Collagen, type X, alpha 1

Collagen, type X, alpha 1
PDB rendering based on 1gr3.
Available structures PDB 1gr3
Identifiers
Symbols	COL10A1;
External IDs	OMIM: 120110 MGI: 88445 HomoloGene: 55466 GeneCards: COL10A1 Gene
Gene Ontology Molecular function • metal ion binding Cellular component • extracellular region • collagen • cell cortex Biological process • skeletal system development Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1300	12813
Ensembl	ENSG00000123500	ENSMUSG00000039462
UniProt	Q03692	Q05306
RefSeq (mRNA)	NM_000493	NM_009925.4
RefSeq (protein)	NP_000484	NP_034055.1
Location (UCSC)	Chr 6: 116.44 – 116.48 Mb	Chr 10: 34.11 – 34.12 Mb
PubMed search	[1]	[2]

Collagen alpha-1(X) chain is a protein that in humans is encoded by the COL10A1 gene.^[1][2]

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. Mutations in this gene are associated with Schmid type metaphyseal chondrodysplasia (SMCD) and Japanese type spondylometaphyseal dysplasia (SMD).^[2]

DDR2 is a collagen receptor for it.^[3]

References

1. ^ Apte S, Mattei MG, Olsen BR (Jul 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 Lett 282 (2): 393–6. doi:10.1016/0014-5793(91)80521-4. PMID 2037056. 
2. ^ ^{a b} "Entrez Gene: COL10A1 collagen, type X, alpha 1(Schmid metaphyseal chondrodysplasia)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1300. 
3. ^ Leitinger B, Kwan AP (August 2006). "The discoidin domain receptor DDR2 is a receptor for type X collagen". Matrix Biol. 25 (6): 355–64. doi:10.1016/j.matbio.2006.05.006. PMID 16806867. http://linkinghub.elsevier.com/retrieve/pii/S0945-053X(06)00058-8. 

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.". Hum. Mutat. 9 (4): 300–15. doi:10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9. PMID 9101290. 
• Kirsch T, Pfäffle M (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 Lett. 310 (2): 143–7. doi:10.1016/0014-5793(92)81316-E. PMID 1397263. 
• Reichenberger E, Beier F, LuValle P, et al. (1992). "Genomic organization and full-length cDNA sequence of human collagen X.". FEBS Lett. 311 (3): 305–10. doi:10.1016/0014-5793(92)81126-7. PMID 1397333. 
• Apte SS, Seldin MF, Hayashi M, Olsen BR (1992). "Cloning of the human and mouse type X collagen genes and mapping of the mouse type X collagen gene to chromosome 10.". Eur. J. Biochem. 206 (1): 217–24. doi:10.1111/j.1432-1033.1992.tb16919.x. PMID 1587271. 
• Reichenberger E, Aigner T, von der Mark K, et al. (1992). "In situ hybridization studies on the expression of type X collagen in fetal human cartilage.". Dev. Biol. 148 (2): 562–72. doi:10.1016/0012-1606(91)90274-7. PMID 1743401. 
• Thomas JT, Cresswell CJ, Rash B, et al. (1992). "The human collagen X gene. Complete primary translated sequence and chromosomal localization.". Biochem. J. 280 ( Pt 3): 617–23. PMC 1130499. PMID 1764025. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1130499. 
• Bonaventure J, Chaminade F, Maroteaux P (1995). "Mutations in three subdomains of the carboxy-terminal region of collagen type X account for most of the Schmid metaphyseal dysplasias.". Hum. Genet. 96 (1): 58–64. doi:10.1007/BF00214187. PMID 7607655. 
• McIntosh I, Abbott MH, Francomano CA (1995). "Concentration of mutations causing Schmid metaphyseal chondrodysplasia in the C-terminal noncollagenous domain of type X collagen.". Hum. Mutat. 5 (2): 121–5. doi:10.1002/humu.1380050204. PMID 7749409. 
• Chan D, Cole WG, Rogers JG, Bateman JF (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.". J. Biol. Chem. 270 (9): 4558–62. doi:10.1074/jbc.270.9.4558. PMID 7876225. 
• McIntosh I, Abbott MH, Warman ML, et al. (1994). "Additional mutations of type X collagen confirm COL10A1 as the Schmid metaphyseal chondrodysplasia locus.". Hum. Mol. Genet. 3 (2): 303–7. doi:10.1093/hmg/3.2.303. PMID 8004099. 
• Dharmavaram RM, Elberson MA, Peng M, et al. (1994). "Identification of a mutation in type X collagen in a family with Schmid metaphyseal chondrodysplasia.". Hum. Mol. Genet. 3 (3): 507–9. doi:10.1093/hmg/3.3.507. PMID 8012364. 
• Warman ML, Abbott M, Apte SS, et al. (1993). "A type X collagen mutation causes Schmid metaphyseal chondrodysplasia.". Nat. Genet. 5 (1): 79–82. doi:10.1038/ng0993-79. PMID 8220429. 
• Wallis GA, Rash B, Sweetman WA, et al. (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.". Am. J. Hum. Genet. 54 (2): 169–78. PMC 1918153. PMID 8304336. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1918153. 
• Pokharel RK, Alimsardjono H, Uno K, et al. (1996). "A novel mutation substituting tryptophan with arginine in the carboxyl-terminal, non-collagenous domain of collagen X in a case of Schmid metaphyseal chondrodysplasia.". Biochem. Biophys. Res. Commun. 217 (3): 1157–62. doi:10.1006/bbrc.1995.2890. PMID 8554571. 
• Wallis GA, Rash B, Sykes B, et al. (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.". J. Med. Genet. 33 (6): 450–7. doi:10.1136/jmg.33.6.450. PMC 1050629. PMID 8782043. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1050629. 
• Stratakis CA, Orban Z, Burns AL, et al. (1997). "Dideoxyfingerprinting (ddF) analysis of the type X collagen gene (COL10A1) and identification of a novel mutation (S671P) in a kindred with Schmid metaphyseal chondrodysplasia.". Biochem. Mol. Med. 59 (2): 112–7. doi:10.1006/bmme.1996.0075. PMID 8986632. 
• Beier F, Eerola I, Vuorio E, et al. (1997). "Variability in the upstream promoter and intron sequences of the human, mouse and chick type X collagen genes.". Matrix Biol. 15 (6): 415–22. doi:10.1016/S0945-053X(96)90160-2. PMID 9049979. 
• Ikegawa S, Nakamura K, Nagano A, et al. (1997). "Mutations in the N-terminal globular domain of the type X collagen gene (COL10A1) in patients with Schmid metaphyseal chondrodysplasia.". Hum. Mutat. 9 (2): 131–5. doi:10.1002/(SICI)1098-1004(1997)9:2<131::AID-HUMU5>3.0.CO;2-C. PMID 9067753.