Summary: Egg lysin (Sperm-lysin)
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Egg lysin Edit Wikipedia article
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| Identifiers | |||||||||
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| Symbol | Egg_lysin | ||||||||
| Pfam | PF01303 | ||||||||
| InterPro | IPR001379 | ||||||||
| SCOP | 1lis | ||||||||
| SUPERFAMILY | 1lis | ||||||||
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Egg lysin is a protein that creates a hole in the envelope of the egg thereby allowing the sperm to pass through the envelope and fuse with the egg.
Fertilization proteins are acrosomal proteins involved in various roles during the fertilization process. Structurally these proteins consist of a closed bundle of helices with a right-hand twist. Lysin and SP18, both characterised in abalone, are two evolutionarily related fertilization proteins that have distinctive roles.
Following its release from sperm, lysin binds to the egg vitelline envelope (VE) via the VE receptor for lysin (VERL), then non-enzymatically dissolves the VE to create a hole, thereby allowing the sperm to pass through the envelope and fuse with the egg.[1] Lysins exhibit species-specific binding to their egg receptor, possibly through differences in charged surface residues.[2] SP18 is also released from sperm, acting as a potent fusagen of liposomes to mediate the fusion between the sperm and egg cell membranes. Despite a similarity in the overall fold, the variation in the surface features of SP18 and lysin account for their different roles in fertilization.[3]
[edit] References
- ^ Stout CD, Vacquier VD, Kresge N (2000). "1.35 and 2.07 A resolution structures of the red abalone sperm lysin monomer and dimer reveal features involved in receptor binding". Acta Crystallogr. D 56: 34–41. PMID 10666624.
- ^ Stout CD, Vacquier VD, Kresge N (2000). "The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of the egg receptor". J. Mol. Biol. 296 (5): 1225–1234. doi:10.1006/jmbi.2000.3533. PMID 10698629.
- ^ Stout CD, Vacquier VD, Kresge N (2001). "The crystal structure of a fusagenic sperm protein reveals extreme surface properties". Biochemistry 40 (18): 5407–5413. doi:10.1021/bi002779v. PMID 11331004.
This article incorporates text from the public domain Pfam and InterPro IPR001379
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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.
Egg lysin (Sperm-lysin) Provide feedback
Egg lysin creates a hole in the envelope of the egg thereby allowing the sperm to pass through the envelope and fuse with the egg.
Literature references
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Shaw A, McRee DE, Vacquier VD, Stout CD; , Science 1993;262:1864-1867.: The crystal structure of lysin, a fertilization protein. PUBMED:8266073 EPMC:8266073
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Shaw A, Fortes PA, Stout CD, Vacquier VD; , J Cell Biol 1995;130:1117-1125.: Crystal structure and subunit dynamics of the abalone sperm lysin dimer: egg envelopes dissociate dimers, the monomer is the active species. PUBMED:7657696 EPMC:7657696
External database links
| HOMSTRAD: | Egg_lysin |
| PANDIT: | PF01303 |
| Pseudofam: | PF01303 |
| SCOP: | 1lis |
| SYSTERS: | Egg_lysin |
This tab holds annotation information from the InterPro database.
InterPro entry IPR001379
Fertilization proteins are acrosomal proteins involved in various roles during the fertilization process. Structurally these proteins consist of a closed bundle of helices with a right-hand twist. Lysin and SP18, both characterised in abalone, are two evolutionarily related fertilization proteins that have distinctive roles. Following its release from sperm, lysin binds to the egg vitelline envelope (VE) via the VE receptor for lysin (VERL), then non-enzymatically dissolves the VE to create a hole, thereby allowing the sperm to pass through the envelope and fuse with the egg [PUBMED:10666624]. Lysins exhibit species-specific binding to their egg receptor, possibly through differences in charged surface residues [PUBMED:10698629]. SP18 is also released from sperm, acting as a potent fusagen of liposomes to mediate the fusion between the sperm and egg cell membranes. Despite a similarity in the overall fold, the variation in the surface features of SP18 and lysin account for their different roles in fertilization [PUBMED:11331004].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Biological process | single fertilization (GO:0007338) |
Domain organisation
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Alignments
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| Seed (24) |
Full (77) |
Representative proteomes | NCBI (85) |
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| RP15 (0) |
RP35 (0) |
RP55 (2) |
RP75 (2) |
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| PP/heatmap | 1 | |||||||
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| Seed (24) |
Full (77) |
Representative proteomes | NCBI (85) |
Meta (0) |
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| RP15 (0) |
RP35 (0) |
RP55 (2) |
RP75 (2) |
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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.
HMM logo
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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: | Pfam-B_1464 (release 3.0) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Finn RD, Bateman A |
| Number in seed: | 24 |
| Number in full: | 77 |
| Average length of the domain: | 88.00 aa |
| Average identity of full alignment: | 52 % |
| Average coverage of the sequence by the domain: | 83.19 % |
HMM information
| HMM build commands: |
build method: hmmbuild --amino -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: | 121 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| 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 Egg_lysin domain has been found. There are 11 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence