Type I collagen

collagen, type I, alpha 1
Identifiers
SymbolCOL1A1
NCBI gene1277
HGNC2197
OMIM120150
RefSeqNM_000088
UniProtP02452
Other data
LocusChr. 17 q21.3-q22
Search for
StructuresSwiss-model
DomainsInterPro
collagen, type I, alpha 2
Identifiers
SymbolCOL1A2
Alt. symbolsOI4
NCBI gene1278
HGNC2198
OMIM120160
RefSeqNM_000089
UniProtP08123
Other data
LocusChr. 7 q21.3-22.1
Search for
StructuresSwiss-model
DomainsInterPro

Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen in vertebrates. Due to this, it is also the most abundant protein type found in all vertebrates. Type I forms large, eosinophilic fibers known as collagen fibers, which make up most of the rope-like dense connective tissue in the body.[1]

Collagen I itself is created by the combination of both a proalpha1 and a proalpha2 chain created by the COL1alpha1 and COL1alpha2 genes respectively. The Col I gene itself takes up a triple-helical conformation due to its Glycine-X-Y structure, x and y being any type of amino acid. Collagen can also be found in two different isoforms, either as a homotrimer or a heterotrimer, both of which can be found during different periods of development. Heterotrimers, in particular, play an important role in wound healing,[2] and are the dominant isoform found in the body.[2]

Type I collagen can be found in a myriad of different places in the body, mainly forming the matrix of connective tissues. It is present in scar tissue as well as tendons, ligaments, the endomysium of myofibrils, the organic part of bone, the dermis, the dentin, and organ capsules.

  1. ^ "Collagen: What It Is, Types, Function & Benefits". Cleveland Clinic. Retrieved 2023-10-25.
  2. ^ a b Elena Makareeva (2014). "Collagen Structure, Folding and Function". Osteogenesis Imperfecta a Translational Approach to Brittle Bone Disease: 71–84. doi:10.1016/B978-0-12-397165-4.00007-1. ISBN 9780123971654.