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Protein

Collagen alpha-1(III) chain

Gene

COL3A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1280Calcium1
Metal bindingi1282Calcium1
Metal bindingi1283Calcium; via carbonyl oxygen1
Metal bindingi1285Calcium; via carbonyl oxygen1
Metal bindingi1288Calcium1

GO - Molecular functioni

  • extracellular matrix structural constituent Source: UniProtKB
  • integrin binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • platelet-derived growth factor binding Source: MGI
  • protease binding Source: CAFA
  • SMAD binding Source: Ensembl

GO - Biological processi

  • aging Source: Ensembl
  • aorta smooth muscle tissue morphogenesis Source: Ensembl
  • cell-matrix adhesion Source: UniProtKB
  • cellular response to amino acid stimulus Source: Ensembl
  • cerebral cortex development Source: UniProtKB
  • collagen fibril organization Source: UniProtKB
  • digestive tract development Source: Ensembl
  • extracellular matrix organization Source: Reactome
  • heart development Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB
  • negative regulation of immune response Source: UniProtKB
  • negative regulation of neuron migration Source: UniProtKB
  • peptide cross-linking Source: UniProtKB
  • platelet activation Source: UniProtKB
  • positive regulation of Rho protein signal transduction Source: UniProtKB
  • regulation of immune response Source: Reactome
  • response to cytokine Source: UniProtKB
  • response to mechanical stimulus Source: Ensembl
  • response to radiation Source: UniProtKB
  • skeletal system development Source: Ensembl
  • skin development Source: UniProtKB
  • supramolecular fiber organization Source: UniProtKB
  • transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • wound healing Source: UniProtKB

Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474244 Extracellular matrix organization
R-HSA-1650814 Collagen biosynthesis and modifying enzymes
R-HSA-186797 Signaling by PDGF
R-HSA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-216083 Integrin cell surface interactions
R-HSA-3000170 Syndecan interactions
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-3000480 Scavenging by Class A Receptors
R-HSA-419037 NCAM1 interactions
R-HSA-8874081 MET activates PTK2 signaling
R-HSA-8948216 Collagen chain trimerization
SIGNORiP02461

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(III) chain
Gene namesi
Name:COL3A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000168542.12
HGNCiHGNC:2201 COL3A1
MIMi120180 gene
neXtProtiNX_P02461

