The research continues...
The human ovum itself does not produce specific proteins that control the acrosomal reaction. Rather, it is the proteins and glycoproteins found on the zona pellucida (the extracellular matrix surrounding the ovum) that interacts with sperm proteins to facilitate the acrosomal reaction. The zona pellucida is composed of several glycoproteins, as mentioned in my prior post, these include: ZP1, ZP2, ZP3, ZP4.
There are more but I'll touch on them later.
Among these glycoproteins, ZP3 is the primary molecule responsible for initiating the acrosomal reaction in the sperm. ZP3 acts as a sperm receptor, binding to proteins on the sperm's surface. This binding triggers a signaling cascade within the sperm that results in the release of enzymes from the sperm's acrosome.
These enzymes help the sperm to digest the zona pellucida, allowing it to penetrate and reach the ovum's plasma membrane for fertilization.
The acrosomal reaction is an extremely complex multistep process that involves various proteins and signaling pathways in both the sperm and the egg.. Researchers are still working to fully understand all the molecular mechanisms involved. The acrosomal reaction is a crucial step in the fertilization process where the sperm's acrosome, a specialized organelle, releases its enzymes to facilitate penetration through the protective layers surrounding the egg (oocyte), such as the zona pellucida.
Other proteins on the ovum that involved are, CD9 and JUNO.
CD9 is a cell surface protein present on the oocyte plasma membrane, known as the oolemma. CD9 is involved in the fusion of the sperm and oocyte plasma membranes during fertilization, which follows the acrosomal reaction. CD9 is a member of the tetraspanin family, has been shown to play a crucial role in sperm-egg fusion. CD9-deficient eggs have reduced sperm binding and fusion capabilities, leading to impaired fertility in mice. It is thought that CD9 may help organize other proteins on the egg's surface, including integrins like Integrin α6β1.
Integrin α6β1, a heterodimeric transmembrane protein, has been implicated in sperm-egg interactions as a potential receptor for the sperm protein ADAM2 (Fertilin beta). In a study by Almeida et al. (1995), the researchers demonstrated that blocking Integrin α6β1 function impaired sperm-egg binding and fusion in mouse eggs.
Some studies have suggested that CD9 may associate with Integrin α6β1, and together, they could form a functional complex on the egg surface. This complex would then be involved in sperm-egg binding and fusion. For instance, Le Naour et al. (2000) found that CD9 and Integrin α6β1 co-immunoprecipitated from the egg's membrane, suggesting that they might be part of a protein complex.
JUNO (also known as IZUMO1R) is an oocyte membrane receptor that interacts with the sperm protein IZUMO1. JUNO is a member of the folate receptor family, and it is classified under the Pfam03024 family. However, its primary role in the fertilization process, specifically in mediating sperm-egg recognition and adhesion, is distinct from the typical function of other folate receptor proteins.
While these proteins are involved in the process of sperm-egg interaction, the regulation of the acrosomal reaction itself is primarily driven by intracellular calcium signaling in the sperm. Binding to the zona pellucida and the specific proteins mentioned above, along with other signaling molecules, triggers a rise in intracellular calcium in the sperm, which in turn stimulates the acrosomal reaction.
It's important to note that the molecular mechanisms and processes underlying fertilization are complex and multifaceted, with several proteins and signaling pathways working together to ensure successful fertilization.
On the sperm side we have; Izumo1, ADAM2, SPACA6, CRISP1, PLCzeta, SOF1, and PRSS37.
From what we know from research the ADAM2 and SPACA6 are primarily involved in sperm/egg fusion.
Izumo1 is a type I transmembrane protein that is composed of an extracellular immunoglobulin-like domain, a single transmembrane domain, and a short cytoplasmic tail. The extracellular domain is essential for the interaction between Izumo1 and its oocyte receptor, JUNO (IZUMO1R). Izumo1 is the sperm protein believed to be essential for sperm-egg fusion. It binds to its receptor, JUNO, on the egg surface, facilitating sperm-egg recognition and adhesion.
ADAM proteins: A Disintegrin And Metalloprotease (ADAM) family members, particularly ADAM2 and ADAM3, are present on the sperm surface and play a role in sperm-oocyte binding and the acrosome reaction. They function as metalloproteases and help in the processing and maturation of other proteins involved in fertilization. ADAM2, also known as Fertilin beta, is a sperm surface protein involved in sperm-egg interaction.
SPACA6 (Sperm acrosome-associated protein 6) is a protein found in the acrosome of mammalian spermatozoa. It is involved in the acrosome reaction however research on the importance of SPACA6 in the acrosomal reaction is limited. That being said, a study in mice demonstrated that the lack of SPACA6 leads to male infertility due to defects in the acrosome reaction. In this study, it was shown that sperm from SPACA6-deficient mice had a significantly reduced ability to undergo the acrosome reaction, which consequently hindered their ability to fertilize eggs.
CRISP1 (Cysteine-rich secretory protein 1)is a sperm protein that contributes to sperm-zona pellucida binding and is believed to play a role in the acrosome reaction but it is not known how if it does.
PLCzeta (PLCζ) is a sperm-specific protein that triggers calcium oscillations in the oocyte upon sperm-egg fusion. These calcium oscillations are essential for egg activation, initiating a series of events that lead to successful fertilization and the formation of a zygote.
SOF1 (Sperm Outer dense fiber protein 1) is found in the outer dense fibers of spermatozoa, and studies in mice have suggested a potential role in sperm-zona pellucida interaction and the acrosome reaction.
PRSS37 (Serine protease 37) is a testis-specific serine protease that has been suggested to be involved in the sperm-zona pellucida penetration. Research investigating the role of PRSS37 in sperm-zona pellucida penetration is relatively limited. A study conducted by Wei et al. (2013) provided evidence for the involvement of PRSS37 in sperm-zona pellucida penetration.
In this study, the authors generated PRSS37-deficient male mice through gene targeting and examined the fertility of these mice. They found that while PRSS37-null male mice were infertile, their female counterparts were fertile. Further investigation revealed that the sperm from PRSS37-null male mice showed severely impaired penetration through the zona pellucida, indicating the importance of PRSS37 in this process.
Additionally, the study demonstrated that the acrosome reaction and motility of sperm from PRSS37-null male mice were not affected, suggesting that PRSS37 specifically plays a role in sperm-zona pellucida penetration rather than in the acrosome reaction or sperm motility.
The list above is not exhaustive, and other proteins are likely to be involved in the complex process of the acrosome reaction and subsequent events leading to fertilization. Many of these proteins are still being investigated to determine their precise functions and interactions during fertilization.
#############################
Now for a bit of additional information for those that wish to more fully understand the following material.
In the Pfam database, sequence alignments of protein families are represented using single-letter codes for amino acids. These single-letter codes are a standardized system for representing the 20 common amino acids found in proteins. In the sequence alignment, each letter corresponds to a specific amino acid residue in the protein sequence.
Here is the list of the 20 common amino acids and their corresponding single-letter codes:
Alanine (A)
Arginine (R)
Asparagine (N)
Aspartic acid (D)
Cysteine (C)
Glutamine (Q)
Glutamic acid (E)
Glycine (G)
Histidine (H)
Isoleucine (I)
Leucine (L)
Lysine (K)
Methionine (M)
Phenylalanine (F)
Proline (P)
Serine (S)
Threonine (T)
Tryptophan (W)
Tyrosine (Y)
Valine (V)
Additionally you may see sequence alignments may include specific symbols or characters to represent gaps, insertions, or deletions in the alignment. For example:
A dash (-) represents a gap in the alignment, indicating that a residue is missing or not conserved at that position in the protein sequence for a particular species.
An "X" signifies that the amino acid residue at a particular position is not known or could not be determined.
A "B" stands for either aspartic acid (D) or asparagine (N), when the specific amino acid cannot be determined.
A "Z" represents either glutamic acid (E) or glutamine (Q) when the specific amino acid cannot be determined.
These single-letter codes and symbols provide a compact and efficient way to represent protein sequences and display alignments across multiple species, highlighting conserved regions and variations within protein families.
