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Details on Person UniProt:P02462 COL4A1
| Class:Id | ReferenceGeneProduct:51132 |
|---|---|
| _chainChangeLog | signal peptide:1-27 added on Sat February 7 2015;propeptide:28-172 added on Sat February 7 2015;chain:173-1669 added on Sat February 7 2015;chain:1445-1669 added on Sat February 7 2015 |
| _displayName | UniProt:P02462 COL4A1 |
| _timestamp | 2024-11-03 19:50:31 |
| chain | signal peptide:1-27 propeptide:28-172 chain:173-1669 chain:1445-1669 |
| checksum | 3BEBA6DFFB9B8A84 |
| comment | FUNCTION Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.FUNCTION Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation.SUBUNIT There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network. Interacts with EFEMP2 (By similarity).INTERACTION Highly expressed in placenta.DOMAIN Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain. NC1 domain mediates hexamerization of alpha chains of type IV collagen (By similarity).PTM Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated. The modified lysines can be O-glycosylated.PTM Contains 4-hydroxyproline (Probable). Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains (By similarity).PTM Contains 3-hydroxyproline. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.PTM Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding (PubMed:2844531). 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.PTM The trimeric structure of the NC1 domains is stabilized by covalent bonds (sulfilimine cross-links) between Lys and Met residues (PubMed:12011424). These cross-links are important for the mechanical stability of the basement membrane (By similarity). Sulfilimine cross-link is catalyzed by PXDN (By similarity).PTM Proteolytic processing produces the C-terminal NC1 peptide, arresten.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE Disease susceptibility is associated with variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry. Causative mutations affect a binding site for miR-29 microRNA located within the 3'UTR of COL4A1 and lead to an up-regulation of this gene.SIMILARITY Belongs to the type IV collagen family.CAUTION Was shown to inhibit expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation, and to function as a ligand for alpha1/beta1 integrin. However, this study was later retracted. |
| description | recommendedName: fullName evidence="32"Collagen alpha-1(IV) chain component recommendedName: Arresten /component |
| geneName | COL4A1 |
| identifier | P02462 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Alternative splicing Angiogenesis Basement membrane Collagen Direct protein sequencing Disease variant Disulfide bond Extracellular matrix Glycoprotein Hydroxylation Proteomics identification Reference proteome Repeat Secreted Signal |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | COL4A1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8994145] ENSEMBL:ENSG00000187498 COL4A1 [Homo sapiens] |
| secondaryIdentifier | CO4A1_HUMAN A7E2W4 B1AM70 F5H5K0 Q1P9S9 Q5VWF6 Q86X41 Q8NF88 Q9NYC5 |
| sequenceLength | 1669 |
| species | [Species:48887] Homo sapiens |
| (isoformParent) | [ReferenceIsoform:384783] UniProt:P02462-2 COL4A1 [Homo sapiens] [ReferenceIsoform:402284] UniProt:P02462-1 COL4A1 [Homo sapiens] |
| (referenceEntity) | [EntityWithAccessionedSequence:139935] COL4A1(173-1669) [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:215922] COL4A1(173-1669) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:2022431] 3Hyp-COL4A1(28-1669) [endoplasmic reticulum lumen] [Homo sapiens] [EntityWithAccessionedSequence:2022519] 5Hyl-COL4A1(28-1669) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:2023549] GalHyl-COL4A1(28-1669) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:2023671] 3x4Hyp-GlcGalHyl-COL4A1(28-1669) [endoplasmic reticulum lumen] [Homo sapiens] [EntityWithAccessionedSequence:2029195] 3x4Hyp-3Hyp-GalHyl-COL4A1(173-1669) [endoplasmic reticulum lumen] [Homo sapiens] [EntityWithAccessionedSequence:2029211] 3x4Hyp-3Hyp-5Hyl-COL4A1(173-1669) [endoplasmic reticulum lumen] [Homo sapiens] [EntityWithAccessionedSequence:2029235] 3x4Hyp-3Hyp-GlcGalHyl-COL4A1(173-1669) [endoplasmic reticulum lumen] [Homo sapiens] [EntityWithAccessionedSequence:2029276] 3x4Hyp-GalHyl-COL4A1(173-1669) [endoplasmic reticulum lumen] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:2022086] (2S,4R)-4-hydroxyproline at unknown position [ModifiedResidue:2022439] (2S,5R)-5-hydroxylysine at unknown position [ModifiedResidue:2022520] (2S,3S)-3-hydroxyproline at unknown position [ModifiedResidue:2023524] O5-galactosyl-L-hydroxylysine at unknown position [ModifiedResidue:2023605] O5-glucosylgalactosyl-L-hydroxylysine at unknown position [GroupModifiedResidue:2682385] (2S,5R)-5-hydroxylysine (sulfilimine bond) at unknown position [GroupModifiedResidue:2682394] (2S,5R)-5-hydroxylysine (sulfilimine bond) at unknown position [GroupModifiedResidue:2682398] (2S,5R)-5-hydroxylysine (sulfilimine bond) at unknown position |
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No pathways have been reviewed or authored by UniProt:P02462 COL4A1 (51132)
