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EC Tree
The enzyme appears in viruses and cellular organisms
Reaction Schemes
proteolytic degradation of proteins
Synonyms
fertilin, fertilin alpha, ph-30, adam1a, adam1, adam1b, adam-1, adam 1, fertilin alpha subunit, a disintegrin and metalloprotease 1,
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a disintegrin and metalloprotease 1
a disintegrin and metalloproteinase domain 1
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a disintegrin and metalloproteinase domain 1a
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a disintegrin and metalloproteinase domain 1b
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fertilin alpha 1a subunit
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fertilin alpha 1b subunit
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a disintegrin and metalloprotease 1
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a disintegrin and metalloprotease 1
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ADAM 1
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fertilin alpha
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fertilin alpha
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heterodimeric protein consisting of ADAM1 and ADAM2 located on the surface of sperm
M12.201
Merops-ID
PH-30
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proteolytic degradation of proteins
proteolytic degradation of proteins
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proteolytic degradation of proteins
mechanism
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proteolytic degradation of proteins
mechanism
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hydrolysis of peptide bond
hydrolysis of peptide bond
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hydrolysis of peptide bond
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hydrolysis of peptide bond
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hydrolysis of peptide bond
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hydrolysis of peptide bond
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additional information
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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potential roles of isozyme a and b in spermatogenesis and fertilization
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proteins + H2O
peptides
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additional information
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the enzyme mediates the cell-cell membrane fusion of egg and sperm
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additional information
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the enzyme mediates the cell-cell membrane fusion of egg and sperm
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additional information
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the enzyme mediates the cell-cell membrane fusion of egg and sperm
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additional information
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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potential roles of isozyme a and b in spermatogenesis and fertilization
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proteins + H2O
peptides
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additional information
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the enzyme mediates the cell-cell membrane fusion of egg and sperm
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additional information
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the enzyme mediates the cell-cell membrane fusion of egg and sperm
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additional information
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the enzyme mediates the cell-cell membrane fusion of egg and sperm
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Ca2+
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activates, required
Zn2+
metalloprotease domain in the beta subunit precursor region, but not in the mature protein, the alpha-subunit conatins a metalloprotease domain, which is the active site, in the mature from with the consensus sequence HEXXHXXGXXHE
additional information
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divalent cations are required for membrane fusion
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additional information
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binding to the egg is reduced by treatment with chymotrypsin
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Alzheimer Disease
Altered cell-matrix associated ADAM proteins in Alzheimer disease.
Herpes Zoster
Characterization of the binding of recombinant mouse sperm fertilin alpha subunit to mouse eggs: evidence for function as a cell adhesion molecule in sperm-egg binding.
Herpes Zoster
Characterization of the binding of recombinant mouse sperm fertilin beta subunit to mouse eggs: evidence for adhesive activity via an egg beta1 integrin-mediated interaction.
Herpes Zoster
Disruption of ADAM3 Impairs the Migration of Sperm into Oviduct in Mouse.
Herpes Zoster
Fertilization defects in sperm from mice lacking fertilin beta.
Herpes Zoster
Mechanisms of Fertilization--A View from the Perspective of Gene Manipulated Mice.
Herpes Zoster
Mice expressing aberrant sperm-specific protein PMIS2 produce normal-looking but fertilization-incompetent spermatozoa.
Herpes Zoster
Mouse Sperm Lacking ADAM1b/ADAM2 Fertilin Can Fuse with the Egg Plasma Membrane and Effect Fertilization.
Infertility
Initial evaluation of fertilin as an immunocontraceptive antigen and molecular cloning of the cynomolgus monkey fertilin beta subunit.
Infertility
Role of the integrin-associated protein CD9 in binding between sperm ADAM 2 and the egg integrin alpha6beta1: implications for murine fertilization.
Infertility
Sperm from the calmegin-deficient mouse have normal abilities for binding and fusion to the egg plasma membrane.
Infertility, Male
Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface.
Infertility, Male
The mechanism of sperm-egg interaction and the involvement of IZUMO1 in fusion.
