Q61245 (COBA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 109.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Collagen alpha-1(XI) 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 | 1804 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 | May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils. |
| Subunit structure | Trimers composed of three different chains: alpha 1(XI), alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational modification of alpha 1(II). Alpha 1(V) can also be found instead of alpha 3(XI)=1(II) 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 | Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. N-glycosylated By similarity. |
| Involvement in disease | Defects in Col11a1 are associated with chondrodysplasia, an autosomal recessive disease characterized by skeletal defects caused by abnormalities in the cartilage of limbs, ribs, mandibles and trachea. Ref.3 |
| Sequence similarities | Belongs to the fibrillar collagen family. Contains 6 collagen-like domains. Contains 1 fibrillar collagen NC1 domain. Contains 1 laminin G-like domain. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform Long (identifier: Q61245-1) 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. | ||||||
| Isoform Short (identifier: Q61245-2) The sequence of this isoform differs from the canonical sequence as follows: 329-413: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 34 | 34 | Potential | ||||||||
| Propeptide | 35 – 511 | 477 | N-terminal propeptide Potential | PRO_0000005777 | |||||||
| Chain | 512 – 1561 | 1050 | Collagen alpha-1(XI) chain | PRO_0000005778 | |||||||
| Propeptide | 1562 – 1804 | 243 | C-terminal propeptide | PRO_0000005779 | |||||||
Regions | |||||||||||
| Domain | 70 – 242 | 173 | Laminin G-like | ||||||||
| Domain | 440 – 488 | 49 | Collagen-like 1 | ||||||||
| Domain | 527 – 584 | 58 | Collagen-like 2 | ||||||||
| Domain | 567 – 623 | 57 | Collagen-like 3 | ||||||||
| Domain | 728 – 781 | 54 | Collagen-like 4 | ||||||||
| Domain | 1427 – 1482 | 56 | Collagen-like 5 | ||||||||
| Domain | 1481 – 1539 | 59 | Collagen-like 6 | ||||||||
| Domain | 1575 – 1803 | 229 | Fibrillar collagen NC1 | ||||||||
| Region | 229 – 417 | 189 | Nonhelical region | ||||||||
| Region | 418 – 506 | 89 | Triple-helical region (interrupted) | ||||||||
| Region | 507 – 509 | 3 | Short nonhelical segment | ||||||||
| Region | 510 – 527 | 18 | Telopeptide | ||||||||
| Region | 528 – 1540 | 1013 | Triple-helical region | ||||||||
| Region | 1541 – 1561 | 21 | Nonhelical region (C-terminal) | ||||||||
Sites | |||||||||||
| Metal binding | 1623 | 1 | Calcium By similarity | ||||||||
| Metal binding | 1625 | 1 | Calcium By similarity | ||||||||
| Metal binding | 1626 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 1628 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 1631 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 610 | 1 | Allysine | ||||||||
| Modified residue | 1450 | 1 | Allysine | ||||||||
| Glycosylation | 1638 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 60 ↔ 242 | By similarity | |||||||||
| Disulfide bond | 181 ↔ 235 | By similarity | |||||||||
| Disulfide bond | 1605 ↔ 1637 | By similarity | |||||||||
| Disulfide bond | 1628 | Interchain By similarity | |||||||||
| Disulfide bond | 1646 ↔ 1801 | By similarity | |||||||||
| Disulfide bond | 1712 ↔ 1755 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 329 – 413 | 85 | Missing in isoform Short. | VSP_001147 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 212 | 1 | T → A in BAA07367. Ref.1 | ||||||||
| Sequence conflict | 370 | 1 | L → V in BAA07367. Ref.1 | ||||||||
| Sequence conflict | 547 | 1 | A → T in BAA07367. Ref.1 | ||||||||
| Sequence conflict | 696 | 1 | P → S in BAA07367. Ref.1 | ||||||||
| Sequence conflict | 1065 | 1 | T → A in BAA07367. Ref.1 | ||||||||
| Sequence conflict | 1476 | 1 | T → S in BAA07367. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Coding sequence and alternative splicing of the mouse alpha 1(XI) collagen gene (Col11a1)." Yoshioka H., Inoguchi K., Khaleduzzaman M., Ninomiya Y., Andrikopoulos K., Ramirez F. Genomics 28:337-340(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), ALTERNATIVE SPLICING. Tissue: Embryo. |
| [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] (ISOFORM LONG). Tissue: Embryo. |
| [3] | "A fibrillar collagen gene, Col11a1, is essential for skeletal morphogenesis." Li Y., Lacerda D.A., Warman M.L., Beier D.R., Yoshioka H., Ninomiya Y., Oxford J.T., Morris N.P., Andrikopoulos K., Ramirez F., Wardell B.B., Lifferth G.D., Teuscher C., Woodward S.R., Taylor B.A., Seegmiller R.E., Olsen B.R. Cell 80:423-430(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 181-198, DISEASE. Strain: C57BL/6. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D38162 mRNA. Translation: BAA07367.1. BC052161 mRNA. Translation: AAH52161.1. S74574 mRNA. Translation: AAB33439.1. |
| IPI | IPI00230065. IPI00400048. |
| PIR | A55648. |
| RefSeq | NP_031755.2. NM_007729.2. |
| UniGene | Mm.209715. |
3D structure databases | |
| ProteinModelPortal | Q61245. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q61245. |
Proteomic databases | |
| PaxDb | Q61245. |
| PRIDE | Q61245. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000092155; ENSMUSP00000089793; ENSMUSG00000027966. |
| GeneID | 12814. |
| KEGG | mmu:12814. |
Organism-specific databases | |
| CTD | 1301. |
| MGI | MGI:88446. Col11a1. |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| GeneTree | ENSGT00700000104155. |
| HOGENOM | HOG000085654. |
| HOVERGEN | HBG004933. |
| KO | K06236. |
| OMA | HPGKEGQ. |
| OrthoDB | EOG49GKHM. |
Gene expression databases | |
| ArrayExpress | Q61245. |
| Bgee | Q61245. |
| CleanEx | MM_COL11A1. |
| Genevestigator | Q61245. |
Family and domain databases | |
| Gene3D | 2.60.120.200. 1 hit. |
| InterPro | IPR008160. Collagen. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR000885. Fib_collagen_C. IPR001791. Laminin_G. [Graphical view] |
| Pfam | PF01410. COLFI. 1 hit. PF01391. Collagen. 6 hits. PF02210. Laminin_G_2. 1 hit. [Graphical view] |
| ProDom | PD002078. Fib_collagen_C. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00038. COLFI. 1 hit. SM00282. LamG. 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 | |
| NextBio | 282270. |
| SOURCE | Search... |
Entry information
| Entry name | COBA1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q61245 Secondary accession number(s): Q64047, Q80WR4 | ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with
