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Search results 101 to 162 out of 162 for Lyzl4

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0.02s
Type Details Score
GXD Expression  
Probe: MGI:1485377
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1763923
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4826047
Age: embryonic day 14.5
Image: euxassay_005328_17
Specimen Label: euxassay_005328_17
Detected: true
Specimen Num: 14
GXD Expression  
Probe: MGI:1485377
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1763923
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4826047
Age: embryonic day 14.5
Image: euxassay_005328_19
Specimen Label: euxassay_005328_19
Detected: true
Specimen Num: 16
Publication
First Author: Pan J
Year: 2025
Journal: Adv Sci (Weinh)
Title: Microglial Lyzl4 Facilitates β-Amyloid Clearance in Alzheimer's Disease.
Volume: 12
Issue: 2
Pages: e2412184
Publication
First Author: Miyata H
Year: 2016
Journal: Proc Natl Acad Sci U S A
Title: Genome engineering uncovers 54 evolutionarily conserved and testis-enriched genes that are not required for male fertility in mice.
Volume: 113
Issue: 28
Pages: 7704-10
Publication        
First Author: Mouse Genome Database and National Center for Biotechnology Information Editorial Staff Collaboration
Year: 2001
Title: LocusLink Collaboration
Publication      
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
Publication      
First Author: Wellcome Trust Sanger Institute
Year: 2009
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute
Publication      
First Author: Shanghai Model Organisms Center
Year: 2017
Journal: MGI Direct Data Submission
Title: Information obtained from the Shanghai Model Organisms Center (SMOC), Shanghai, China
Publication        
First Author: The Gene Ontology Consortium
Year: 2014
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
Publication        
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
Publication
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
Publication
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
Publication        
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Publication      
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Protein Domain
Type: Family
Description: The vertebrate lysozyme family is composed of lysozyme c, lactalbumin and calcium-binding lysozyme. The classical lysozyme c has been extensively studied []. From human testis cDNA libraries, a group of lysozyme c-like sequences is identified [, ]. The function of this group of lysozyme c-like proteins is not clear. Some of them (LYZL2, SLLP1/SPACA3/LYXL3, LYZL4 and LYZL6) are expressed in the male reproductive tract [, ]and may be involved in fertilisation.This entry represents LYZL1 and LYZL2.
Publication
First Author: Herrero MB
Year: 2005
Journal: Dev Biol
Title: Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding and fertilization.
Volume: 284
Issue: 1
Pages: 126-42
Publication
First Author: Alesi V
Year: 2012
Journal: Gene
Title: 335.4 kb microduplication in chromosome band Xp11.2p11.3 associated with developmental delay, growth retardation, autistic disorder and dysmorphic features.
Volume: 505
Issue: 2
Pages: 384-7
Protein Domain
Type: Family
Description: The vertebrate lysozyme family is composed of lysozyme c, lactalbumin and calcium-binding lysozyme. The classical lysozyme c has been extensively studied []. From human testis cDNA libraries, a group of lysozyme c-like sequences is identified [, ]. The function of this group of lysozyme c-like proteins is not clear. Some of them (LYZL2, SLLP1/SPACA3/LYXL3, LYZL4 and LYZL6) are expressed in the male reproductive tract [, ]and may be involved in fertilisation.Lysozyme-like protein 3 (LYZL3), also known as sperm acrosome membrane-associated protein 3 (SPACA3/SLLP1/LYXL3), is one of them. Mouse LYZL3 (SLLP1) has been shown to be involved in sperm-egg binding and fertilisation [].
Protein Domain
Type: Family
Description: The vertebrate lysozyme family is composed of lysozyme c, lactalbumin and calcium-binding lysozyme. The classical lysozyme c has been extensively studied []. From human testis cDNA libraries, a group of lysozyme c-like sequences is identified [, ]. The function of this group of lysozyme c-like proteins is not clear. Some of them (LYZL2, SLLP1/SPACA3/LYXL3, LYZL4 and LYZL6) are expressed in the male reproductive tract [, ]and may be involved in fertilisation.Lysozyme-like protein 5 (LYZL5), also known as sperm acrosome-associated protein 5 (SPACA5/SLLP-X), is highly expressed in testis and maps to the X chromosome [].
