background:
May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.
Function:
May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.
Subunit:
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).
Subcellular Location:
Secreted. extracellular space. extracellular matrix.
Post-translational modifications:
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
A disulfide-bonded peptide called proline/arginine-rich protein or PARP is released from the N-terminus during extracellular processing and is subsequently retained in the cartilage matrix from which it can be isolated in significant amounts.
DISEASE:
Defects in COL11A2 are the cause of Stickler syndrome type 3 (STL3) [MIM:184168]. STL3 is an autosomal dominant non-ocular form of Stickler syndrome. Classical Stickler syndrome associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular symptoms are absent in STL3. Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable.
Defects in COL11A2 are the cause of autosomal recessive otospondylomegaepiphyseal dysplasia (OSMED) [MIM:215150]. OSMED is a skeletal dysplasia accompanied by severe hearing loss. The phenotype overlaps that of autosomal dominant skeletal disorders (Stickler and Marshall syndromes) but can be distinguished by disproportionately short limbs and lack of ocular involvement.
Defects in COL11A2 are the cause of Weissenbacher-Zweymueller syndrome (WZS) [MIM:277610]. WZS is an autosomal dominant disorder allelic with STL3 and OSMED. WZS is also referred to as heterozygous OSMED.
Defects in COL11A2 are the cause of deafness autosomal dominant type 13 (DFNA13) [MIM:601868]. DFNA13 is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
Defects in COL11A2 are the cause of deafness autosomal recessive type 53 (DFNB53) [MIM:609706].
Similarity:
Belongs to the fibrillar collagen family.
Contains 1 fibrillar collagen NC1 domain.
Contains 1 TSP N-terminal (TSPN) domain.
Database links:
UniProtKB/Swiss-Prot: P13942.5
Entrez Gene: 1302 Human
Omim: 120290 Human
SwissProt: P13942 Human
SwissProt: Q5JP94 Human
SwissProt: Q5STP6 Human
SwissProt: Q5SUI8 Human
SwissProt: Q7Z6C3 Human
Unigene: 390171 Human
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
|
|
