We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU00736
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00736
General rule information
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| Accession | PRU00736 |
| Dates | 10-DEC-2008 (Created)
21-NOV-2019 (Last updated, Version 11) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51403; NC1_IV |
Name | Collagen IV carboxyl-terminal non-collagenous (NC1) domain |
| Function | Each type IV chain contains a long triple-helical collagenous domain flanked by a short 7S domain of 25 residues and a globular non-collagenous NC1 domain of ~230 residues at the N- and C-terminus, respectively. |
| Scope(s) |
Eukaryota Metazoa |
| Example(s) | P02462; |
Propagated annotation
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Comments
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| SUBCELLULAR LOCATION | Secreted, extracellular space, extracellular matrix, basement membrane. |
| 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. |
| PTM | Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. |
| PTM | Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. |
| SIMILARITY | Belongs to the type IV collagen family. |
Keywords
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| Basement membrane | |
| Collagen | |
| Extracellular matrix | |
| Secreted | |
| case <FTTag:disulf> | |
| Disulfide bond | |
| end case | |
Gene Ontology
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| GO:0005604; Cellular component:basement membrane |
| GO:0031012; Cellular component:extracellular matrix |
Features
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| From: PS51403 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="Collagen IV NC1 #" | |||||||||
| DISULFID | 16 | 106 | disulf | C-x*-C | ||||||||
| DISULFID | 49 | 103 | disulf | C-x*-C | ||||||||
| DISULFID | 61 | 67 | disulf | C-x*-C | ||||||||
| DISULFID | 125 | 220 | disulf | C-x*-C | ||||||||
| DISULFID | 159 | 217 | disulf | C-x*-C | ||||||||
| DISULFID | 171 | 177 | disulf | C-x*-C | ||||||||
Additional information
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| Size range | 220-230 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Not cytoplasmic |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Eukaryota [20] All [ 20 ]
- Retrieve set of proteins with 3D structure for this domain