P28481 (CO2A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 131.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Collagen alpha-1(II) chain Alternative name(s): Alpha-1 type II collagen Cleaved into the following 2 chains: | ||
| 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 | 1487 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces. |
| Subunit structure | Homotrimers of alpha 1(II) chains. |
| Subcellular location | Secreted › extracellular space › extracellular matrix By similarity. |
| Developmental stage | Expressed in chondrogenic tissues in advance of chondrocyte differentiation. Expressed early in embryogenesis at 9.5 days both in the cranial mesenchyme destined for the chondrocranium, and the sclerotome of the somites, and at 12.5 days in the primordia of the hyoid and the laryngeal cartilage. Detected in all the chondrogenic tissues of the axial and appendicular skeleton until the onset of endochondral ossification. Expression also observed in non-chondrogenic tissues such as the notochord. Also expressed much later in the tail tendon, at 16.5-18.5 days. Transiently expressed in the heart at 9.5-12.5 days, the epidermis at 10.5-14.5 days, the calvarial mesenchyme at 12.5-16.5 days, the inner ear at 14.5 days and the fetal brain from 9.5-14.5 days. Within the neural tube, expression is localized to the proliferative ventricular cells of the forebrain and midbrain of 9.5-10.5 day embryos, and subsequently, restricted to the rhombencephalic basal plate, the ventricular layer of the hindbrain and the cervical spinal cord. Ref.3 |
| 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 | Probably 3-hydroxylated on prolines by LEPREL1 By similarity. Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains. |
| Involvement in disease | Defects in Col2a1 are the cause of a phenotype resembling human spondyloepiphyseal dysplasia congenita (sedc). Homozygous sedc mice can be identified at birth by their small size and shortened trunk. Adults have shortened noses, dysplastic vertebrae, femora and tibias, and retinoschisis and hearing loss. |
| Sequence similarities | Belongs to the fibrillar collagen family. Contains 1 fibrillar collagen NC1 domain. Contains 1 VWFC domain. |
| Sequence caution | The sequence BAC25865.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 2 | EBI-738477,EBI-738477 |
Alternative products
| This entry describes 7 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: P28481-3) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 2 (identifier: P28481-1) Also known as: Long; The sequence of this isoform differs from the canonical sequence as follows: 114-142: Missing. | ||||||
| Isoform 3 (identifier: P28481-2) Also known as: Short; The sequence of this isoform differs from the canonical sequence as follows: 29-97: QEAGSCLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIICEDPDCLNPEIPFGECCPICPADLATASG → R 114-142: Missing. | ||||||
| Isoform 4 (identifier: P28481-4) The sequence of this isoform differs from the canonical sequence as follows: 103-113: Missing. 125-142: Missing. | ||||||
| Isoform 5 (identifier: P28481-5) The sequence of this isoform differs from the canonical sequence as follows: 114-124: Missing. 143-177: Missing. | ||||||
| Isoform 6 (identifier: P28481-6) The sequence of this isoform differs from the canonical sequence as follows: 103-113: Missing. 143-177: Missing. | ||||||
| Isoform 7 (identifier: P28481-7) The sequence of this isoform differs from the canonical sequence as follows: 29-97: QEAGSCLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIICEDPDCLNPEIPFGECCPICPADLATASG → R | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 25 | 25 | Potential | ||||||||
| Propeptide | 26 – 181 | 156 | N-terminal propeptide By similarity | PRO_0000005732 | |||||||
| Chain | 182 – 1241 | 1060 | Collagen alpha-1(II) chain | PRO_0000005733 | |||||||
| Chain | 1242 – 1487 | 246 | Chondrocalcin | PRO_0000005734 | |||||||
Regions | |||||||||||
| Domain | 32 – 89 | 58 | VWFC | ||||||||
| Domain | 1253 – 1487 | 235 | Fibrillar collagen NC1 | ||||||||
| Region | 201 – 1214 | 1014 | Triple-helical region | ||||||||
| Region | 1215 – 1241 | 27 | Nonhelical region (C-terminal) | ||||||||
Sites | |||||||||||
| Metal binding | 1301 | 1 | Calcium By similarity | ||||||||
| Metal binding | 1303 | 1 | Calcium By similarity | ||||||||
| Metal binding | 1304 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 1306 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 1309 | 1 | Calcium By similarity | ||||||||