So for instance if we wanted to compare CD9 between Humans, Dogs, Horses, and Mice, we would have the following Protein sequences:
Human:
MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGV
YILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKE
VQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKS
CPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV
Dog:
MPVKGGTKCIKYLLFGFNFVFWLAGIAVLAVGLWLRFDSQTKSIFEQDTQPSSFYTGVYI
LIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQ
EFYKDTYSKLKSKDEPQRDTLKAIHYALNCCGLVGGVEQFISDICPQKDVLSSITVKPCP
EAIKEVFQNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRSREMV
Horse:
MPVKGGTKCIKYLLFGFNFVFWLAGIAVLAIGLWLRFDSQTKSIFEQENNNSSFYTGVYI
LIGAGALIMVVGFLGCCGAVQESQCMLGLFFCFLLVIFAIEIAAAIWGYSHKDEVIKDIQ
EFYKDTYNKLKTKDEPQRETLKAIHYAVGHLCKDPDPCGLSGGRLCTWDACHTSLCRSSF
YLFLSPPSLSLQLDCCGIVGGVEQFISDICPQKDVLSSFTTKPCPEAIKEVFDNKFHIIG
AVGIGIAVVMIFGMIFSMILCCAIRRSREMV
Mouse:
MPVKGGSKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQENNHSSFYTGVYI
LIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAVWGYTHKDEVIKELQ
EFYKDTYQKLRSKDEPQRETLKAIHMALDCCGIAGPLEQFISDTCPKKQLLESFQVKPCP
EAISEVFNNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRSREMV
Sources:
Human:
https://www.ensembl.org/Homo_sapien...010278;r=12:6200400-6238266;t=ENST00000009180
Dog:
https://www.ensembl.org/Canis_lupus...3;r=27:39099221-39131485;t=ENSCAFT00845052450
Horse:
https://www.ensembl.org/Equus_cabal...02;r=6:34796287-34828525;t=ENSECAT00000111308
Mouse:
https://www.ensembl.org/Mus_musculu...;r=6:125437229-125471754;t=ENSMUST00000032492
#############################
When preforming comparative analysis, these will be length matched with gaps added to find the common amino acids in the protein.
When length correcting CD9 we get the following Comparison.
The similarity between human and dog is 93.04%.
The similarity between human and horse is 76.92%.
The similarity between human and mouse is 90.11%.
The reason I choose these three animals is due to the fact that mice are most commonly used for testing due to their similarity to humans in many regards. I included horse, because of the results that were shown in a study mentioned here:
https://www.zoovilleforum.net/threads/dog-semen-human-egg-fertilization.7841/post-1702428
I was curious to see if any inference could be made as to if canine sperm would behave the same way as Horse Sperm do with a human ovum.
Ok, so lets go down the list of Proteins and see what's what. Note, all of these comparisons are length corrected. This might not be 100% accurate as it can be very difficult to deduce where to cut and lengthen a string to match.
ZP2:
The similarity between human and dog 65.15%.
The similarity between human and horse 66.53%.
The similarity between human and mouse 47.12%.
ZP3:
The similarity between human and dog 67.29%.
The similarity between human and horse <10%.
The similarity between human and mouse 66.20%.
ZP4:
The similarity between human and dog 62.54%.
The similarity between human and horse <10%.
The similarity between human and mouse 69.81%.
JUNO:
The similarity between human and dog is 54.09%. (The dogs protein has a very different length, if we lop off that end bit our similarity is = 67.45%)
The similarity between human and horse is 74.00%.
The similarity between human and mouse is 64.40%.
ADAM2:
The similarity between human and dog is 69.64%.
The similarity between human and horse is 40.62%.
The similarity between human and mouse is 50.07%.
SPACA6:
The similarity between human and dog 70.46%.
The similarity between human and horse 81.23%.
The similarity between human and mouse 53.24%.
PRSS37:
The similarity between human and dog 85.53%.
The similarity between human and horse 85.11%.
The similarity between human and mouse 82.28%.
The following do not seem to have analogous proteins between the four species so I didn't spend the time to analyze these. Someone else can if they want.
ZP1, ADAM3, CRISP1, PLCzeta, GLIPR1L1.
#############################
So what in all this am I focusing on. Research does tend to show that CD9 is more important for sperm-zona pellucida interaction than IZUMO1R.
CD9 (Cluster of Differentiation 9) is a cell surface protein expressed on both the oocyte and sperm surfaces that is involved in a variety of biological processes, including cell adhesion, migration, and fusion. CD9 is known to interact with other proteins, including integrins and ADAMs, to mediate sperm-egg fusion.
IZUMO1R (Izumo1 receptor) is a protein expressed on the oocyte surface that is involved in the recognition and binding of IZUMO1 on the surface of sperm. IZUMO1R plays a critical role in the fusion of sperm and egg membranes during fertilization, but it is not directly involved in sperm-zona pellucida interaction.
On the sperm side of the matter research tends to show that while both ADAM2 and SPACA6 are involved in sperm-zona pellucida interaction in human reproduction, but ADAM2 is considered more important.
ADAM2 plays a crucial role in sperm-egg interaction by binding to a glycoprotein on the surface of the egg called zona pellucida glycoprotein 3 (ZP3).
