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1  structure 28  species 0  interactions 800  sequences 64  architectures

Family: C1_3 (PF07649)

Summary: C1-like domain

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This is the Wikipedia entry entitled "C1 domain". More...

C1 domain Edit Wikipedia article

Phorbol esters/diacylglycerol binding domain (C1 domain)
1ptr.png
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
SCOP 2cpk
SUPERFAMILY 2cpk
OPM superfamily 63
OPM protein 1ptr

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[edit]

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[edit]

  1. ^ 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. 
  2. ^ 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[edit]

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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-like domain Provide feedback

This short domain is rich in cysteines and histidines. The pattern of conservation is similar to that found in PF00130.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR011424

This short domain is rich in cysteines and histidines. The pattern of conservation is similar to that found in INTERPRO. C1 domains are protein kinase C-like zinc finger structures. Diacylglycerol (DAG) kinases (DGKs) have a two or three commonly conserved cysteine-rich C1 domains [PUBMED:18691010]. DGKs modulate the balance between the two signaling lipids, DAG and phosphatidic acid (PA), by phosphorylating DAG to yield PA [PUBMED:17512245].

The PKD (protein kinase D) family are novel DAG receptors. They have twin C1 domains, designated C1a and C1b, which bind DAG or phorbol esters. Individual C1 domains differ in ligand-binding activity and selectivity [PUBMED:18076381].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

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 contains the following 5 members:

C1_1 C1_2 C1_3 C1_4 ZZ

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...

View options

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
(194)
Full
(800)
Representative proteomes NCBI
(923)
Meta
(2)
RP15
(367)
RP35
(463)
RP55
(489)
RP75
(533)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(194)
Full
(800)
Representative proteomes NCBI
(923)
Meta
(2)
RP15
(367)
RP35
(463)
RP55
(489)
RP75
(533)
Alignment:
Format:
Order:
Sequence:
Gaps:
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Download options

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
(194)
Full
(800)
Representative proteomes NCBI
(923)
Meta
(2)
RP15
(367)
RP35
(463)
RP55
(489)
RP75
(533)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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.

Pfam alignments:

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 View help on the curation process

Seed source: Context Domains
Previous IDs: none
Type: Domain
Author: Finn RD
Number in seed: 194
Number in full: 800
Average length of the domain: 29.60 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 11.59 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 20.7 20.7
Noise cut-off 20.6 20.6
Model length: 30
Family (HMM) version: 7
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_3 domain has been found. There are 1 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 seqence.

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