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Ehlers-Danlos syndrome 3 (EDS3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. It is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity.
See also OMIM:130020
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001783804G → S in EDS3. 1 PublicationCorresponds to variant dbSNP:rs121912920EnsemblClinVar.1
Ehlers-Danlos syndrome 4 (EDS4)29 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionThe most severe form of Ehlers-Danlos syndrome, a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. Characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas.
See also OMIM:130050
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001768183G → C in EDS4. 2 PublicationsCorresponds to variant dbSNP:rs121912926EnsemblClinVar.1
Natural variantiVAR_011095183G → D in EDS4. Corresponds to variant dbSNP:rs587779420EnsemblClinVar.1
Natural variantiVAR_011096183G → S in EDS4. Corresponds to variant dbSNP:rs121912926EnsemblClinVar.1
Natural variantiVAR_011097192G → V in EDS4. Corresponds to variant dbSNP:rs587779710EnsemblClinVar.1
Natural variantiVAR_001769201G → R in EDS4. 2 PublicationsCorresponds to variant dbSNP:rs587779436EnsemblClinVar.1
Natural variantiVAR_011098204G → D in EDS4. 1 PublicationCorresponds to variant dbSNP:rs587779626EnsemblClinVar.1
Natural variantiVAR_011099204G → S in EDS4. Corresponds to variant dbSNP:rs587779711EnsemblClinVar.1
Natural variantiVAR_011100210G → D in EDS4. 1 Publication1
Natural variantiVAR_011101219G → C in EDS4. Corresponds to variant dbSNP:rs587779624EnsemblClinVar.1
Natural variantiVAR_011102225G → V in EDS4. Corresponds to variant dbSNP:rs587779533EnsemblClinVar.1
Natural variantiVAR_001770228G → E in EDS4. 2 PublicationsCorresponds to variant dbSNP:rs587779555EnsemblClinVar.1
Natural variantiVAR_011103240G → R in EDS4. Corresponds to variant dbSNP:rs587779468EnsemblClinVar.1
Natural variantiVAR_011104243G → V in EDS4. Corresponds to variant dbSNP:rs587779629EnsemblClinVar.1
Natural variantiVAR_011105249G → D in EDS4. Corresponds to variant dbSNP:rs121912927EnsemblClinVar.1
Natural variantiVAR_011106249G → V in EDS4. Corresponds to variant dbSNP:rs121912927EnsemblClinVar.1
Natural variantiVAR_011107252G → D in EDS4. Corresponds to variant dbSNP:rs587779464EnsemblClinVar.1
Natural variantiVAR_011108252G → R in EDS4. Corresponds to variant dbSNP:rs587779705EnsemblClinVar.1
Natural variantiVAR_011109252G → V in EDS4. Corresponds to variant dbSNP:rs587779464EnsemblClinVar.1
Natural variantiVAR_011110255G → V in EDS4. Corresponds to variant dbSNP:rs587779605EnsemblClinVar.1
Natural variantiVAR_011111264G → R in EDS4. 1 Publication1
Natural variantiVAR_011112267G → V in EDS4. Corresponds to variant dbSNP:rs587779427EnsemblClinVar.1
Natural variantiVAR_037007297G → R in EDS4. 1 Publication1
Natural variantiVAR_001771303G → R in EDS4. 1 PublicationCorresponds to variant dbSNP:rs121912919EnsemblClinVar.1
Natural variantiVAR_011113321G → V in EDS4. Corresponds to variant dbSNP:rs587779588EnsemblClinVar.1
Natural variantiVAR_011114327G → D in EDS4. 1 Publication1
Natural variantiVAR_011115345G → R in EDS4. Corresponds to variant dbSNP:rs587779419EnsemblClinVar.1
Natural variantiVAR_011116417G → R in EDS4. Corresponds to variant dbSNP:rs587779637EnsemblClinVar.1
Natural variantiVAR_011117444G → R in EDS4. Corresponds to variant dbSNP:rs587779489EnsemblClinVar.1
Natural variantiVAR_011118489G → E in EDS4. Corresponds to variant dbSNP:rs587779476EnsemblClinVar.1
Natural variantiVAR_011119501G → R in EDS4. Corresponds to variant dbSNP:rs587779523EnsemblClinVar.1