On the other hand, SPACA6 is also involved in sperm-egg interaction, but its exact function is not yet fully understood. It is believed to play a role in the formation of the acrosome, a structure on the head of the sperm that helps it penetrate the zona pellucida.
So lets look at the ones that stand out as important, but cataloged by species instead of protein.
Dog similarity to Human:
CD9: 93.04%
ZP3: 67.29%
JUNO: 54.09% (at best 67.45%)
ADAM2: 69.64%
SPACA6: 70.46%
Horse similarity to Human:
CD9: 76.92%
ZP3: <10%
JUNO: 74.00%
ADAM2: 40.62%
SPACA6: 81.23%
Mouse similarity to Human:
CD9: 90.11%
ZP3: 66.20%
JUNO: 64.40%
ADAM2: 50.07%
SPACA6: 53.24%
With research seemingly indicating that CD9, ZP3, and ADAM2 being the playing the primary roles in Sperm/Egg interaction and initial capture, the numbers show that Dogs are more similar to Humans than Horses are.
So we can tentatively infer that the interaction between Canine Sperm and a Human Ovum should behave somewhere between the interaction of Horse Sperm and a Human Ovum and a Human Sperm and Human Ovum.
To what extent that is, I have no idea. We cannot infer much more than this... and anyone who reads this and thinks "The Science is settled" is an idiot and deserves to be mocked relentlessly. I have not ready every study on this, so there may be studies out there that contradict my inferences. Furthermore, this is an inferrence based on nothing more than protien similarity, but those amino acid differences between proteins matter. They will affect the way the protein folds and interacts with other proteins. This is very much an inference based on an inference based on an assumption.
This is not proven in any meaning of the word. This is effectively nothing more than an educated guess backed by logical deduction.
It is important to keep in mind that we are only talking about Sperm Capture.
This does not mean that the Acrosomal Reaction occurs.
This does not mean ZP Penetration occurs.
This does not mean Fertilization occurs.
This does not mean a Hybrid is formed.
This does not mean a Zygote will implant in the uterine wall.
This only means... at best... that canine sperm may 'stick' to a human egg... nothing more.
Ok now that that is out of the way for the tards that will think this means their dreams will come true...
I am actually somewhat surprised that Dogs are protein sequence wise, more similar to Humans than Mice. I did not expect that to be the case. Outside of ZP2, ZP4, and JUNO, the Canine's protein sequence was all closer to humans.
Note: I may make minor corrections to this over time if I realize later I had any typos, grammatical errors, or I explained something incorrectly because it's late and I'm trying to quickly get this into a digestible format for people who don't have a degree in biology and spend free time reading up on micro-cellular biology.
#############################
Source for those who want to go down the rabbit hole, in no particular order...
(I had to break these links so that the page wouldnt freak out trying to render previews. You can fix the link by removing the extra space.
https:/ /www.nature.com/articles/s41598-020-62091-y
https:/ /www.ncbi.nlm.nih.gov/gene/75202
https:/ /www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=DetailsSearch&Term=147650
https:/ /rgd.mcw.edu/rgdweb/report/gene/main.html?id=1588836
https:/ /www.ncbi.nlm.nih.gov/pmc/articles/PMC9671554/
https:/ /www.biorxiv.org/content/10.1101/2022.02.01.478669v2.full
https:/ /www.genecards.org/cgi-bin/carddisp.pl?gene=IZUMO1R
https:/ /swissmodel.expasy.org/repository/uniprot/A6ND01?range=20-228&template=5f4e.1.B
https:/ /www.ebi.ac.uk/pdbe/pdbe-kb/proteins/A6ND01/structures
https:/ /alphafold.ebi.ac.uk/entry/A6ND01
