Information about Type I Hair Keratin

Hair keratin is a type of keratin found in hair and nails. There are two types of hair keratin:

• the acidic type I hair keratin
• type I hair keratin 1, KRT31

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Proteins are large organic compounds made of amino acids arranged in a linear chain and joined together by peptide bonds between the carboxyl and amino groups of adjacent amino acid residues.
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dimer refers to a molecule composed of two identical subunits or monomers linked together.

Chemistry

The molecules in a dimer are connected by covalent bonds or weaker interactions such as hydrogen bonds.
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Type II hair keratin is one of the two types of hair keratin. It is a basic protein which heterodimerizes with type I hair keratins to form hair and nails.

See also

• Monilethrix

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Hair is a filamentous outgrowth of protein, found only on mammals. It projects from the epidermis, though it grows from hair follicles deep in the dermis. Although many other organisms, especially insects, show filamentous outgrowths, these are not considered "hair".
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nail is a horn-like structure at the end of a human's or an animal's finger or toe. See also claw.

Parts of the nail

Anatomically fingernails and toenails
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Proteins are large organic compounds made of amino acids arranged in a linear chain and joined together by peptide bonds between the carboxyl and amino groups of adjacent amino acid residues.
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Fibrous proteins, also called scleroproteins, are long filamentous protein molecules that form one of the two main classes of tertiary structure protein (the other being globular proteins). Fibrous proteins are only found in animals.
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Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, ^[1] making up about 25% of the total protein content.

Uses

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Identifiers
Symbol COL1A2
Alt. Symbols OI4

Entrez 1278
HUGO 2198
OMIM 120160

RefSeq NM_000089
UniProt P08123
Other data

Locus Chr. 7 q21.3-22.1 Type-I collagen is the most abundant collagen of the human body.
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COL1A1 (collagen, type I, alpha 1) is a human gene that is one of several genes that provide instructions for making components of collagen. Collagen is a protein that strengthens and supports many tissues in the body, including cartilage, bone, tendon, skin and the white
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Type-II collagen is the basis for articular cartilage and hyaline cartilage.

It makes up 50% of all protein in cartilage and 85-90% of collagen of articular cartilage.
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COL2A1 (collagen, type II, alpha 1 (primary osteoarthritis, spondyloepiphyseal dysplasia, congenital)) is a human gene that provides instructions for the production of the pro-alpha1(II) chain of type II collagen.
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Type-III collagen is a fibrous scleroprotein in bone and cartilage and tendon and other connective tissue; yields gelatin on boiling.

Scleroprotein is a simple protein found in horny and cartilaginous tissues and in the lens of the eye.
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Type-IV collagen is a type of collagen found primarily in the basal lamina. The C-terminus domain is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel.
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Type-V collagen is a form of fibrillar^[1] collagen associated with classical Ehlers-Danlos syndrome.

Genes

• COL5A1 , COL5A2 , COL5A3

References

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COL11A2 (collagen, type XI, alpha 2) is a human gene that is one of several genes that provide instructions for the production of type XI collagen. The COL11A2 gene produces one component of this type of collagen, called the pro-alpha2(XI) chain.
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Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion ^[1].
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Type XVIII collagen is a type of collagen which can be cleaved to form endostatin.

External links

• MeSH Collagen+Type+XVIII

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Keratins are a family of fibrous structural proteins; tough and insoluble, they form the hard but nonmineralized structures found in reptiles, birds, amphibians and mammals. They are rivaled as biological materials in toughness only by chitin.
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Cytokeratins are intermediate filament keratins found in the intracytoplasmic cytoskeleton of epithelial tissue. There are two types of cytokeratins: the low weight, acidic type I cytokeratins and the high weight, basic or neutral type II cytokeratins.
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Type I keratins (or Type I cytokeratins) constitutes the Type I intermediate filaments (IFs) of the intracytoplasmatic cytoskeleton, which is present in all mammalian epithelial cells.
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Keratin 10 is a type I cytokeratin. Mutations in the gene encoding this protein are associated with the variants of epidermolytic hyperkeratosis in which the palms and soles of the feet are unaffected.
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Keratin 12 is a keratin found expressed in corneal epithelia. Mutations in the gene encoding this protein lead to Meesmann corneal dystrophy.


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Keratin 13 is a type I cytokeratin, it is paired with keratin 4 and found in the suprabasal layers of non-cornified stratified epithelia. Mutations in the gene encoding this protein and keratin 4 have been associated with the autosomal dominant disorder White Sponge Nevus.
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Keratin 14 is a type I cytokeratin. It is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells.
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Keratin 15 is a type I cytokeratin. It is found in some progenitor basal cells within complex epithelia.


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Keratin 16 is a type I cytokeratin. It is paired with keratin 6 in a number of epithelial tissues, including nail bed, esophagus, tongue, and hair follicles. Mutations in the gene encoding this protein are associated with the genetic skin disorders pachyonychia congenita,
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Keratin 17 is a type I cytokeratin. It is found in nail beds, hair follicles, sebaceous glands, and other epidermal appendages. Mutations in the gene encoding this protein lead to Jackson-Lawler type pachyonychia congenita and steatocystoma multiplex.
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Keratin 18 is a type I cytokeratin. It is, together with its filament partner keratin 8, perhaps the most commonly found products of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body.
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