Natural variantiVAR_011120519G → V in EDS4. 1
Natural variantiVAR_001772540G → R in EDS4. 2 PublicationsCorresponds to variant dbSNP:rs587779584EnsemblClinVar.1
Natural variantiVAR_011121549G → E in EDS4. Corresponds to variant dbSNP:rs587779679EnsemblClinVar.1
Natural variantiVAR_011122552G → E in EDS4. Corresponds to variant dbSNP:rs121912928EnsemblClinVar.1
Natural variantiVAR_001773567G → E in EDS4. 1 Publication1
Natural variantiVAR_001774582G → S in EDS4. 1 PublicationCorresponds to variant dbSNP:rs121912923EnsemblClinVar.1
Natural variantiVAR_011123588G → D in EDS4. Corresponds to variant dbSNP:rs587779691EnsemblClinVar.1
Natural variantiVAR_011124636G → R in EDS4. Corresponds to variant dbSNP:rs587779522EnsemblClinVar.1
Natural variantiVAR_011125657G → E in EDS4. Corresponds to variant dbSNP:rs587779699EnsemblClinVar.1
Natural variantiVAR_011126660G → D in EDS4. Corresponds to variant dbSNP:rs587779493EnsemblClinVar.1
Natural variantiVAR_001777666G → D in EDS4. 1 PublicationCorresponds to variant dbSNP:rs121912921EnsemblClinVar.1
Natural variantiVAR_011128699G → R in EDS4. Corresponds to variant dbSNP:rs587779668EnsemblClinVar.1
Natural variantiVAR_001779726G → R in EDS4. 2 PublicationsCorresponds to variant dbSNP:rs587779638EnsemblClinVar.1
Natural variantiVAR_011129738G → S in EDS4. Corresponds to variant dbSNP:rs121912925EnsemblClinVar.1
Natural variantiVAR_011130738G → V in EDS4. Corresponds to variant dbSNP:rs587779615EnsemblClinVar.1
Natural variantiVAR_011131744G → V in EDS4. Corresponds to variant dbSNP:rs587779697EnsemblClinVar.1
Natural variantiVAR_001780756G → E in EDS4. 1 Publication1
Natural variantiVAR_001781762G → C in EDS4. 1 Publication1
Natural variantiVAR_001782786G → R in EDS4. 1 PublicationCorresponds to variant dbSNP:rs113485686EnsemblClinVar.1
Natural variantiVAR_001784828G → R in EDS4. 1 Publication1
Natural variantiVAR_011132828G → W in EDS4. Corresponds to variant dbSNP:rs587779486EnsemblClinVar.1
Natural variantiVAR_037008830 – 838Missing in EDS4. 1 Publication9
Natural variantiVAR_011133852G → C in EDS4. Corresponds to variant dbSNP:rs587779690EnsemblClinVar.1
Natural variantiVAR_011134879G → V in EDS4. Corresponds to variant dbSNP:rs587779645EnsemblClinVar.1
Natural variantiVAR_011135882G → D in EDS4. Corresponds to variant dbSNP:rs587779622EnsemblClinVar.1
Natural variantiVAR_011136900G → D in EDS4. Corresponds to variant dbSNP:rs587779599EnsemblClinVar.1
Natural variantiVAR_011137903G → E in EDS4. Corresponds to variant dbSNP:rs587779505EnsemblClinVar.1
Natural variantiVAR_001785909G → D in EDS4. 1 Publication1
Natural variantiVAR_011138909G → V in EDS4. Corresponds to variant dbSNP:rs587779483EnsemblClinVar.1
Natural variantiVAR_011139918G → E in EDS4. Corresponds to variant dbSNP:rs587779662EnsemblClinVar.1
Natural variantiVAR_011140924G → C in EDS4. Corresponds to variant dbSNP:rs587779471EnsemblClinVar.1
Natural variantiVAR_001786936G → R in EDS4. 2 PublicationsCorresponds to variant dbSNP:rs587779566EnsemblClinVar.1
Natural variantiVAR_001787936G → S in EDS4. 1
Natural variantiVAR_001788939G → D in EDS4. 1 PublicationCorresponds to variant dbSNP:rs112978464Ensembl.1
Natural variantiVAR_011141942G → E in EDS4. Corresponds to variant dbSNP:rs587779517EnsemblClinVar.1
Natural variantiVAR_001789957G → S in EDS4; severe variant. 1 PublicationCorresponds to variant dbSNP:rs121912913Ensembl.1
Natural variantiVAR_001790960G → V in EDS4; severe variant. 1 PublicationCorresponds to variant dbSNP:rs121912922EnsemblClinVar.1
