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Biotechnological applications of selenocysteine include use of 73 Se-labeled Sec (half-life of 73 Se = 7.2 hours) in positron emission tomography (PET) studies and 75 Se-labeled Sec (half-life of 75 Se = 118.5 days) in specific radiolabeling, facilitation of phase determination by multiwavelength anomalous diffraction in X-ray crystallography ...
1281 12825 Ensembl ENSG00000168542 ENSMUSG00000026043 UniProt P02461 P08121 RefSeq (mRNA) NM_000090 NM_001376916 NM_009930 RefSeq (protein) NP_000081 NP_034060 Location (UCSC) Chr 2: 188.97 – 189.01 Mb Chr 1: 45.35 – 45.39 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Type III Collagen is a homotrimer, or a protein composed of three identical peptide chains (monomers), each ...
Collagen VI (ColVI) is a type of collagen primarily associated with the extracellular matrix of skeletal muscle. [1] ColVI maintains regularity in muscle function and stabilizes the cell membrane. [ 2 ]
Collagen VI is a major structural component of microfibrils. The basic structural unit of collagen VI is a heterotrimer of the alpha1(VI), alpha2(VI), and alpha3(VI) chains. The alpha2(VI) and alpha3(VI) chains are encoded by the COL6A2 and COL6A3 genes, respectively. The protein encoded by this gene is the alpha 1 subunit of type VI collagen ...
Collagen alpha-1(XIII) chain is a protein that in humans is encoded by the COL13A1 gene. [5]This gene encodes the alpha chain of one of the nonfibrillar collagens. The function of this gene product is not known, however, it has been detected at low levels in all connective tissue-producing cells so it may serve a general function in connective tissues.
Collagen XVII is a homotrimer of three alpha1(XVII)-chains [11] and a transmembrane protein in type II orientation. Each 180 kD a-chain contains a globular intracellular domain of approximately 70 kDa, which interacts with beta4-integrin, plectin, and BP230 [12] [13] and is necessary for the stable attachment of hemidesmosomes to keratin intermediate filaments.
Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by homotrimers of collagen, type II, alpha 1 chains. It makes up 50% of all protein in cartilage and 85–90% of collagen of articular cartilage.
The COL11A1 gene encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen. Type XI collagen is a heterotrimer but the third alpha chain is a post-translationally modified alpha 1 type II chain. Three transcript variants encoding different isoforms have been identified for this gene. [6]
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