EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.4.11.1 | additional information | construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview | Drosophila melanogaster |
3.4.11.1 | additional information | construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview | Drosophila melanogaster |
3.4.11.1 | additional information | construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview | Drosophila melanogaster |
3.4.11.1 | additional information | construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview | Drosophila melanogaster |
3.4.11.1 | additional information | construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview | Drosophila melanogaster |
3.4.11.1 | additional information | construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function | Drosophila melanogaster |
3.4.11.1 | additional information | construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation | Drosophila melanogaster |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.11.1 | mitochondrion | two mitochondrial derivatives differentiate and by the end of spermatogenesis the minor one reduces its size and the major one accumulates paracrystalline material inside it. The S-Lap enzymes are important constituents of the paracrystalline material in mitochondria of Drosophila melanogaster sperm. S-Lap proteins localize and accumulate in the paracrystalline material of the major mitochondrial derivative, S-Lap proteins are collectively present in the isolates | Drosophila melanogaster | 5739 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.11.1 | Mn2+ | required | Drosophila melanogaster | |
3.4.11.1 | Zn2+ | required | Drosophila melanogaster |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.11.1 | Drosophila melanogaster | Q500X4 | - |
- |
3.4.11.1 | Drosophila melanogaster | Q7K2S9 | - |
- |
3.4.11.1 | Drosophila melanogaster | Q7K5K9 | - |
- |
3.4.11.1 | Drosophila melanogaster | Q8T4F1 | - |
- |
3.4.11.1 | Drosophila melanogaster | Q95R35 | - |
- |
3.4.11.1 | Drosophila melanogaster | Q961W5 | - |
- |
3.4.11.1 | Drosophila melanogaster | Q9VSM6 | - |
- |
3.4.11.1 | Drosophila melanogaster | Q9VSM7 | - |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.4.11.1 | semen | - |
Drosophila melanogaster | - |
3.4.11.1 | testis | - |
Drosophila melanogaster | - |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.11.1 | ? | x * 55000, SDS-PAGE | Drosophila melanogaster |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.11.1 | leucylaminopeptidase | - |
Drosophila melanogaster |
3.4.11.1 | S-Lap1 | - |
Drosophila melanogaster |
3.4.11.1 | S-Lap2 | - |
Drosophila melanogaster |
3.4.11.1 | S-Lap3 | - |
Drosophila melanogaster |
3.4.11.1 | S-Lap4 | - |
Drosophila melanogaster |
3.4.11.1 | S-Lap5 | - |
Drosophila melanogaster |
3.4.11.1 | S-Lap6 | - |
Drosophila melanogaster |
3.4.11.1 | S-Lap7 | - |
Drosophila melanogaster |
3.4.11.1 | S-Lap8 | - |
Drosophila melanogaster |
3.4.11.1 | sperm-leucylaminopeptidase | - |
Drosophila melanogaster |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.11.1 | 7.4 | - |
assay at | Drosophila melanogaster |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.4.11.1 | malfunction | S-Lap1 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids | Drosophila melanogaster |
3.4.11.1 | malfunction | S-Lap2 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids | Drosophila melanogaster |
3.4.11.1 | malfunction | S-Lap3 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids | Drosophila melanogaster |
3.4.11.1 | malfunction | S-Lap4 gene mutant homozygotes are male semi-sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids | Drosophila melanogaster |
3.4.11.1 | malfunction | S-Lap5 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids | Drosophila melanogaster |
3.4.11.1 | malfunction | S-Lap6 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids | Drosophila melanogaster |
3.4.11.1 | malfunction | S-Lap7 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids | Drosophila melanogaster |
3.4.11.1 | malfunction | S-Lap8 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids | Drosophila melanogaster |
3.4.11.1 | physiological function | sperm-leucylaminopeptidases are required for male fertility as structural components of mitochondrial paracrystalline material in Drosophila melanogaster sperm | Drosophila melanogaster |