O54766 · ZP1_RAT

  • Protein
    Zona pellucida sperm-binding protein 1
  • Gene
    Zp1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the zona pellucida.

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 Componentcollagen-containing extracellular matrix
Cellular Componentegg coat
Cellular Componentextracellular region
Cellular Componentplasma membrane
Molecular Functionacrosin binding
Molecular Functionstructural constituent of egg coat
Biological Processbinding of sperm to zona pellucida
Biological Processprevention of polyspermy

Keywords

Names & Taxonomy

Protein names

Gene names

    • Name
      Zp1

Organism names

  • Taxonomic identifier
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    O54766

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Single-pass type I membrane protein

Processed zona pellucida sperm-binding protein 1

Zona pellucida

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain21-588Extracellular
Transmembrane589-609Helical
Topological domain610-617Cytoplasmic

Keywords

PTM/Processing

Features

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

Type
IDPosition(s)Description
Signal1-20
ChainPRO_000030455521-?Processed zona pellucida sperm-binding protein 1
Modified residue21Pyrrolidone carboxylic acid
ChainPRO_000004168121-544Zona pellucida sperm-binding protein 1
Glycosylation49N-linked (GlcNAc...) asparagine
Glycosylation68N-linked (GlcNAc...) asparagine
Disulfide bond226↔251
Disulfide bond235↔250
Disulfide bond245↔260
Glycosylation369N-linked (GlcNAc...) asparagine
Disulfide bond447↔468
PropeptidePRO_0000041682545-617Removed in mature form

Post-translational modification

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
O-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in oocytes.

Interaction

Subunit

Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers. Interacts with ZP3.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region179-198Disordered
Compositional bias180-194Pro residues
Domain224-264P-type
Domain269-540ZP

Domain

The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.

Sequence similarities

Belongs to the ZP domain family. ZPB subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    617
  • Mass (Da)
    67,853
  • Last updated
    1998-06-01 v1
  • Checksum
    AF52D9227F8A4CCC
MAWGCFVVLLLLVAAPLRLGQHLHLKPGFQYSYDCGVQGMQLLVFPRPNQTIQFKVLDEFGNRFEVNNCSICYHWVISEAQKPAVFSADYKGCHVLEKQDGRFHLRVFIQAVLPNGRVDTAQDVTLICPKPDHILTPESYLAPPTTPQPFIPHTFALHPISGHTLAGSGHTGLTTLYPETHPTPAPPSSEPGPVGPTVPQSQWGTLGSWELTELDSIGTHLLQERCQVASGHIPCMVKGSSEEACQQAGCCYDNTKEMPCYYGNTVTLQCFRSGYFTLVMSQETALTHGVMLDNVHLAYAPNGCPPTQKTSAFVVFHVPLTLCGTAIQVVGKQLVYENQLVSNIEVQTGPQGSITRDGVFRLHVRCIFNASDFLPIRASIFSPQPPAPVTRSGPLRLELRIATDKTFSSYYQGSDYPLVRLLQEPVYIEVRLLQRTDPGLALMLHQCWATPSASPFEQPQWPILSDGCPFKGDNYRTQMVAADRATLPFWSHYQRFTIATFTLLDSSSQNALRGQVYFFCSASACHPVGSETCSTTCDSEIARHRRSSGHHNSTIRALDIVSSPGAVGFEDAPKLEPSGSTRNSGSRPLLWVLQLLALTLVLGDGVLVGLSWAWAWA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
G3V8U5G3V8U5_RATZp1617

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias180-194Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB000928
EMBL· GenBank· DDBJ
BAA24486.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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