Protein Domain
Type: Family
Description: The vertebrate lysozyme family is composed of lysozyme c, lactalbumin and calcium-binding lysozyme. The classical lysozyme c has been extensively studied []. From human testis cDNA libraries, a group of lysozyme c-like sequences is identified [, ]. The function of this group of lysozyme c-like proteins is not clear. Some of them (LYZL2, SLLP1/SPACA3/LYXL3, LYZL4 and LYZL6) are expressed in the male reproductive tract [, ]and may be involved in fertilisation.LYZL6 exhibits antibacterial activity and may contribute to the innate immunity of the male genital tract [].
Publication
First Author: Stewart CB
Year: 1987
Journal: Nature
Title: Adaptive evolution in the stomach lysozymes of foregut fermenters.
Volume: 330
Issue: 6146
Pages: 401-4
Publication
First Author: Chung LP
Year: 1988
Journal: Proc Natl Acad Sci U S A
Title: Cloning the human lysozyme cDNA: inverted Alu repeat in the mRNA and in situ hybridization for macrophages and Paneth cells.
Volume: 85
Issue: 17
Pages: 6227-31
Publication
First Author: Huang P
Year: 2017
Journal: PLoS One
Title: LYZL6, an acidic, bacteriolytic, human sperm-related protein, plays a role in fertilization.
Volume: 12
Issue: 2
Pages: e0171452
Protein Domain
Type: Family
Description: O-Glycosyl hydrolases () are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [, ]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) website.Glycoside hydrolase family 22 comprises enzymes with two known activities; lysozyme type C () and alpha-lactalbumins. Asp and/or the carbonyl oxygen of the C-2 acetamido group of the substrate acts as the catalytic nucleophile/base. Lysozyme is a muramidase that hydrolyses beta-1,4-links between N-acetyl-muramic acid and N-acetyl-D-glucosamine in the peptidoglycan of bacterial cell walls [], thus helping to fight invading bacteria. In this capacity, the enzyme is found in tears and saliva, but it has also been recruited for a digestive role in the true stomach (abomasum) of ruminants and colobine monkeys: here it probably degrades the cell walls of bacteria passing from the foregut, allowing the breakdown products to be digested by other stomach enzymes [, ]. The stomach form of lysozyme is endowed with special physiochemical properties that allow it to function in an acidic and protease-rich environment.Lysozyme C is similar to alpha-lactalbumin in terms of primary sequence and structure [], and both have probably evolved from a common ancestral protein. There is, however, no similarity in function, lactalbumin being involved in the formation of lactose and is essential for milk production. Another significant difference between the two enzymes is that while all lactalbumins have the ability to bind calcium, this property is restricted to only a few lysozymes [].From human testis cDNA libraries, a group of lysozyme c-like sequences is identified [, ]. The function of this group of lysozyme c-like proteins is not clear. Some of them (LYZL2, SLLP1/SPACA3/LYXL3, LYZL4 and LYZL6) are expressed in the male reproductive tract [, , ]and may be involved in fertilisation.
Protein
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: false
Publication
First Author: Shewale JG
Year: 1984
Journal: J Biol Chem
Title: Evolution of alpha-lactalbumins. The complete amino acid sequence of the alpha-lactalbumin from a marsupial (Macropus rufogriseus) and corrections to regions of sequence in bovine and goat alpha-lactalbumins.
Volume: 259
Issue: 8
Pages: 4947-56
Publication
First Author: Nitta K
Year: 1987
Journal: FEBS Lett
Title: The calcium-binding property of equine lysozyme.
Volume: 223
Issue: 2
Pages: 405-8
Publication
First Author: Irwin DM
Year: 1989
Journal: J Biol Chem
Title: Multiple cDNA sequences and the evolution of bovine stomach lysozyme.
Volume: 264
Issue: 19
Pages: 11387-93
Publication
First Author: Henrissat B
Year: 1995
Journal: Proc Natl Acad Sci U S A
Title: Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.
Volume: 92
Issue: 15
Pages: 7090-4
Publication
First Author: Davies G
Year: 1995
Journal: Structure
Title: Structures and mechanisms of glycosyl hydrolases.
Volume: 3
Issue: 9
Pages: 853-9