Natural variantiVAR_011142966G → V in EDS4. Corresponds to variant dbSNP:rs587779571EnsemblClinVar.1
Natural variantiVAR_011143972G → A in EDS4. Corresponds to variant dbSNP:rs587779559EnsemblClinVar.1
Natural variantiVAR_011144984G → T in EDS4; requires 2 nucleotide substitutions. 1
Natural variantiVAR_001791996G → E in EDS4. 1 PublicationCorresponds to variant dbSNP:rs587779576EnsemblClinVar.1
Natural variantiVAR_011145999G → R in EDS4. Corresponds to variant dbSNP:rs587779548EnsemblClinVar.1
Natural variantiVAR_0111461011G → E in EDS4. Corresponds to variant dbSNP:rs587779552EnsemblClinVar.1
Natural variantiVAR_0017921014G → E in EDS4. 1 PublicationCorresponds to variant dbSNP:rs121912916EnsemblClinVar.1
Natural variantiVAR_0111471032G → V in EDS4. Corresponds to variant dbSNP:rs587779428EnsemblClinVar.1
Natural variantiVAR_0111481035G → C in EDS4. Corresponds to variant dbSNP:rs587779704EnsemblClinVar.1
Natural variantiVAR_0111491044G → D in EDS4. 1 Publication1
Natural variantiVAR_0017931050G → D in EDS4; mild variant. 1 PublicationCorresponds to variant dbSNP:rs121912914EnsemblClinVar.1
Natural variantiVAR_0111501050G → V in EDS4. 1 PublicationCorresponds to variant dbSNP:rs121912914EnsemblClinVar.1
Natural variantiVAR_0017941071G → V in EDS4. 1 PublicationCorresponds to variant dbSNP:rs587779709EnsemblClinVar.1
Natural variantiVAR_0017951077G → V in EDS4. 1 PublicationCorresponds to variant dbSNP:rs121912915EnsemblClinVar.1
Natural variantiVAR_0111511089G → D in EDS4. Corresponds to variant dbSNP:rs587779672EnsemblClinVar.1
Natural variantiVAR_0111521098G → D in EDS4. 1 Publication1
Natural variantiVAR_0111531098G → V in EDS4. Corresponds to variant dbSNP:rs587779614EnsemblClinVar.1
Natural variantiVAR_0017961101G → E in EDS4. 1 PublicationCorresponds to variant dbSNP:rs121912924EnsemblClinVar.1
Natural variantiVAR_0017971104G → A in EDS4. 1 Publication1
Natural variantiVAR_0111541161G → V in EDS4. Corresponds to variant dbSNP:rs587779473EnsemblClinVar.1
Natural variantiVAR_0111551164G → E in EDS4. Corresponds to variant dbSNP:rs587779431EnsemblClinVar.1
Natural variantiVAR_0111561164G → R in EDS4. Corresponds to variant dbSNP:rs587779553EnsemblClinVar.1
Natural variantiVAR_0017991167G → V in EDS4. 1 PublicationCorresponds to variant dbSNP:rs587779578EnsemblClinVar.1
Natural variantiVAR_0018001170G → D in EDS4. 2 PublicationsCorresponds to variant dbSNP:rs587779465EnsemblClinVar.1
Natural variantiVAR_0111571170G → V in EDS4. Corresponds to variant dbSNP:rs587779465EnsemblClinVar.1
Natural variantiVAR_0018011173G → E in EDS4. 3 PublicationsCorresponds to variant dbSNP:rs121912918EnsemblClinVar.1
Natural variantiVAR_0111581173G → R in EDS4; Gottron type acrogeria. 1 PublicationCorresponds to variant dbSNP:rs587779521EnsemblClinVar.1
Natural variantiVAR_0018021176G → V in EDS4; severe. 1 Publication1
Natural variantiVAR_0111591179G → R in EDS4. Corresponds to variant dbSNP:rs587779574EnsemblClinVar.1
Natural variantiVAR_0018031182G → E in EDS4. 1 PublicationCorresponds to variant dbSNP:rs111505097EnsemblClinVar.1
Natural variantiVAR_0018041185G → D in EDS4; severe variant. 1 PublicationCorresponds to variant dbSNP:rs121912917EnsemblClinVar.1
Natural variantiVAR_0018051185G → V in EDS4. 1 PublicationCorresponds to variant dbSNP:rs121912917EnsemblClinVar.1
Natural variantiVAR_0018061188G → E in EDS4; severe variant. 2 PublicationsCorresponds to variant dbSNP:rs112456072EnsemblClinVar.1
Natural variantiVAR_0018071188G → R in EDS4. 1 PublicationCorresponds to variant dbSNP:rs587779504EnsemblClinVar.1

