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Domain

The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity).

Function

Type I collagen is a member of group I collagen (fibrillar forming collagen).

Involvement in disease

Caffey disease

CAFYD

An autosomal dominant disorder characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age.

None

The disease is caused by variants affecting the gene represented in this entry.

Ehlers-Danlos syndrome, classic type, 1

EDSCL1

A form of Ehlers-Danlos syndrome, a group of connective tissue disorders characterized by skin hyperextensibility, articular hypermobility, and tissue fragility. The main features of classic Ehlers-Danlos syndrome are joint hypermobility and dislocation, and fragile, bruisable skin. EDSCL1 inheritance is autosomal dominant.

None

The disease may be caused by variants affecting the gene represented in this entry.

Ehlers-Danlos syndrome, arthrochalasia type, 1

EDSARTH1

A form of Ehlers-Danlos syndrome, a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDSARTH1 is an autosomal dominant form characterized by frequent congenital hip dislocation and extreme joint laxity with recurrent joint subluxations and minimal skin involvement.

None

The disease is caused by variants affecting the gene represented in this entry.

Osteogenesis imperfecta 1

OI1

An autosomal dominant form of osteogenesis imperfecta, a disorder of bone formation characterized by bone low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI1 is a non-deforming form with normal height or mild short stature, and no dentinogenesis imperfecta.

None

The disease is caused by variants affecting the gene represented in this entry.

Osteogenesis imperfecta 2

OI2

An autosomal dominant form of osteogenesis imperfecta, a disorder of bone formation characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI2 is characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency.

None

The disease is caused by variants affecting the gene represented in this entry.

Osteogenesis imperfecta 3

OI3

An autosomal dominant form of osteogenesis imperfecta, a disorder of bone formation characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI3 is characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera and dentinogenesis imperfecta.

None

The disease is caused by variants affecting the gene represented in this entry.

Osteogenesis imperfecta 4

OI4

An autosomal dominant form of osteogenesis imperfecta, a disorder of bone formation characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI4 is characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta.

None

The disease is caused by variants affecting the gene represented in this entry.

Combined osteogenesis imperfecta and Ehlers-Danlos syndrome 1

OIEDS1

An autosomal dominant connective tissue disorder characterized by osteopenia, bone fragility, long bone fractures, blue sclerae, joint hyperextensibility, soft and hyperextensible skin, abnormal wound healing, easy bruising, and vascular fragility.

None

The disease is caused by variants affecting the gene represented in this entry.

Osteoporosis

OSTEOP

A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs.

None

Disease susceptibility is associated with variants affecting the gene represented in this entry.

A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.

Post-translational modifications

Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.

Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.

O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.

Sequence similarities

Belongs to the fibrillar collagen family.

Tissue specificity

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

Cellular localization

  • Secreted
  • Extracellular space
  • Extracellular matrix

Alternative names

Collagen alpha-1(I) chain, Alpha-1 type I collagen, COL1A1

Target type

Proteins

Primary research area

Immuno-oncology

Molecular weight

138941Da

We found 43 products in 4 categories

Assay Kits

Target

Reactive species

Proteins & Peptides

Cell Lines & Lysates

Target

Cell type

Species or organism

Search our catalogue for 'COL1A1' (43)

Products

ab138492

Anti-Collagen I antibody [EPR7785]

Lab Essentials
Recombinant
RabMAb
KO Validated

ab316222

Anti-Collagen I antibody [RM1131]

Lab Essentials
Recombinant
RabMAb
20ul selling size

ab260043

Anti-Collagen I antibody [EPR22894-89]

Lab Essentials
Recombinant
RabMAb

ab255809

Anti-Collagen I antibody [EPR22209-75]

Lab Essentials
Recombinant
RabMAb

ab317789

Anti-Collagen I antibody [EPR7785] – Mouse IgG1 (Chimeric)

Lab Essentials
Recombinant
20ul selling size

ab215969

Anti-Collagen I antibody [EPR7785] - BSA and Azide free

Recombinant
RabMAb
KO Validated

ab210966

Human Pro-Collagen I alpha 1 ELISA Kit

Recombinant
SimpleStep

ab229389

Human Pro-Collagen I alpha 1 ELISA Kit, Fluorescent

Recombinant
CatchPoint SimpleStep ELISA

ab254113

Anti-Collagen I antibody

Lab Essentials

ab233080

Anti-Collagen I antibody

Lab Essentials