https:/ /useast.ensembl.org/Canis_lupus_familiaris/Transcript/Summary?db=core;g=ENSCAFG00845020509;r=21:6777062-6784386;t=ENSCAFT00845036118
https:/ /www.ncbi.nlm.nih.gov/gene/607523
https:/ /www.ncbi.nlm.nih.gov/gene/390243
https:/ /www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=397250
https:/ /useast.ensembl.org/Equus_caballus/Transcript/ProteinSummary?db=core;g=ENSECAG00000002989;r=12:24179479-24189489;t=ENSECAT00000003876
https:/ /useast.ensembl.org/Homo_sapiens/Transcript/Sequence_Protein?db=core;g=ENSG00000149506;r=11:60867542-60875693;t=ENST00000278853
https:/ /useast.ensembl.org/Mus_musculus/Transcript/ProteinSummary?db=core;g=ENSMUSG00000024734;r=19:10891651-10897996;t=ENSMUST00000025641
https:/ /useast.ensembl.org/Canis_lupus_familiaris/Gene/Summary?db=core;g=ENSCAFG00845004559;r=6:7406839-7415182;t=ENSCAFT00845008161
https:/ /useast.ensembl.org/Mus_musculus/Transcript/ProteinSummary?db=core;g=ENSMUSG00000004948;r=5:136008953-136017478;t=ENSMUST00000005073
https:/ /useast.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000188372;r=7:76397518-76442071
https:/ /useast.ensembl.org/Equus_caballus/Transcript/ProteinSummary?db=core;g=ENSECAG00000008731;r=13:10561209-10570863;t=ENSECAT00000009170
https:/ /useast.ensembl.org/Canis_lupus_familiaris/Gene/Summary?db=core;g=ENSCAFG00845002311;r=4:2343307-2350533;t=ENSCAFT00845004088
https:/ /useast.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000116996;r=1:237877864-237890922
GLLLQQCWATPSTDPLSQPQWPILVKGCPYIGDNYQTQLIPVQKALDLPFPSHHQRFSIF
https:/ /useast.ensembl.org/Mus_musculus/Transcript/ProteinSummary?db=core;g=ENSMUSG00000020226;r=10:75893328-75946795;t=ENSMUST00000120757
https:/ /useast.ensembl.org/Equus_caballus/Transcript/Sequence_Protein?db=core;g=ENSECAG00000010697;r=1:74820305-74834029;t=ENSECAT00000101449
https:/ /useast.ensembl.org/Homo_sapiens/Transcript/https://useast.ensembl.org/Equus_caballus/Gene/Summary?db=core;g=ENSECAG00000011049;r=20:48856838-48887485
https:/ /useast.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000025431;r=17:40604649-40630098;t=ENSMUST00000026498
https:/ /useast.ensembl.org/Canis_lupus_familiarisgermanshepherd/Gene/Summary?db=core;g=ENSCAFG00805030125;r=16:26520796-26652100
https:/ /useast.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000104755;r=8:39743735-39838227
https:/ /useast.ensembl.org/Equus_caballus/Gene/Summary?db=core;g=ENSECAG00000000073;r=27:6427508-6562796
https:/ /useast.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000022039;r=14:66264778-66315182
https:/ /useast.ensembl.org/Homo_sapiens/Transcript/ProteinSummary?db=core;g=ENSG00000156886;r=16:31393335-31426505;t=ENST00000389202
https:/ /useast.ensembl.org/Canis_lupus_familiaris/Gene/
https:/ /useast.ensembl.org/Canis_lupus_familiaris/Gene/Summary?db=core;g=ENSCAFG00845030911;r=16:7300899-7306701;t=ENSCAFT00845054940
https:/ /useast.ensembl.org/Homo_sapiens/Transcript/ProteinSummary?db=core;g=ENSG00000165076;r=7:141836300-141841487;t=ENST00000350549
https:/ /useast.ensembl.org/Equus_caballus/Transcript/Sequence_Protein?db=core;g=ENSECAG00000007637;r=4:94708134-94713793;t=ENSECAT00000007704
https:/ /useast.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000029909;r=6:40491758-40496442
https:/ /useast.ensembl.org/Canis_lupus_familiaris/Transcript/ProteinSummary?db=core;g=ENSCAFG00845003418;r=6:24381539-24393797;t=ENSCAFT00845006076
https:/ /useast.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000103310;r=16:21197450-21214510
https:/ /useast.ensembl.org/Equus_caballus/Gene/Summary?db=core;g=ENSECAG00000019961;r=13:26897628-26918256
https:/ /useast.ensembl.org/Mus_musculus/Transcript/ProteinSummary?db=core;g=ENSMUSG00000030911;r=7:119725995-119744514;t=ENSMUST00000033207
Reference:
https:/ /bmcbiol.biomedcentral.com/articles/10.1186/s12915-019-0701-1
https:/ /useast.ensembl.org/Canis_lupus_familiaris/Transcript/ProteinSummary?db=core;g=ENSCAFG00845020509;r=21:6777062-6784386;t=ENSCAFT00845036118
https:/ /useast.ensembl.org/Canis_lupus_familiaris/Gene/Summary?db=core;g=ENSCAFG00845004847;r=1:105901344-105909988;t=ENSCAFT00845008679
https:/ /useast.ensembl.org/homo_sapiens/Gene/Summary?g=ENSG00000182310&db=core
https:/ /useast.ensembl.org/Canis_lupus_familiaris/Gene/Summary?db=core;g=ENSCAFG00845004847;r=1:105901344-105909988;t=ENSCAFT00845008679
https:/ /useast.ensembl.org/Equus_caballus/Gene/Summary?db=core;g=ENSECAG00000006938;r=10:21663697-21676161
https:/ /useast.ensembl.org/Mus_musculus/Transcript/ProteinSummary?db=core;g=ENSMUSG00000080316;r=17:18047420-18063271;t=ENSMUST00000172097
https:/ /useast.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000173401;r=12:75334670-75370560
https:/ /useast.ensembl.org/Canis_lupus_familiaris/Gene/Summary?db=core;g=ENSCAFG00845017781;r=12:2582113-2583737;t=ENSCAFT00845031475
https:/ /useast.ensembl.org/Equus_caballus/Gene/Summary?db=core;g=ENSECAG00000015592;r=28:4284888-4323990
https:/ /useast.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000020213;r=10:111896094-111914415;t=ENSMUST00000073617
https:/ /useast.ensembl.org/Homo_sapiens/Transcript/ProteinSummary?db=core;g=ENSG00000183560;r=11:94304580-94308146;t=ENST00000687084
https:/ /www.ensembl.org/Canis_lupus_familiaris/Transcript/ProteinSummary?db=core;g=ENSCAFG00845020509;r=21:6777062-6784386;t=ENSCAFT00845036118
https:/ /useast.ensembl.org/Equus_caballus/Transcript/ProteinSummary?db=core;g=ENSECAG00000007254;r=7:54977424-55001377;t=ENSECAT00000031919
https:/ /useast.ensembl.org/Mus_musculus/Transcript/ProteinSummary?db=core;g=ENSMUSG00000031933;r=9:14797110-14815245;t=ENSMUST00000034409
Other Studies:
Cho, C., Bunch, D. O., Faure, J. E., Goulding, E. H., Eddy, E. M., Primakoff, P., & Myles, D. G. (1998). Fertilization defects in sperm from mice lacking fertilin beta. Science, 281(5384), 1857-1859.
Blobel, C. P., Wolfsberg, T. G., Turck, C. W., Myles, D. G., Primakoff, P., & White, J. M. (1992). A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature, 356(6366), 248-252.
Almeida, E. A., Huovila, A. P., Sutherland, A. E., Stephens, L. E., Calarco, P. G., Shaw, L. M., Mercurio, A. M., Sonnenberg, A., Primakoff, P., Myles, D. G., & White, J. M. (1995). Mouse egg integrin α6β1 functions as a sperm receptor. Cell, 81(7), 1095-1104.
Le Naour, F., Rubinstein, E., Jasmin, C., Prenant, M., & Boucheix, C. (2000). Severely reduced female fertility in CD9-deficient mice. Science, 287(5451), 319-321.
Wei, Z., Chen, X., Wang, W., Cao, Y., Zhang, S., Wang, X., He, Z., Zhou, P., & Dong, C. (2013). Disruption of testis-specific serine protease 37 (PRSS37) causes male infertility. The FASEB Journal, 27(12), 4867-4878.
Inoue, N., Ikawa, M., Isotani, A., & Okabe, M. (2005). The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs. Nature, 434(7030), 234-238.
Bianchi, E., Doe, B., Goulding, D., & Wright, G. J. (2014). Juno is the egg Izumo receptor and is essential for mammalian fertilization. Nature, 508(7497), 483-487.
Aydin, H., Sultana, A., Li, S., Thavalingam, A., & Lee, J. E. (2016). Molecular architecture of the human sperm IZUMO1 and egg JUNO fertilization complex. Nature, 534(7608), 562-565.
Ohto, U., Ishida, H., Krayukhina, E., Uchiyama, S., Inoue, N., & Shimizu, T. (2016). Structure of IZUMO1-JUNO reveals sperm-oocyte recognition during mammalian fertilization. Nature, 534(7608), 566-569.
Fujihara, Y., Oji, A., Larasati, T., Kojima-Kita, K., Ikawa, M. (2018). Human Globozoospermia-Related Gene Spata16 Is Required for Sperm Formation Revealed by CRISPR/Cas9-Mediated Mouse Models. International Journal of Molecular Sciences, 19(10), 2909.
)