Collagen, type X, alpha 1

COL10A1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1GR3
Identifiers
Aliases	COL10A1 , collagen type X alpha 1 chain
External IDs	OMIM: 120110; MGI: 88445; HomoloGene: 55466; GeneCards: COL10A1; OMA:COL10A1 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) [1] Band 6q22.1 Start 116,118,909 bp [1] End 116,158,747 bp [1]
Gene location (Mouse) Chr. Chromosome 10 (mouse) [2] Band 10 B1|10 18.85 cM Start 34,265,977 bp [2] End 34,273,081 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tibia periodontal fiber buccal mucosa cell cartilage tissue mucosa of paranasal sinus trabecular bone visceral pleura gallbladder Achilles tendon pancreatic epithelial cell Top expressed in humerus intercostal muscle tibia forearm trachea radius epiphyseal plate ulna bones of pectoral girdle human fetus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding metal ion binding extracellular matrix structural constituent extracellular matrix structural constituent conferring tensile strength Cellular component cell cortex collagen endoplasmic reticulum lumen extracellular region extracellular matrix extracellular space collagen-containing extracellular matrix Biological process skeletal system development extracellular matrix organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1300 12813 Ensembl ENSG00000123500 ENSMUSG00000039462 UniProt Q03692 Q05306 RefSeq (mRNA) NM_000493 NM_009925 RefSeq (protein) NP_000484 NP_034055 Location (UCSC) Chr 6: 116.12 – 116.16 Mb Chr 10: 34.27 – 34.27 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Collagen alpha-1(X) chain is a protein that in humans is a member of the collagen family encoded by the COL10A1 gene. ^{[5] [6]}

This gene encodes the alpha chain of type X collagen, a short chain collagen expressed by hypertrophic chondrocytes during endochondral ossification. Unlike type VIII collagen, the other short chain collagen, type X collagen is a homotrimer. Type X collagen has a short triple helical collagen domain flanked by the N-terminal NC2 and the C-terminal NC1 domains. The C-terminal NC1 domain has complement C1q-like structure. Collagen X forms hexamer complexes through the association of NC1 regions. ^[7] Mutations in this gene are associated with Schmid type metaphyseal chondrodysplasia (SMCD) and Japanese type spondylometaphyseal dysplasia (SMD). ^[6]

DDR2 is a collagen receptor for it. ^[8]

Recent studies into the early detection of colon cancer have identified COL10A1 protein levels in serum as a potential diagnostic biomarker candidate to detect both adenoma lesions and tumor. ^[9]

Collagen alpha-1(X) undergoes degradation in the active growth plate releasing an intact NC1 region with a small amount of collagenous region attached. This degradation byproduct has been deemed CXM and has potential to be a useful biomarker to assess real time growth velocity in children and fracture healing in adults. ^[10]

References

1. GRCh38: Ensembl release 89: ENSG00000123500 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000039462 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Apte S, Mattei MG, Olsen BR (May 1991). "Cloning of human alpha 1(X) collagen DNA and localization of the COL10A1 gene to the q21-q22 region of human chromosome 6". FEBS Letters. 282 (2): 393–396. doi: 10.1016/0014-5793(91)80521-4 . PMID   2037056. S2CID   6753444.
6. "Entrez Gene: COL10A1 collagen, type X, alpha 1(Schmid metaphyseal chondrodysplasia)".
7. Kwan et al. 2005
8. Leitinger B, Kwan AP (August 2006). "The discoidin domain receptor DDR2 is a receptor for type X collagen". Matrix Biology. 25 (6): 355–364. doi:10.1016/j.matbio.2006.05.006. PMID   16806867.
9. Solé X, Crous-Bou M, Cordero D, Olivares D, Guinó E, Sanz-Pamplona R, et al. (September 2014). "Discovery and validation of new potential biomarkers for early detection of colon cancer". PLOS ONE. 9 (9) e106748. Bibcode:2014PLoSO...9j6748S. doi: 10.1371/journal.pone.0106748 . PMC   4162553 . PMID   25215506.
10. Coghlan RF, Oberdorf JA, Sienko S, Aiona MD, Boston BA, Connelly KJ, et al. (December 2017). "A degradation fragment of type X collagen is a real-time marker for bone growth velocity". Science Translational Medicine. 9 (419) eaan4669. doi:10.1126/scitranslmed.aan4669. PMC   6516194 . PMID   29212713.

