Summary: Crisp
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This is the Wikipedia entry entitled "CAP protein family". More...
CAP protein family Edit Wikipedia article
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This is the Wikipedia entry entitled "Cysteine-rich secretory protein". More...
Cysteine-rich secretory protein Edit Wikipedia article
Cysteine-rich secretory proteins, often abbreviated as CRISPs, are a group of glycoproteins[1] found exclusively in vertebrates. They are a subgroup of the CRISP, antigen 5 and Pr-1 (CAP) protein superfamily and are substantially implicated in the functioning of the mammalian reproductive system.[2] CRISPs are also found in a variety of snake venoms where they inhibit both smooth muscle contraction and cyclic nucleotide-gated ion channels.[3]
Mammalian redropduction
CRISPs are found in the testes and epididymis of mammals, and are also involved in the process of fertilisation.[1] In the spermatogenesis process (development of the spermatozoa in the testis), the CRISP2 protein is incorporated into the acrosome where it is believed to be involved in the adhesion of germ cells with Sertoli cells. CRISP2 also forms part of the sperm tail where it is thought to be involved in regulating flagellar beating. Proteins CRISP1 and CRISP4 are both found in the epididymis where they are also incorporated within the spermatozoa as it matures. Protein CRISP3 is found in seminal fluid, excreted from the prostate although its function is presently unknown.[2]
Snake venom
CRISPs are found in the venom of a wide variety of snake species.[3] Examples include ophanin from the King Cobra (Ophiophagus hannah), piscivorin from the Eastern Cottonmouth (Agkistrodon piscivorus)[4] and triflin from the Habu snake (Trimeresurus flavoviridis)[5] – each of these proteins is named for the snake species in which it was discovered. These venoms are toxic due to their blocking of calcium channel and also because they reduce potassium-induced smooth muscle contraction.[6]
References
- ^ a b Cammack, R.; Attwood, T. K.; Campbell, P. N.; Parish, J. H.; Smith, A. D.; Stirling, J. L.; Vella, F., eds. (2006). Oxford Dictionary of Biochemistry and Molecular Biology (2 ed.). New York: Oxford University Press. p. 150. ISBN 0198529171. Retrieved October 27, 2010.
- ^ a b Koppers, A. J.; Reddy, T.; O'Bryan, M. K. (2010). "The Role of Cysteine-Rich Secretory Proteins in Male Fertility". Asian Journal of Andrology. doi:10.1038/aja.2010.77.
- ^ a b Yamazaki, Y.; Morita, T. (2004). "Structure and Function of Snake Venom Cysteine-Rich Secretory Proteins". Toxicon. 44 (3): 227–231. PMID 15302528.
- ^ Yamazaki, Y.; Hyodo, F.; Morita, T. (2003). "Wide Distribution of Cysteine-Rich Secretory Proteins in Snake Venoms: Isolation and Cloning of Novel Snake Venom Cysteine-Rich Secretory Proteins". Arch. Biochem. Biophys. 412 (1): 133–141. doi:10.1016/S0003-9861(03)00028-6.
- ^ Shikamoto, Y.; Suto, K.; Yamazaki, Y.; Morita, T.; Mizuno, H. (2005). "Crystal Structure of a CRISP Family Calcium-Channel Blocker Derived from Snake Venom". J. Mol. Biol. 350 (4): 735–743. doi:10.1016/j.jmb.2005.05.020. PMID 15953617.
- ^ Yamasaki, Y.; Koike, H.; Sugiyama, Y.; Motoyoshi, K.; Wada, T.; Hishinuma, S.; Mita, M.; Morita, T. (2002). "Cloning and Characterization of Novel Snake Venom Proteins that Block Smooth Muscle Contraction". Eur. J. Biochem. 269 (11): 2708–2715. PMID 12047379.
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.
Crisp Provide feedback
This domain is found on Crisp proteins which contain PF00188 and has been termed the Crisp domain. It is found in the mammalian reproductive tract and the venom of reptiles, and has been shown to regulate ryanodine receptor Ca2+ signalling [1]. It contains 10 conserved cysteines which are all involved in disulphide bonds and is structurally related to the ion channel inhibitor toxins BgK and ShK [1].
Literature references
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Gibbs GM, Scanlon MJ, Swarbrick J, Curtis S, Gallant E, Dulhunty A, O'bryan MK; , J Biol Chem. 2005; [Epub ahead of print]: The crisp domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signalling. PUBMED:16339766 EPMC:16339766
This tab holds annotation information from the InterPro database.
InterPro entry IPR013871
This entry is found on Crisp proteins which contain INTERPRO and has been termed the Crisp domain. It is found in the mammalian reproductive tract and the venom of reptiles, and has been shown to regulate ryanodine receptor Ca2+ signalling [ PUBMED:16339766 ]. It contains 10 conserved cysteines which are all involved in disulphide bonds and is structurally related to the ion channel inhibitor toxins BgK and ShK [ PUBMED:16339766 ].
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 ShK-like (CL0213), which has the following description:
Members of this clan include the Crisp domain which is involved in ryanodine receptor Ca2+ signalling, and the ShK domain which is named after the ShK channel inhibitor toxin. Both domains are cysteine rich and contain multiple disulphide bonds [1][2][3].
The clan contains the following 2 members:
Crisp ShKAlignments
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 (65) |
Full (719) |
Representative proteomes | UniProt (1352) |
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RP15 (77) |
RP35 (215) |
RP55 (553) |
RP75 (734) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
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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 (65) |
Full (719) |
Representative proteomes | UniProt (1352) |
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RP15 (77) |
RP35 (215) |
RP55 (553) |
RP75 (734) |
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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: | manual |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Mistry J |
Number in seed: | 65 |
Number in full: | 719 |
Average length of the domain: | 55.5 aa |
Average identity of full alignment: | 47 % |
Average coverage of the sequence by the domain: | 22.07 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 55 | ||||||||||||
Family (HMM) version: | 13 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
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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 Crisp domain has been found. There are 26 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.