Summary: C1 domain
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C1 domain Edit Wikipedia article
| Phorbol esters/diacylglycerol binding domain (C1 domain) | |||||||||
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| 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. |
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| Identifiers | |||||||||
| Symbol | C1 | ||||||||
| Pfam | PF00130 | ||||||||
| InterPro | IPR002219 | ||||||||
| SMART | C1 | ||||||||
| PROSITE | PDOC00379 | ||||||||
| SCOP | 2cpk | ||||||||
| SUPERFAMILY | 2cpk | ||||||||
| OPM superfamily | 63 | ||||||||
| OPM protein | 1ptr | ||||||||
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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.
[edit] 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;
[edit] References
- ^ Azzi A, Boscoboinik D, Hensey C (1992). "The protein kinase C family". Eur. J. Biochem. 208 (3): 547â557. 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): 4868â4871. doi:10.1073/pnas.86.13.4868. PMC 297516. PMID 2500657. //www.ncbi.nlm.nih.gov/pmc/articles/PMC297516/.
[edit] 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.
C1 domain Provide feedback
This short domain is rich in cysteines and histidines. The pattern of conservation is similar to that found in PF00130 therefore we have termed this domain DC1 for divergent C1 domain. This domain probably also binds to two zinc ions. The function of proteins with this domain is uncertain, however this domain may bind to molecules such as diacylglycerol (A Bateman pers. obs.). This family are found in plant proteins.
Internal database links
| SCOOP: | zf-UBR Baculo_IE-1 |
| Similarity to PfamA using HHSearch: | C1_1 C1_3 |
External database links
| PANDIT: | PF03107 |
| Pseudofam: | PF03107 |
| SYSTERS: | C1_2 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR004146
This short domain is rich in cysteines and histidines. The pattern of conservation is similar to that found in DAG_PE-bind (INTERPRO), therefore we have termed this domain DC1 for divergent C1 domain. This domain probably also binds to two zinc ions. The function of proteins with this domain is uncertain, however this domain may bind to molecules such as diacylglycerol. This family are found in plant proteins.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
Alignments
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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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| Seed (90) |
Full (558) |
Representative proteomes | NCBI (664) |
Meta (0) |
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| RP15 (312) |
RP35 (351) |
RP55 (358) |
RP75 (370) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (90) |
Full (558) |
Representative proteomes | NCBI (664) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (312) |
RP35 (351) |
RP55 (358) |
RP75 (370) |
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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.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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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
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Curation and family details
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Curation
| Seed source: | Pfam-B_16 (release 6.5) |
| Previous IDs: | DC1; |
| Type: | Domain |
| Author: | Bateman A |
| Number in seed: | 90 |
| Number in full: | 558 |
| Average length of the domain: | 31.30 aa |
| Average identity of full alignment: | 34 % |
| Average coverage of the sequence by the domain: | 11.07 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 30 | ||||||||||||
| Family (HMM) version: | 11 | ||||||||||||
| Download: | download the raw HMM for this family |
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