Further reading

• Kuivaniemi H, Tromp G, Prockop DJ (1997). "Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels". Human Mutation. 9 (4): 300–315. doi: 10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9 . PMID   9101290. S2CID   6890740.
• Kirsch T, Pfäffle M (September 1992). "Selective binding of anchorin CII (annexin V) to type II and X collagen and to chondrocalcin (C-propeptide of type II collagen). Implications for anchoring function between matrix vesicles and matrix proteins". FEBS Letters. 310 (2): 143–147. doi: 10.1016/0014-5793(92)81316-E . PMID   1397263. S2CID   9498732.
• Reichenberger E, Beier F, LuValle P, Olsen BR, von der Mark K, Bertling WM (October 1992). "Genomic organization and full-length cDNA sequence of human collagen X". FEBS Letters. 311 (3): 305–310. doi: 10.1016/0014-5793(92)81126-7 . PMID   1397333. S2CID   12022346.
• Apte SS, Seldin MF, Hayashi M, Olsen BR (May 1992). "Cloning of the human and mouse type X collagen genes and mapping of the mouse type X collagen gene to chromosome 10". European Journal of Biochemistry. 206 (1): 217–224. doi: 10.1111/j.1432-1033.1992.tb16919.x . PMID   1587271.
• Reichenberger E, Aigner T, von der Mark K, Stöss H, Bertling W (December 1991). "In situ hybridization studies on the expression of type X collagen in fetal human cartilage". Developmental Biology. 148 (2): 562–572. doi:10.1016/0012-1606(91)90274-7. PMID   1743401.
• Thomas JT, Cresswell CJ, Rash B, Nicolai H, Jones T, Solomon E, et al. (December 1991). "The human collagen X gene. Complete primary translated sequence and chromosomal localization". The Biochemical Journal. 280 ( Pt 3) (Pt 3): 617–623. doi:10.1042/bj2800617. PMC   1130499 . PMID   1764025.
• Bonaventure J, Chaminade F, Maroteaux P (July 1995). "Mutations in three subdomains of the carboxy-terminal region of collagen type X account for most of the Schmid metaphyseal dysplasias". Human Genetics. 96 (1): 58–64. doi:10.1007/BF00214187. PMID   7607655. S2CID   20888881.
• McIntosh I, Abbott MH, Francomano CA (1995). "Concentration of mutations causing Schmid metaphyseal chondrodysplasia in the C-terminal noncollagenous domain of type X collagen". Human Mutation. 5 (2): 121–125. doi:10.1002/humu.1380050204. PMID   7749409. S2CID   26291298.
• Chan D, Cole WG, Rogers JG, Bateman JF (March 1995). "Type X collagen multimer assembly in vitro is prevented by a Gly618 to Val mutation in the alpha 1(X) NC1 domain resulting in Schmid metaphyseal chondrodysplasia". The Journal of Biological Chemistry. 270 (9): 4558–4562. doi: 10.1074/jbc.270.9.4558 . PMID   7876225.
• McIntosh I, Abbott MH, Warman ML, Olsen BR, Francomano CA (February 1994). "Additional mutations of type X collagen confirm COL10A1 as the Schmid metaphyseal chondrodysplasia locus". Human Molecular Genetics. 3 (2): 303–307. doi:10.1093/hmg/3.2.303. PMID   8004099.
• Dharmavaram RM, Elberson MA, Peng M, Kirson LA, Kelley TE, Jimenez SA (March 1994). "Identification of a mutation in type X collagen in a family with Schmid metaphyseal chondrodysplasia". Human Molecular Genetics. 3 (3): 507–509. doi:10.1093/hmg/3.3.507. PMID   8012364.
• Warman ML, Abbott M, Apte SS, Hefferon T, McIntosh I, Cohn DH, et al. (September 1993). "A type X collagen mutation causes Schmid metaphyseal chondrodysplasia". Nature Genetics. 5 (1): 79–82. doi:10.1038/ng0993-79. PMID   8220429. S2CID   196834.
• Wallis GA, Rash B, Sweetman WA, Thomas JT, Super M, Evans G, et al. (February 1994). "Amino acid substitutions of conserved residues in the carboxyl-terminal domain of the alpha 1(X) chain of type X collagen occur in two unrelated families with metaphyseal chondrodysplasia type Schmid". American Journal of Human Genetics. 54 (2): 169–178. PMC   1918153 . PMID   8304336.
• Pokharel RK, Alimsardjono H, Uno K, Fujii S, Shiba R, Matsuo M (December 1995). "A novel mutation substituting tryptophan with arginine in the carboxyl-terminal, non-collagenous domain of collagen X in a case of Schmid metaphyseal chondrodysplasia". Biochemical and Biophysical Research Communications. 217 (3): 1157–1162. doi:10.1006/bbrc.1995.2890. hdl: 20.500.14094/D1001967 . PMID   8554571.
• Wallis GA, Rash B, Sykes B, Bonaventure J, Maroteaux P, Zabel B, et al. (June 1996). "Mutations within the gene encoding the alpha 1 (X) chain of type X collagen (COL10A1) cause metaphyseal chondrodysplasia type Schmid but not several other forms of metaphyseal chondrodysplasia". Journal of Medical Genetics. 33 (6): 450–457. doi:10.1136/jmg.33.6.450. PMC   1050629 . PMID   8782043.
• Stratakis CA, Orban Z, Burns AL, Vottero A, Mitsiades CS, Marx SJ, et al. (December 1996). "Dideoxyfingerprinting (ddF) analysis of the type X collagen gene (COL10A1) and identification of a novel mutation (S671P) in a kindred with Schmid metaphyseal chondrodysplasia". Biochemical and Molecular Medicine. 59 (2): 112–117. doi: 10.1006/bmme.1996.0075 . PMID   8986632.
• Beier F, Eerola I, Vuorio E, Luvalle P, Reichenberger E, Bertling W, et al. (December 1996). "Variability in the upstream promoter and intron sequences of the human, mouse and chick type X collagen genes". Matrix Biology. 15 (6): 415–422. doi:10.1016/S0945-053X(96)90160-2. PMID   9049979.
• Ikegawa S, Nakamura K, Nagano A, Haga N, Nakamura Y (1997). "Mutations in the N-terminal globular domain of the type X collagen gene (COL10A1) in patients with Schmid metaphyseal chondrodysplasia". Human Mutation. 9 (2): 131–135. doi: 10.1002/(SICI)1098-1004(1997)9:2<131::AID-HUMU5>3.0.CO;2-C . PMID   9067753. S2CID   22871274.