| Predicate | Object |
|---|---|
| rdf:type | |
| biopax3:comment |
FUNCTION: Collagen type III occurs in most soft connective tissues along with type I collagen. SUBUNIT: 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. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P02461-1; Sequence=Displayed; Name=2; IsoId=P02461-2; Sequence=VSP_022502; Note=No experimental confirmation available; PTM: Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group. DISEASE: Defects in COL3A1 are a cause of Ehlers-Danlos syndrome type 3 (EDS3) [MIM:130020]; also known as benign hypermobility syndrome. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS3 is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity. DISEASE: Defects in COL3A1 are the cause of Ehlers-Danlos syndrome type 4 (EDS4) [MIM:130050]. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS4 is the most severe form of the disease. It is 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. DISEASE: Defects in COL3A1 are a cause of susceptibility to aortic aneurysm abdominal (AAA) [MIM:100070]. AAA is a common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells. SIMILARITY: Belongs to the fibrillar collagen family. SIMILARITY: Contains 1 fibrillar collagen NC1 domain. SIMILARITY: Contains 1 VWFC domain. WEB RESOURCE: Name=COL3A1; Note=Collagen type III alpha-1 chain mutations; URL="http://www.le.ac.uk/genetics/collagen/col3a1.html"; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/COL3A1"; WEB RESOURCE: Name=Wikipedia; Note=Type-III collagen entry; URL="http://en.wikipedia.org/wiki/Type-III_collagen"; GENE SYNONYMS:COL3A1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
SEQUENCE 1466 AA; 138564 MW; B904B4E05E17D339 CRC64;
|
| biopax3:xref |
urn:biopax:RelationshipXref:HGNC_HGNC:2201,
urn:biopax:RelationshipXref:NCBI GENE_1281,
urn:biopax:RelationshipXref:REFSEQ_NP_000081,
urn:biopax:UnificationXref:UNIPROT_D3DPH4,
urn:biopax:UnificationXref:UNIPROT_P02461,
urn:biopax:UnificationXref:UNIPROT_P78429,
urn:biopax:UnificationXref:UNIPROT_Q15112,
urn:biopax:UnificationXref:UNIPROT_Q16403,
urn:biopax:UnificationXref:UNIPROT_Q53S91,
urn:biopax:UnificationXref:UNIPROT_Q541P8,
urn:biopax:UnificationXref:UNIPROT_Q6LDB3,
urn:biopax:UnificationXref:UNIPROT_Q6LDJ2,
urn:biopax:UnificationXref:UNIPROT_Q6LDJ3,
urn:biopax:UnificationXref:UNIPROT_Q7KZ56,
urn:biopax:UnificationXref:UNIPROT_Q8N6U4,
urn:biopax:UnificationXref:UNIPROT_Q9UC88,
urn:biopax:UnificationXref:UNIPROT_Q9UC89,
urn:biopax:UnificationXref:UNIPROT_Q9UC90,
urn:biopax:UnificationXref:UNIPROT_Q9UC91
|
| biopax3:displayName |
CO3A1_HUMAN
|
| biopax3:name |
COL3A1
|
| biopax3:entityFeature |
urn:biopax:ModificationFeature:CO3A1_HUMAN_1,
urn:biopax:ModificationFeature:CO3A1_HUMAN_2,
urn:biopax:ModificationFeature:CO3A1_HUMAN_3,
urn:biopax:ModificationFeature:CO3A1_HUMAN_4,
urn:biopax:ModificationFeature:CO3A1_HUMAN_5,
urn:biopax:ModificationFeature:CO3A1_HUMAN_6,
urn:biopax:ModificationFeature:CO3A1_HUMAN_7,
urn:biopax:ModificationFeature:CO3A1_HUMAN_8
|
| biopax3:organism | |
| biopax3:sequence |
MMSFVQKGSWLLLALLHPTIILAQQEAVEGGCSHLGQSYADRDVWKPEPCQICVCDSGSVLCDDIICDDQELDCPNPEIPFGECCAVCPQPPTAPTRPPNGQGPQGPKGDPGPPGIPGRNGDPGIPGQPGSPGSPGPPGICESCPTGPQNYSPQYDSYDVKSGVAVGGLAGYPGPAGPPGPPGPPGTSGHPGSPGSPGYQGPPGEPGQAGPSGPPGPPGAIGPSGPAGKDGESGRPGRPGERGLPGPPGIKGPAGIPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGENGAPGPMGPRGAPGERGRPGLPGAAGARGNDGARGSDGQPGPPGPPGTAGFPGSPGAKGEVGPAGSPGSNGAPGQRGEPGPQGHAGAQGPPGPPGINGSPGGKGEMGPAGIPGAPGLMGARGPPGPAGANGAPGLRGGAGEPGKNGAKGEPGPRGERGEAGIPGVPGAKGEDGKDGSPGEPGANGLPGAAGERGAPGFRGPAGPNGIPGEKGPAGERGAPGPAGPRGAAGEPGRDGVPGGPGMRGMPGSPGGPGSDGKPGPPGSQGESGRPGPPGPSGPRGQPGVMGFPGPKGNDGAPGKNGERGGPGGPGPQGPPGKNGETGPQGPPGPTGPGGDKGDTGPPGPQGLQGLPGTGGPPGENGKPGEPGPKGDAGAPGAPGGKGDAGAPGERGPPGLAGAPGLRGGAGPPGPEGGKGAAGPPGPPGAAGTPGLQGMPGERGGLGSPGPKGDKGEPGGPGADGVPGKDGPRGPTGPIGPPGPAGQPGDKGEGGAPGLPGIAGPRGSPGERGETGPPGPAGFPGAPGQNGEPGGKGERGAPGEKGEGGPPGVAGPPGGSGPAGPPGPQGVKGERGSPGGPGAAGFPGARGLPGPPGSNGNPGPPGPSGSPGKDGPPGPAGNTGAPGSPGVSGPKGDAGQPGEKGSPGAQGPPGAPGPLGIAGITGARGLAGPPGMPGPRGSPGPQGVKGESGKPGANGLSGERGPPGPQGLPGLAGTAGEPGRDGNPGSDGLPGRDGSPGGKGDRGENGSPGAPGAPGHPGPPGPVGPAGKSGDRGESGPAGPAGAPGPAGSRGAPGPQGPRGDKGETGERGAAGIKGHRGFPGNPGAPGSPGPAGQQGAIGSPGPAGPRGPVGPSGPPGKDGTSGHPGPIGPPGPRGNRGERGSEGSPGHPGQPGPPGPPGAPGPCCGGVGAAAIAGIGGEKAGGFAPYYGDEPMDFKINTDEIMTSLKSVNGQIESLISPDGSRKNPARNCRDLKFCHPELKSGEYWVDPNQGCKLDAIKVFCNMETGETCISANPLNVPRKHWWTDSSAEKKHVWFGESMDGGFQFSYGNPELPEDVLDVHLAFLRLLSSRASQNITYHCKNSIAYMDQASGNVKKALKLMGSNEGEFKAEGNSKFTYTVLEDGCTKHTGEWSKTVFEYRTRKAVRLPIVDIAPYDIGGPDQEFGVDVGPVCFL
|
| biopax3:standardName |
Collagen alpha-1(III) chain
|