| Site | 181 – 182 | 2 | Cleavage; by procollagen N-endopeptidase By similarity | ||||||||
| Site | 1241 – 1242 | 2 | Cleavage; by procollagen C-endopeptidase By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 190 | 1 | 5-hydroxylysine By similarity | ||||||||
| Modified residue | 287 | 1 | 5-hydroxylysine By similarity | ||||||||
| Modified residue | 299 | 1 | 5-hydroxylysine By similarity | ||||||||
| Modified residue | 308 | 1 | 5-hydroxylysine By similarity | ||||||||
| Modified residue | 374 | 1 | 5-hydroxylysine By similarity | ||||||||
| Modified residue | 608 | 1 | 5-hydroxylysine By similarity | ||||||||
| Modified residue | 620 | 1 | 5-hydroxylysine By similarity | ||||||||
| Modified residue | 670 | 1 | 3-hydroxyproline By similarity | ||||||||
| Modified residue | 907 | 1 | 3-hydroxyproline By similarity | ||||||||
| Modified residue | 1144 | 1 | 3-hydroxyproline By similarity | ||||||||
| Modified residue | 1186 | 1 | 3-hydroxyproline By similarity | ||||||||
| Modified residue | 1201 | 1 | 3-hydroxyproline By similarity | ||||||||
| Modified residue | 1207 | 1 | 3-hydroxyproline By similarity | ||||||||
| Modified residue | 1213 | 1 | 3-hydroxyproline By similarity | ||||||||
| Glycosylation | 190 | 1 | O-linked (Gal...) By similarity | ||||||||
| Glycosylation | 287 | 1 | O-linked (Gal...) By similarity | ||||||||
| Glycosylation | 299 | 1 | O-linked (Gal...) By similarity | ||||||||
| Glycosylation | 308 | 1 | O-linked (Gal...) By similarity | ||||||||
| Glycosylation | 374 | 1 | O-linked (Gal...) By similarity | ||||||||
| Glycosylation | 608 | 1 | O-linked (Gal...) By similarity | ||||||||
| Glycosylation | 620 | 1 | O-linked (Gal...) By similarity | ||||||||
| Disulfide bond | 1283 ↔ 1315 | By similarity | |||||||||
| Disulfide bond | 1289 | Interchain (with C-1306) By similarity | |||||||||
| Disulfide bond | 1306 | Interchain (with C-1289) By similarity | |||||||||
| Disulfide bond | 1323 ↔ 1485 | By similarity | |||||||||
| Disulfide bond | 1393 ↔ 1438 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 29 – 97 | 69 | QEAGS…ATASG → R in isoform 3 and isoform 7. | VSP_022780 | |||||||
| Alternative sequence | 103 – 113 | 11 | Missing in isoform 4 and isoform 6. | VSP_022781 | |||||||
| Alternative sequence | 114 – 142 | 29 | Missing in isoform 2 and isoform 3. | VSP_022782 | |||||||
| Alternative sequence | 114 – 124 | 11 | Missing in isoform 5. | VSP_022783 | |||||||
| Alternative sequence | 125 – 142 | 18 | Missing in isoform 4. | VSP_022784 | |||||||
| Alternative sequence | 143 – 177 | 35 | Missing in isoform 5 and isoform 6. | VSP_022785 | |||||||
| Natural variant | 989 | 1 | R → C in sedc mice. Ref.7 | ||||||||
Experimental info | |||||||||||
| Sequence conflict | 97 | 1 | G → GR in AAA68100. Ref.1 | ||||||||
| Sequence conflict | 97 | 1 | G → GR in AAA68101. Ref.1 | ||||||||
| Sequence conflict | 97 | 1 | G → GR in AAA68099. Ref.1 | ||||||||
| Sequence conflict | 97 | 1 | G → GR in AAA68102. Ref.1 | ||||||||
| Sequence conflict | 272 | 1 | Q → M in AAA68100. Ref.1 | ||||||||
| Sequence conflict | 272 | 1 | Q → M in AAA68101. Ref.1 | ||||||||
| Sequence conflict | 272 | 1 | Q → M in AAA68099. Ref.1 | ||||||||
| Sequence conflict | 272 | 1 | Q → M in AAA68102. Ref.1 | ||||||||
| Sequence conflict | 539 | 1 | T → A in AAA68100. Ref.1 | ||||||||
| Sequence conflict | 539 | 1 | T → A in AAA68101. Ref.1 | ||||||||
| Sequence conflict | 539 | 1 | T → A in AAA68099. Ref.1 | ||||||||
| Sequence conflict | 539 | 1 | T → A in AAA68102. Ref.1 | ||||||||
| Sequence conflict | 806 | 1 | V → A in AAA68100. Ref.1 | ||||||||
| Sequence conflict | 806 | 1 | V → A in AAA68101. Ref.1 | ||||||||
| Sequence conflict | 806 | 1 | V → A in AAA68099. Ref.1 | ||||||||
| Sequence conflict | 806 | 1 | V → A in AAA68102. Ref.1 | ||||||||
| Sequence conflict | 824 | 1 | R → P in AAA68100. Ref.1 | ||||||||
| Sequence conflict | 824 | 1 | R → P in AAA68101. Ref.1 | ||||||||
| Sequence conflict | 824 | 1 | R → P in AAA68099. Ref.1 | ||||||||
| Sequence conflict | 947 | 1 | Q → E in AAA68100. Ref.1 | ||||||||
| Sequence conflict | 947 | 1 | Q → E in AAA68101. Ref.1 | ||||||||
| Sequence conflict | 947 | 1 | Q → E in AAA68099. Ref.1 | ||||||||
| Sequence conflict | 947 | 1 | Q → E in AAA68102. Ref.1 | ||||||||
| Sequence conflict | 1119 | 1 | G → R in AAH51383. Ref.2 | ||||||||
| Sequence conflict | 1141 – 1145 | 5 | LPGPP → SAWPS in AAC06113. Ref.4 | ||||||||
Sequences