Keywords - Diseasei

Aortic aneurysm, Disease mutation, Ehlers-Danlos syndrome

Organism-specific databases

DisGeNETi1281
GeneReviewsiCOL3A1
MalaCardsiCOL3A1
MIMi130020 phenotype
130050 phenotype
OpenTargetsiENSG00000168542
Orphaneti2500 Acrogeria
286 Ehlers-Danlos syndrome, vascular type
86 Familial abdominal aortic aneurysm
231160 Familial cerebral saccular aneurysm
PharmGKBiPA26716

Chemistry databases

ChEMBLiCHEMBL2364188
DrugBankiDB00048 Collagenase clostridium histolyticum

Polymorphism and mutation databases

BioMutaiCOL3A1
DMDMi124056490

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Add BLAST23
PropeptideiPRO_000000574024 – 153N-terminal propeptideAdd BLAST130
ChainiPRO_0000005741154 – 1221Collagen alpha-1(III) chainAdd BLAST1068
PropeptideiPRO_00000057421222 – 1466C-terminal propeptideAdd BLAST245

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1734-hydroxyproline1 Publication1
Modified residuei1794-hydroxyproline1 Publication1
Modified residuei1824-hydroxyproline1 Publication1
Modified residuei1854-hydroxyproline1 Publication1
Modified residuei1914-hydroxyproline1 Publication1
Modified residuei1944-hydroxyproline1 Publication1
Modified residuei1974-hydroxyproline1 Publication1
Modified residuei2034-hydroxyproline1 Publication1
Modified residuei2064-hydroxyproline1 Publication1
Modified residuei2154-hydroxyproline1 Publication1
Modified residuei2184-hydroxyproline1 Publication1
Modified residuei2364-hydroxyproline1 Publication1
Modified residuei2394-hydroxyproline1 Publication1
Modified residuei2454-hydroxyproline1 Publication1
Modified residuei2484-hydroxyproline1 Publication1
Modified residuei2574-hydroxyproline1 Publication1
Modified residuei2604-hydroxyproline1 Publication1
Modified residuei2635-hydroxylysine; alternate1 Publication1
Glycosylationi263O-linked (Gal...) hydroxylysine; alternate1
Modified residuei2814-hydroxyproline1 Publication1
Modified residuei2845-hydroxylysine1 Publication1
Modified residuei2904-hydroxyproline1 Publication1
Modified residuei2964-hydroxyproline1 Publication1
Modified residuei3054-hydroxyproline1 Publication1
Modified residuei3114-hydroxyproline1 Publication1
Modified residuei3144-hydroxyproline1 Publication1
Modified residuei3324-hydroxyproline1 Publication1
Modified residuei3354-hydroxyproline1 Publication1
Modified residuei3384-hydroxyproline1 Publication1
Modified residuei3444-hydroxyproline1 Publication1
Modified residuei3474-hydroxyproline1 Publication1
Modified residuei3594-hydroxyproline1 Publication1
Modified residuei3654-hydroxyproline1 Publication1
Modified residuei3714-hydroxyproline1 Publication1
Modified residuei3834-hydroxyproline1 Publication1
Modified residuei3864-hydroxyproline1 Publication1
Modified residuei3924-hydroxyproline1 Publication1
Modified residuei4044-hydroxyproline1 Publication1
Modified residuei4074-hydroxyproline1 Publication1
Modified residuei4164-hydroxyproline1 Publication1
Modified residuei4254-hydroxyproline1 Publication1
Modified residuei4344-hydroxyproline1 Publication1
Modified residuei4434-hydroxyproline1 Publication1
Modified residuei4554-hydroxyproline1 Publication1
Modified residuei4584-hydroxyproline1 Publication1
Modified residuei4704-hydroxyproline1 Publication1
Modified residuei4734-hydroxyproline1 Publication1
Modified residuei4794-hydroxyproline1 Publication1
Modified residuei4884-hydroxyproline1 Publication1
Modified residuei5004-hydroxyproline1 Publication1
Modified residuei5124-hydroxyproline1 Publication1
Modified residuei5244-hydroxyproline1 Publication1
Modified residuei5304-hydroxyproline1 Publication1
Modified residuei5334-hydroxyproline1 Publication1
Modified residuei5394-hydroxyproline1 Publication1
Modified residuei5424-hydroxyproline1 Publication1
Modified residuei5454-hydroxyproline1 Publication1
Modified residuei5514-hydroxyproline1 Publication1
Modified residuei5544-hydroxyproline1 Publication1
Modified residuei5634-hydroxyproline1 Publication1
Modified residuei5664-hydroxyproline1 Publication1
Modified residuei5754-hydroxyproline1 Publication1
Modified residuei5814-hydroxyproline1 Publication1
Modified residuei5904-hydroxyproline1 Publication1
Modified residuei5994-hydroxyproline1 Publication1
Modified residuei6024-hydroxyproline1 Publication1
Modified residuei6084-hydroxyproline1 Publication1
Modified residuei6204-hydroxyproline1 Publication1
Modified residuei6354-hydroxyproline1 Publication1
Modified residuei6444-hydroxyproline1 Publication1
Modified residuei6504-hydroxyproline1 Publication1
Modified residuei6564-hydroxyproline1 Publication1
