
| Domain | 877 – 936 | 60 | Collagen-like 5 | ||||||||
| Domain | 937 – 996 | 60 | Collagen-like 6 | ||||||||
| Domain | 997 – 1038 | 42 | Collagen-like 7 | ||||||||
| Domain | 1039 – 1096 | 58 | Collagen-like 8 | ||||||||
| Domain | 1117 – 1176 | 60 | Collagen-like 9 | ||||||||
| Domain | 1177 – 1236 | 60 | Collagen-like 10 | ||||||||
| Domain | 1240 – 1299 | 60 | Collagen-like 11 | ||||||||
| Domain | 1325 – 1384 | 60 | Collagen-like 12 | ||||||||
| Domain | 1424 – 1483 | 60 | Collagen-like 13 | ||||||||
| Domain | 1484 – 1543 | 60 | Collagen-like 14 | ||||||||
| Domain | 1544 – 1603 | 60 | Collagen-like 15 | ||||||||
| Domain | 1645 – 1845 | 201 | Fibrillar collagen NC1 | ||||||||
| Region | 610 – 1603 | 994 | Triple-helical | ||||||||
Sites | |||||||||||
| Metal binding | 1693 | 1 | Calcium By similarity | ||||||||
| Metal binding | 1695 | 1 | Calcium By similarity | ||||||||
| Metal binding | 1698 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 1701 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 272 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 340 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1754 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 1675 ↔ 1707 | By similarity | |||||||||
| Disulfide bond | 1681 | Interchain (with C-1285) By similarity | |||||||||
| Disulfide bond | 1698 | Interchain (with C-1268) By similarity | |||||||||
| Disulfide bond | 1716 ↔ 1843 | By similarity | |||||||||
| Disulfide bond | 1752 ↔ 1796 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 293 – 295 | 3 | LAP → VAR in AAN87341. Ref.1 | ||||||||
| Sequence conflict | 302 – 306 | 5 | LRTVH → VRSVR in AAN87341. Ref.1 | ||||||||
| Sequence conflict | 312 – 314 | 3 | HSS → RSC in AAN87341. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification, characterization and expression analysis of a new fibrillar collagen gene, COL27A1." Pace J.M., Corrado M., Missero C., Byers P.H. Matrix Biol. 22:3-14(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY. Strain: C57BL/6. |
| [2] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [3] | "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H. DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 989-1845. Tissue: Thymus. |
| [4] | "Type XXVII collagen at the transition of cartilage to bone during skeletogenesis." Hjorten R., Hansen U., Underwood R.A., Telfer H.E., Fernandes R.J., Krakow D., Sebald E., Wachsmann-Hogiu S., Bruckner P., Jacquet R., Landis W.J., Byers P.H., Pace J.M. Bone 41:535-542(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [5] | "Collagen XXVII is developmentally regulated and forms thin fibrillar structures distinct from those of classical vertebrate fibrillar collagens." Plumb D.A., Dhir V., Mironov A., Ferrara L., Poulsom R., Kadler K.E., Thornton D.J., Briggs M.D., Boot-Handford R.P. J. Biol. Chem. 282:12791-12795(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY167568 mRNA. Translation: AAN87341.2. AL683828, AL691496 Genomic DNA. Translation: CAI25268.1. AL691496, AL683828 Genomic DNA. Translation: CAI25993.1. AK173283 mRNA. Translation: BAD32561.1. |
| IPI | IPI00408491. |
| RefSeq | NP_079961.3. NM_025685.3. |
| UniGene | Mm.194116. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1Q7D based on UniProtKB Q15201. |
| ProteinModelPortal | Q5QNQ9. |
| SMR | Q5QNQ9. Positions 1663-1845. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q5QNQ9. |
Proteomic databases | |
| PaxDb | Q5QNQ9. |
| PRIDE | Q5QNQ9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000036300; ENSMUSP00000043816; ENSMUSG00000045672. |
| GeneID | 373864. |
| KEGG | mmu:373864. |
| UCSC | uc008tfs.1. mouse. |
Organism-specific databases | |
| CTD | 85301. |
| MGI | MGI:2672118. Col27a1. |
| Rouge | Search... |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| GeneTree | ENSGT00700000104301. |
| HOGENOM | HOG000085654. |
| HOVERGEN | HBG098141. |
| InParanoid | Q5QNQ9. |
| KO | K06236. |
| OMA | YSYPDRL. |
| OrthoDB | EOG4FBHSB. |
Gene expression databases | |
| Bgee | Q5QNQ9. |
| CleanEx | MM_COL27A1. |
| Genevestigator | Q5QNQ9. |
Family and domain databases | |
| InterPro | IPR008160. Collagen. IPR008985. ConA-like_lec_gl_sf. IPR000885. Fib_collagen_C. IPR001791. Laminin_G. [Graphical view] |
| Pfam | PF01410. COLFI. 2 hits. PF01391. Collagen. 9 hits. [Graphical view] |
| ProDom | PD002078. Fib_collagen_C. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00038. COLFI. 1 hit. SM00210. TSPN. 1 hit. [Graphical view] |
| SUPFAM | SSF49899. ConA_like_lec_gl. 1 hit. |
| PROSITE | PS50025. LAM_G_DOMAIN. False negative. PS51461. NC1_FIB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | COL27A1. mouse. |
| NextBio | 400955. |
| SOURCE | Search... |
Entry information
| Entry name | CORA1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q5QNQ9 Secondary accession number(s): Q69Z83, Q80UA8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
