Summary: Phorbol esters/diacylglycerol binding domain (C1 domain)
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C1 domain Edit Wikipedia article
| Phorbol esters/diacylglycerol binding domain (C1 domain) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 C1 domain of PKC-delta (1ptr)
Middle plane of the lipid bilayer - black dots. Boundary of the hydrocarbon core region - blue dots (cytoplasmic side). Layer of lipid phosphates - yellow dots. | |||||||||
| Identifiers | |||||||||
| Symbol | C1 | ||||||||
| Pfam | PF00130 | ||||||||
| InterPro | IPR002219 | ||||||||
| SMART | C1 | ||||||||
| PROSITE | PDOC00379 | ||||||||
| SCOPe | 2cpk / SUPFAM | ||||||||
| OPM superfamily | 60 | ||||||||
| OPM protein | 1ptr | ||||||||
| CDD | cd00029 | ||||||||
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C1 domain (also known as phorbol esters/diacylglycerol binding domain) binds an important secondary messenger diacylglycerol (DAG), as well as the analogous phorbol esters.[1] Phorbol esters can directly stimulate protein kinase C, PKC. The N-terminal region of PKC, known as C1, has been shown[2]
Phorbol esters (such as PMA) are analogues of DAG and potent tumor promoters that cause a variety of physiological changes when administered to both cells and tissues. DAG activates a family of serine/threonine protein kinases, collectively known as protein kinase C (PKC). Phorbol esters can directly stimulate PKC.
The N-terminal region of PKC, known as C1, binds PMA and DAG in a phospholipid and zinc-dependent fashion. The C1 region contains one or two copies of a cysteine-rich domain, which is about 50 amino-acid residues long, and which is essential for DAG/PMA-binding.
The DAG/PMA-binding domain binds two zinc ions; the ligands of these metal ions are probably the six cysteines and two histidines that are conserved in this domain.
Human proteins containing this domain
AKAP13; ARAF; ARHGAP29; ARHGEF2; BRAF; CDC42BPA; CDC42BPB; CDC42BPG; CHN1; CHN2; CIT; DGKA; DGKB; DGKD; DGKE; DGKG; DGKH; DGKI; DGKK; DGKQ; DGKZ; GMIP; HMHA1; KSR1; KSR2; MYO9A; MYO9B; PDZD8; PRKCA; PRKCB1; PRKCD; PRKCE; PRKCG; PRKCH; PRKCI; PRKCN; PRKCQ; PRKCZ; PRKD1; PRKD2; PRKD3; RACGAP1; RAF1; RASGRP; RASGRP1; RASGRP2; RASGRP3; RASGRP4; RASSF1; RASSF5; ROCK1; ROCK2; STAC; STAC2; STAC3; TENC1; UNC13A; UNC13B; UNC13C; VAV1; VAV2; VAV3;
References
- ^ Azzi A, Boscoboinik D, Hensey C (1992). "The protein kinase C family". Eur. J. Biochem. 208 (3): 547–557. doi:10.1111/j.1432-1033.1992.tb17219.x. PMID 1396661.
- ^ Kikkawa U, Nishizuka Y, Igarashi K, Fujii T, Ono Y, Kuno T, Tanaka C (1989). "Phorbol ester binding to protein kinase C requires a cysteine-rich zinc-finger-like sequence". Proc. Natl. Acad. Sci. U.S.A. 86 (13): 4868–4871. doi:10.1073/pnas.86.13.4868. PMC 297516. PMID 2500657.
External links
- UMich Orientation of Proteins in Membranes families/superfamily-63 - Orientations of C1 domains in membranes (OPM)
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Phorbol esters/diacylglycerol binding domain (C1 domain) Provide feedback
This domain is also known as the Protein kinase C conserved region 1 (C1) domain.
Literature references
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Knighton DR, Zheng JH, Ten Eyck LF, Ashford VA, Xuong NH, Taylor SS, Sowadski JM; , Science. 1991;253:407-414.: Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. PUBMED:1862342 EPMC:1862342
Internal database links
| SCOOP: | C1_2 PH PHD PHD_2 Prok-RING_1 zf-C2H2 zf-H2C2_2 zf-PHD-like zf-RING-like zf-RING_2 zf-RING_9 Zf_RING Zn_ribbon_17 |
| Similarity to PfamA using HHSearch: | C1_2 zf-RING-like |
External database links
| HOMSTRAD: | C1 |
| PRINTS: | PR00008 |
| PROSITE: | PDOC00379 |
| SCOP: | 2cpk |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002219
Diacylglycerol (DAG) is an important second messenger. Phorbol esters (PE) are analogues of DAG and potent tumour promoters that cause a variety of physiological changes when administered to both cells and tissues. DAG activates a family of serine/threonine protein kinases, collectively known as protein kinase C (PKC) [ PUBMED:1396661 ]. Phorbol esters can directly stimulate PKC. The N-terminal region of PKC, known as C1, has been shown [ PUBMED:2500657 ] to bind PE and DAG in a phospholipid and zinc-dependent fashion. The C1 region contains one or two copies (depending on the isozyme of PKC) of a cysteine-rich domain, which is about 50 amino-acid residues long, and which is essential for DAG/PE-binding. The DAG/PE-binding domain binds two zinc ions; the ligands of these metal ions are probably the six cysteines and two histidines that are conserved in this domain.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Biological process | intracellular signal transduction (GO:0035556) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan C1 (CL0006), which has the following description:
The members of this clan are all variations of the protein kinase C1 domain that is characterised by a rich cysteine and histidine content. The C1 domain is the N-terminal region of conservation found in protein kinase C domains. This domain is involved in binding many ligands, which include diacylglycerol, phorbol esters and zinc [1].
The clan contains the following 4 members:
C1_1 C1_2 C1_4 ZZAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (44) |
Full (35851) |
Representative proteomes | UniProt (61200) |
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| RP15 (4516) |
RP35 (11800) |
RP55 (30364) |
RP75 (41297) |
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| HTML | |||||||
| PP/heatmap | 1 | ||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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| Seed (44) |
Full (35851) |
Representative proteomes | UniProt (61200) |
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|---|---|---|---|---|---|---|---|
| RP15 (4516) |
RP35 (11800) |
RP55 (30364) |
RP75 (41297) |
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| Raw Stockholm | |||||||
| Gzipped | |||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Prosite |
| Previous IDs: | DAG_PE-bind; C1; |
| Type: | Domain |
| Sequence Ontology: | SO:0000417 |
| Author: |
Bateman A 
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| Number in seed: | 44 |
| Number in full: | 35851 |
| Average length of the domain: | 52.60 aa |
| Average identity of full alignment: | 31 % |
| Average coverage of the sequence by the domain: | 7.45 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 53 | ||||||||||||
| Family (HMM) version: | 24 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the C1_1 domain has been found. There are 57 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.