Modified residuei6594-hydroxyproline1 Publication1
Modified residuei6614-hydroxyproline1 Publication1
Modified residuei6684-hydroxyproline1 Publication1
Modified residuei6714-hydroxyproline1 Publication1
Modified residuei6804-hydroxyproline1 Publication1
Modified residuei6864-hydroxyproline1 Publication1
Modified residuei6924-hydroxyproline1 Publication1
Modified residuei7014-hydroxyproline1 Publication1
Modified residuei7034-hydroxyproline1 Publication1
Modified residuei7134-hydroxyproline1 Publication1
Modified residuei7164-hydroxyproline1 Publication1
Modified residuei7224-hydroxyproline1 Publication1
Modified residuei7284-hydroxyproline1 Publication1
Modified residuei7374-hydroxyproline1 Publication1
Modified residuei7464-hydroxyproline1 Publication1
Modified residuei7494-hydroxyproline1 Publication1
Modified residuei7554-hydroxyproline1 Publication1
Modified residuei7704-hydroxyproline1 Publication1
Modified residuei7764-hydroxyproline1 Publication1
Modified residuei7854-hydroxyproline1 Publication1
Modified residuei7884-hydroxyproline1 Publication1
Modified residuei7974-hydroxyproline1 Publication1
Modified residuei8064-hydroxyproline1 Publication1
Modified residuei8124-hydroxyproline1 Publication1
Modified residuei8154-hydroxyproline1 Publication1
Modified residuei8214-hydroxyproline1 Publication1
Modified residuei8304-hydroxyproline1 Publication1
Modified residuei8394-hydroxyproline1 Publication1
Modified residuei8454-hydroxyproline1 Publication1
Modified residuei8544-hydroxyproline1 Publication1
Modified residuei8605-hydroxylysine1 Publication1
Modified residuei8664-hydroxyproline1 Publication1
Modified residuei8694-hydroxyproline1 Publication1
Modified residuei8754-hydroxyproline1 Publication1
Modified residuei8814-hydroxyproline1 Publication1
Modified residuei8844-hydroxyproline1 Publication1
Modified residuei8904-hydroxyproline1 Publication1
Modified residuei8924-hydroxyproline1 Publication1
Modified residuei8994-hydroxyproline1 Publication1
Modified residuei9054-hydroxyproline1 Publication1
Modified residuei9144-hydroxyproline1 Publication1
Modified residuei9174-hydroxyproline1 Publication1
Modified residuei9294-hydroxyproline1 Publication1
Modified residuei9354-hydroxyproline1 Publication1
Modified residuei9414-hydroxyproline1 Publication1
Modified residuei9444-hydroxyproline1 Publication1
Modified residuei9624-hydroxyproline1 Publication1
Modified residuei9654-hydroxyproline1 Publication1
Modified residuei9714-hydroxyproline1 Publication1
Modified residuei9775-hydroxylysine1 Publication1
Modified residuei9834-hydroxyproline1 Publication1
Modified residuei9954-hydroxyproline1 Publication1
Modified residuei10014-hydroxyproline1 Publication1
Modified residuei10104-hydroxyproline1 Publication1
Modified residuei10164-hydroxyproline1 Publication1
Modified residuei10224-hydroxyproline1 Publication1
Modified residuei10284-hydroxyproline1 Publication1
Modified residuei10404-hydroxyproline1 Publication1
Modified residuei10434-hydroxyproline1 Publication1
Modified residuei10464-hydroxyproline1 Publication1
Modified residuei10494-hydroxyproline1 Publication1
Modified residuei10524-hydroxyproline1 Publication1
Modified residuei10764-hydroxyproline1 Publication1
Modified residuei10854-hydroxyproline1 Publication1
Modified residuei11065-hydroxylysine1 Publication1
Modified residuei11124-hydroxyproline1 Publication1
Modified residuei11154-hydroxyproline1 Publication1
Modified residuei11184-hydroxyproline1 Publication1
Modified residuei11214-hydroxyproline1 Publication1
Modified residuei11334-hydroxyproline1 Publication1
Modified residuei11484-hydroxyproline1 Publication1
Modified residuei11574-hydroxyproline1 Publication1
Modified residuei11634-hydroxyproline1 Publication1
Modified residuei11784-hydroxyproline1 Publication1
Modified residuei11814-hydroxyproline1 Publication1
Modified residuei11844-hydroxyproline1 Publication1
Modified residuei11874-hydroxyproline1 Publication1
Modified residuei11904-hydroxyproline1 Publication1
Modified residuei11934-hydroxyproline1 Publication1
Disulfide bondi1196InterchainPROSITE-ProRule annotation1 Publication
Disulfide bondi1197InterchainPROSITE-ProRule annotation1 Publication
Disulfide bondi1262 ↔ 1294PROSITE-ProRule annotation1 Publication
Disulfide bondi1268Interchain (with C-1285)PROSITE-ProRule annotation1 Publication
Disulfide bondi1285Interchain (with C-1268)PROSITE-ProRule annotation1 Publication
Disulfide bondi1302 ↔ 1464PROSITE-ProRule annotation1 Publication
Disulfide bondi1372 ↔ 1417PROSITE-ProRule annotation1 Publication