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precursor
SwissProt
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SwissProt
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2 isozymes A and B
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precursor
SwissProt
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isozyme a
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additional information
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isozymes precursors form in each case a heterodimer with ADAM2
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epididymal, isozyme b
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2 isozymes
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high expression, proteolytic processing occurs mainly in the testis
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of germ cells, contains exclusively isozyme a
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on the cell surface
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cell surface fof epididymal sperm, contains exclusively isozyme b
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on the cell surface
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type I integral membrane glycoprotein, on the surface of sperm
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physiological function
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ADAM-1 forms a fertilin complex involved in key steps of the sperm-oocyte membrane interaction
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ADAM1_RAT
789
0
86140
Swiss-Prot
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Q60410_CAVPO
804
0
86903
TrEMBL
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ADM1A_MOUSE
791
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87490
Swiss-Prot
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ADM1B_MOUSE
806
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89369
Swiss-Prot
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10800
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estimated from SDS-PAGE band pattern
120000
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x * 48000, mature isozyme a, SDS-PAGE, x * 60000, mature isozyme b, SDS-PAGE, x * 100000, precursor of isozyme a, SDS-PAGE, x * 120000, precursor of isozyme b, SDS-PAGE
44000
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1 * 60000, alpha subunit, + 1 * 44000, beta subunit, SDS-PAGE
48000
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x * 48000, mature isozyme a, SDS-PAGE, x * 60000, mature isozyme b, SDS-PAGE, x * 100000, precursor of isozyme a, SDS-PAGE, x * 120000, precursor of isozyme b, SDS-PAGE
95000
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unprocessed expected mass of ADAM-1
100000
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gel filtration
100000
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x * 48000, mature isozyme a, SDS-PAGE, x * 60000, mature isozyme b, SDS-PAGE, x * 100000, precursor of isozyme a, SDS-PAGE, x * 120000, precursor of isozyme b, SDS-PAGE
60000
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1 * 60000, alpha subunit, + 1 * 44000, beta subunit, SDS-PAGE
60000
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x * 48000, mature isozyme a, SDS-PAGE, x * 60000, mature isozyme b, SDS-PAGE, x * 100000, precursor of isozyme a, SDS-PAGE, x * 120000, precursor of isozyme b, SDS-PAGE
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x * 48000, mature isozyme a, SDS-PAGE, x * 60000, mature isozyme b, SDS-PAGE, x * 100000, precursor of isozyme a, SDS-PAGE, x * 120000, precursor of isozyme b, SDS-PAGE
homodimer
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x * 50000-55000, SDS-PAGE
homotrimer
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3 * 3600, estimated from SDS-PAGE band pattern
dimer
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1 * 60000, alpha subunit, + 1 * 44000, beta subunit, SDS-PAGE
additional information
domain organization, the alpha subunit contains a putative fusion peptide, beta subunit contains a soluble disintegrin ligand
additional information
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the alpha subunit contains a putative fusion peptide, beta subunit contains a soluble disintegrin ligand
additional information
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the alpha subunit contains a putative fusion peptide, beta subunit contains a soluble disintegrin ligand
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glycoprotein
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N-glycosylation
glycoprotein
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N-glycosylation
proteolytic modification
processing of the subunit a and b precursors to mature proteins during sperm development
proteolytic modification
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processing of precursor to mature protein
proteolytic modification
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isozyme a is partially processed to a 48 kDa mature protein in round and elongating spermatids, isozyme b precursor is totally processed to a 63 kDa intermediate during spermatogenesis and finally to a 60 kDa mature protein during sperm transit in the epididymis
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additional information
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ADAM1a-deficient mice, capable of fertilizing cumulus-intact, zona pellucida-intact eggs in vitro
additional information
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ADAM1b deficient mice, no significant defect in sperm functions such as migration from the uterus into oviduct, binding to egg zona pellucida, and fusion with zona pellucida-free eggs, but severe reduction of ADAM2 on cell surface
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DNA and amino acid sequence determination, alpha and beta subunits
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expression of subunit alpha as fusion protein with maltose binding protein in Escherichia coli DH5alpha
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medicine
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crucial role of ADAM1b/ADAM2 fertilin not in the sperm/egg fusion, but in the appearance of these two ADAMs on the sperm surface
medicine
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loss of ADAM1a results in male infertility due to severely impaired ability of sperm to migrate from the uterus into the oviduct through the uterotubul junction
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Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Rattus norvegicus (P70505), Mus musculus (Q60813), Mus musculus (Q8R534)
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Kim, E.; Nishimura, H.; Baba, T.
Differential localization of ADAM1a and ADAM1b in the endoplasmic reticulum of testicular germ cells and on the surface of epididymal sperm
Biochem. Biophys. Res. Commun.
304
313-319
2003
Mus musculus
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Evans, J.P.; Schultz, R.M.; Kopf, G.S.
Characterization of the binding of recombinant mouse sperm fertilin alpha subunit to mouse eggs: evidence for function as a cell adhesion molecule in sperm-egg binding
Dev. Biol.
187
94-106
1997
Mus musculus
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Blobel, C.P.; Wolfsberg, T.G.; Turck, C.W.; Myles, D.G.; Primakoff, P.; White, J.M.
A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
Nature
356
248-252
1992
Homo sapiens
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Wolfsberg, T.G.; Bazan, J.F.; Blobel, C.P.; Myles, D.G.; Primakoff, P.; White, J.M.
The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications
Proc. Natl. Acad. Sci. USA
90
10783-10787
1993
Cavia porcellus (Q60410)
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Nishimura, H.; Kim, E.; Nakanishi, T.; Baba, T.
Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface
J. Biol. Chem.
279
34957-34962
2004
Mus musculus
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Kim, E.; Yamashita, M.; Nakanishi, T.; Park, K.E.; Kimura, M.; Kashiwabara, S.; Baba, T.
Mouse sperm lacking ADAM1b/ADAM2 fertilin can fuse with the egg plasma membrane and effect fertilization
J. Biol. Chem.
281
5634-5639
2006
Mus musculus
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Gan, S.W.; Xin, L.; Torres, J.
The transmembrane homotrimer of ADAM 1 in model lipid bilayers
Protein Sci.
16
285-292
2007
Cavia porcellus
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Fabrega, A.; Guyonnet, B.; Dacheux, J.L.; Gatti, J.L.; Puigmule, M.; Bonet, S.; Pinart, E.
Expression, immunolocalization and processing of fertilins ADAM-1 and ADAM-2 in the boar (Sus domesticus) spermatozoa during epididymal maturation
Reprod. Biol. Endocrinol.
9
96
2011
Sus scrofa
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