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Mouse type II collagen gene. Complete nucleotide sequence, exon structure, and alternative splicing." Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E. J. Biol. Chem. 266:16862-16869(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7). Strain: C57BL/6. Tissue: Brain, Eye and Olfactory epithelium. |
| [3] | "Expression of the mouse alpha 1(II) collagen gene is not restricted to cartilage during development." Cheah K.S., Lau E.T., Au P.K., Tam P.P. Development 111:945-953(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, DEVELOPMENTAL STAGE. |
| [4] | "The mouse Col2a-1 gene is highly conserved and is linked to Int-1 on chromosome 15." Cheah K.S., Au P.K., Lau E.T., Little P.F., Stubbs L. Mamm. Genome 1:171-183(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28; 1031-1145 AND 1359-1487. |
| [5] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 597-1487. Strain: C57BL/6J. Tissue: Head. |
| [6] | "Specific hybridization probes for mouse type I, II, III and IX collagen mRNAs." Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E. Biochim. Biophys. Acta 1089:241-243(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1483-1487. |
| [7] | "A missense mutation in the mouse Col2a1 gene causes spondyloepiphyseal dysplasia congenita, hearing loss, and retinoschisis." Donahue L.R., Chang B., Mohan S., Miyakoshi N., Wergedal J.E., Baylink D.J., Hawes N.L., Rosen C.J., Ward-Bailey P., Zheng Q.Y., Bronson R.T., Johnson K.R., Davisson M.T. J. Bone Miner. Res. 18:1612-1621(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SEDC CYS-989. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M65161 Genomic DNA. Translation: AAA68099.1. M65161 Genomic DNA. Translation: AAA68100.1. M65161 Genomic DNA. Translation: AAA68101.1. M65161 Genomic DNA. Translation: AAA68102.1. BC030913 mRNA. Translation: AAH30913.1. BC051383 mRNA. Translation: AAH51383.1. BC052326 mRNA. Translation: AAH52326.1. BC082331 mRNA. Translation: AAH82331.1. S63190 Genomic DNA. Translation: AAB19627.1. M63708 Genomic DNA. Translation: AAA37436.1. M63709 Genomic DNA. Translation: AAC06113.1. M63710 Genomic DNA. Translation: AAA37435.1. AK028295 mRNA. Translation: BAC25865.1. Different initiation. X57982 Genomic DNA. Translation: CAA41047.1. | ||||||||||||
| IPI | IPI00471183. IPI00621255. IPI00622890. IPI00623625. IPI00828467. IPI00828653. IPI00828753. | ||||||||||||
| PIR | A41182. B41182. | ||||||||||||
| RefSeq | NP_001106987.2. NM_001113515.2. NP_112440.2. NM_031163.3. | ||||||||||||
| UniGene | Mm.2423. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P28481. | ||||||||||||
| SMR | P28481. Positions 29-96, 1271-1487. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P28481. 1 interaction. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P28481. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P28481. | ||||||||||||
| PRIDE | P28481. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSMUST00000023123; ENSMUSP00000023123; ENSMUSG00000022483. ENSMUST00000088355; ENSMUSP00000085693; ENSMUSG00000022483. | ||||||||||||
| GeneID | 12824. | ||||||||||||
| KEGG | mmu:12824. | ||||||||||||
| UCSC | uc007xlp.2. mouse. uc007xlq.2. mouse. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 1280. | ||||||||||||
| MGI | MGI:88452. Col2a1. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | NOG12793. | ||||||||||||
| GeneTree | ENSGT00660000095287. | ||||||||||||
| HOVERGEN | HBG004933. | ||||||||||||
| InParanoid | P28481. | ||||||||||||
| KO | K06236. | ||||||||||||
| OMA | SSCRICV. | ||||||||||||
| OrthoDB | EOG4FTW1C. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P28481. | ||||||||||||
| Bgee | P28481. | ||||||||||||
| CleanEx | MM_COL2A1. | ||||||||||||
| Genevestigator | P28481. | ||||||||||||
| GermOnline | ENSMUSG00000022483. Mus musculus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR008160. Collagen. IPR000885. Fib_collagen_C. IPR001007. VWF_C. [Graphical view] | ||||||||||||
| Pfam | PF01410. COLFI. 1 hit. PF01391. Collagen. 11 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... | ||||||||||||
Other | |||||||||||||
| ChiTaRS | COL2A1. mouse. | ||||||||||||
| EvolutionaryTrace | P28481. | ||||||||||||
| NextBio | 282306. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | CO2A1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P28481 Secondary accession number(s): Q61428 Q8K0N6 | ||||||||
| Entry history |
| ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
