Q60411 · ADAM2_CAVPO

  • Protein
    Disintegrin and metalloproteinase domain-containing protein 2
  • Gene
    ADAM2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Molecular Functionmetalloendopeptidase activity
Biological Processbinding of sperm to zona pellucida
Biological Processcell adhesion
Biological Processmale gonad development
Biological Processproteolysis

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Disintegrin and metalloproteinase domain-containing protein 2
  • Short names
    ADAM 2
  • Alternative names
    • Fertilin subunit beta
    • PH-30 (PH30)
    • PH30-beta

Gene names

    • Name
      ADAM2
    • Synonyms
      FTNB

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Hystricomorpha > Caviidae > Cavia

Accessions

  • Primary accession
    Q60411

Proteomes

Subcellular Location

Membrane ; Single-pass type I membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain16-680Extracellular
Transmembrane681-701Helical
Topological domain702-735Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, glycosylation, chain, disulfide bond, modified residue.

TypeIDPosition(s)Description
Signal1-15
PropeptidePRO_000002904016-176
Glycosylation55N-linked (GlcNAc...) asparagine
ChainPRO_0000029041177-735Disintegrin and metalloproteinase domain-containing protein 2
Glycosylation220N-linked (GlcNAc...) asparagine
Disulfide bond287↔370
Glycosylation288N-linked (GlcNAc...) asparagine
Disulfide bond329↔354
Disulfide bond331↔336
Glycosylation353N-linked (GlcNAc...) asparagine
Disulfide bond442↔455
Glycosylation456N-linked (GlcNAc...) asparagine
Glycosylation564N-linked (GlcNAc...) asparagine
Disulfide bond614↔625
Disulfide bond619↔631
Disulfide bond633↔642
Modified residue723Phosphoserine

Post-translational modification

The signal and the metalloprotease domain are cleaved during the epididymal maturation of the spermatozoa.

Keywords

PTM databases

Expression

Tissue specificity

Expressed specifically in testis.

Developmental stage

Expression begins during meiotic prophase.

Interaction

Subunit

Heterodimer with ADAM1/fertilin subunit alpha.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain178-375Peptidase M12B
Domain384-470Disintegrin
Domain610-643EGF-like
Region716-735Disordered

Domain

A tripeptide motif (TDE) within disintegrin-like domain could be involved in the binding to egg integrin receptor and thus could mediate sperm/egg binding.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    735
  • Mass (Da)
    81,905
  • Last updated
    1996-11-01 v1
  • Checksum
    7535FC39F44FB645
MLCLLLLLCGLASLGGPLKKYVENSGMQITVPEKIRSVKRGSVESEVSYKIVIENTTYIVNLVRKMFLPHDFQVYSYDSAGIMKPFEDYSQNFCYYQGHIEGFPTSLASISTCAGLRGLLQFETVSYGIEPLKSSIGFEHVIYPVKHDNEKSQYLKKSINVKNVVYKIKSIKSSVRTHYIEMHIIVEKNLYKHMGGNTATVTEKIFQLVGLMNAFFSTLNLTVILASLELWIDENKIPTTGDVNELLHAFQKWKKSYLVLRPHDVAFLLVYRESPSYIGAIFQGMICNTSYGGGIALHSKTITLDSFGVILVQLLSVSMGIAYDNADLCRCRGAICLMSPEAVFSSGMKMFSNCSVKAFKLFTSSQVSQCLQNQPYLEPVYRSNPVCGNNRVEQGEDCDCGSQEECQDTCCDAATCRLKSTSRCAQGPCCNQCEFKTKGEVCRESTDECDLPEYCNGSSGACQEDLYVINGHRCANEEWICMNGRCLSGKAQVQETFGTEMEMGSVDCFEQLNTKNDITGNCGILSPGNYKACGASNWKCGKLICSYDKSEILRNKEGMTIYANISGHICVSIEYPPGHAKSALMWVRDGTVCGPSEVCRQQQCVSSSYLGYDCTPATCSDHGVCNNKRHCHCNPTYVPPNCETQDSTKPGGSVDSGNLRYEPIPETYFVEGAYHTKSRKWPFFLIIPFFVIFSVLVATVVKVYYQKKKWKTEDYANDENIESESEPKSSKVSSK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z11720
EMBL· GenBank· DDBJ
CAA77784.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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