Post-translational modificationi

Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.2 Publications
O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

EPDiP02461
PaxDbiP02461
PeptideAtlasiP02461
PRIDEiP02461

PTM databases

iPTMnetiP02461
PhosphoSitePlusiP02461

Expressioni

Gene expression databases

BgeeiENSG00000168542
ExpressionAtlasiP02461 baseline and differential
GenevisibleiP02461 HS

Organism-specific databases

HPAiCAB016766
CAB059993
HPA007583

Interactioni

Subunit structurei

Trimers of identical alpha 1(III) chains. The chains are linked to each other by interchain disulfide bonds. Trimers are also cross-linked via hydroxylysines.

Binary interactionsi

Show more details

GO - Molecular functioni

  • integrin binding Source: UniProtKB
  • platelet-derived growth factor binding Source: MGI
  • protease binding Source: CAFA
  • SMAD binding Source: Ensembl

Protein-protein interaction databases

BioGridi107678, 11 interactors
DIPiDIP-57177N
IntActiP02461, 23 interactors
MINTiP02461
STRINGi9606.ENSP00000304408

Structurei

Secondary structure

11466
Legend: HelixTurnBeta strandPDB Structure known for this area
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Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1236 – 1249Combined sources14
Beta strandi1253 – 1257Combined sources5
Helixi1262 – 1268Combined sources7
Beta strandi1274 – 1279Combined sources6
Helixi1286 – 1288Combined sources3
Beta strandi1290 – 1295Combined sources6
Turni1296 – 1299Combined sources4
Beta strandi1300 – 1303Combined sources4
Beta strandi1305 – 1307Combined sources3
Beta strandi1309 – 1313Combined sources5
Beta strandi1320 – 1322Combined sources3
Helixi1328 – 1331Combined sources4
Beta strandi1339 – 1341Combined sources3
Beta strandi1343 – 1345Combined sources3
Helixi1347 – 1360Combined sources14
Beta strandi1364 – 1374Combined sources11
Turni1381 – 1384Combined sources4
Beta strandi1391 – 1393Combined sources3
Beta strandi1395 – 1397Combined sources3
Beta strandi1399 – 1404Combined sources6
Helixi1406 – 1408Combined sources3
Beta strandi1411 – 1415Combined sources5
Beta strandi1422 – 1434Combined sources13
Helixi1436 – 1438Combined sources3
Beta strandi1443 – 1445Combined sources3
Beta strandi1455 – 1465Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V53X-ray3.20B/C/D564-584[»]
3DMWX-ray2.30A/B/C1158-1199[»]
4AE2X-ray1.68A/B/C1222-1466[»]
4AEJX-ray2.21A/B/C1222-1466[»]
4AK3X-ray3.50A1222-1466[»]
4GYXX-ray1.49A/B/C1158-1200[»]
ProteinModelPortaliP02461
SMRiP02461
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02461

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 89VWFCPROSITE-ProRule annotationAdd BLAST60
Domaini1232 – 1466Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST235

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni149 – 167Nonhelical region (N-terminal)Add BLAST19
Regioni168 – 1196Triple-helical regionAdd BLAST1029
Regioni1197 – 1205Nonhelical region (C-terminal)9

Domaini

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.

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00900000140789
HOVERGENiHBG004933
InParanoidiP02461
KOiK19720
OMAiCRDLKFC
OrthoDBiEOG091G03LV
PhylomeDBiP02461
TreeFamiTF344135

Family and domain databases

InterProiView protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom
PfamiView protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 8 hits
PF00093 VWC, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002078 Fib_collagen_C, 1 hit
SMARTiView protein in SMART
SM00038 COLFI, 1 hit