Q05996 · ZP2_HUMAN

  • Protein
    Zona pellucida sperm-binding protein 2
  • Gene
    ZP2
  • 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 (PubMed:29895852).
The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor (PubMed:29895852).

Features

Showing features for site.

1745100200300400500600700
TypeIDPosition(s)Description
Site172-173Cleavage; by ASTL
Site640-641Cleavage

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 Componentendoplasmic reticulum
Cellular Componentextracellular region
Cellular Componentmultivesicular body
Cellular Componentplasma membrane
Molecular Functionacrosin binding
Molecular Functioncoreceptor activity
Molecular Functionidentical protein binding
Molecular Functionstructural constituent of egg coat
Biological Processbinding of sperm to zona pellucida
Biological Processprevention of polyspermy

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      ZP2
    • Synonyms
      ZPA

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q05996
  • Secondary accessions
    • B2R7J2
    • Q4VAN9
    • Q4VAP0
    • Q4VAP1

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Single-pass type I membrane protein

Processed zona pellucida sperm-binding protein 2

Zona pellucida

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain39-716Extracellular
Transmembrane717-736Helical
Topological domain737-745Cytoplasmic

Keywords

Disease & Variants

Involvement in disease

Oocyte/zygote/embryo maturation arrest 6 (OZEMA6)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An autosomal recessive infertility disorder characterized by oocyte fertilization failure, due to defective sperm-binding to an abnormally thin zona pellucida in patient oocytes.
  • See also
    MIM:618353

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_02470536in dbSNP:rs2075520

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,019 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

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

Type
IDPosition(s)Description
Signal1-38
ChainPRO_000030455939-?Processed zona pellucida sperm-binding protein 2
ChainPRO_000004168939-640Zona pellucida sperm-binding protein 2
Disulfide bond55↔138
Disulfide bond88↔106
Glycosylation105N-linked (GlcNAc...) asparagine
Glycosylation122N-linked (GlcNAc...) asparagine
Disulfide bond372↔465
Disulfide bond403↔424
Glycosylation462O-linked (GalNAc...) threonine
Disulfide bond545↔615
Disulfide bond566↔634
Disulfide bond620↔630
PropeptidePRO_0000041690641-745Removed in mature form

Post-translational modification

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
Proteolytically cleaved in the N-terminal part by the metalloendopeptidase ASTL exocytosed from cortical granules after fertilization, yielding a N-terminal peptide of about 30 kDa which remains covalently attached to the C-terminal peptide via disulfide bond(s). This cleavage may play an important role in the post-fertilization block to polyspermy. Additional proteolytically cleavage of the N-terminal peptide of 30 kDa occurs in one-cell and two-cell embryos.
N-glycosylated.
O-glycosylated; contains sulfate-substituted glycans.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in occytes(at protein level).

Gene expression databases

Organism-specific databases

Interaction

Subunit

Can form homopolymers that assemble into long fibers (in vitro). Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers (By similarity).
Interacts with ZP3 (PubMed:28886344).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY Q05996ACR P103234EBI-1755919, EBI-21280149
BINARY Q05996VDAC2 P45880-32EBI-1755919, EBI-11614013
BINARY Q05996ZP2 Q059966EBI-1755919, EBI-1755919

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain371-637ZP
Region469-491Disordered
Region673-708Disordered

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. ZPA subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q05996-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    745
  • Mass (Da)
    82,357
  • Last updated
    1994-02-01 v1
  • MD5 Checksum
    6013B57DE3AE0175ADF8916EBEC05A15
MACRQRGGSWSPSGWFNAGWSTYRSISLFFALVTSGNSIDVSQLVNPAFPGTVTCDEREITVEFPSSPGTKKWHASVVDPLGLDMPNCTYILDPEKLTLRATYDNCTRRVHGGHQMTIRVMNNSAALRHGAVMYQFFCPAMQVEETQGLSASTICQKDFMSFSLPRVFSGLADDSKGTKVQMGWSIEVGDGARAKTLTLPEAMKEGFSLLIDNHRMTFHVPFNATGVTHYVQGNSHLYMVSLKLTFISPGQKVIFSSQAICAPDPVTCNATHMTLTIPEFPGKLKSVSFENQNIDVSQLHDNGIDLEATNGMKLHFSKTLLKTKLSEKCLLHQFYLASLKLTFLLRPETVSMVIYPECLCESPVSIVTGELCTQDGFMDVEVYSYQTQPALDLGTLRVGNSSCQPVFEAQSQGLVRFHIPLNGCGTRYKFEDDKVVYENEIHALWTDFPPSKISRDSEFRMTVKCSYSRNDMLLNINVESLTPPVASVKLGPFTLILQSYPDNSYQQPYGENEYPLVRFLRQPIYMEVRVLNRDDPNIKLVLDDCWATSTMDPDSFPQWNVVVDGCAYDLDNYQTTFHPVGSSVTHPDHYQRFDMKAFAFVSEAHVLSSLVYFHCSALICNRLSPDSPLCSVTCPVSSRHRRATGATEAEKMTVSLPGPILLLSDDSSFRGVGSSDLKASGSSGEKSRSETGEEVGSRGAMDTKGHKTAGDVGSKAVAAVAAFAGVVATLGFIYYLYEKRTVSNH

Q05996-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_054508460-468in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M90366
EMBL· GenBank· DDBJ
AAA61335.1
EMBL· GenBank· DDBJ
mRNA
AK313003
EMBL· GenBank· DDBJ
BAG35839.1
EMBL· GenBank· DDBJ
mRNA
AF001550
EMBL· GenBank· DDBJ
AAB67599.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471228
EMBL· GenBank· DDBJ
EAW66859.1
EMBL· GenBank· DDBJ
Genomic DNA
BC096304
EMBL· GenBank· DDBJ
AAH96304.1
EMBL· GenBank· DDBJ
mRNA
BC096305
EMBL· GenBank· DDBJ
AAH96305.1
EMBL· GenBank· DDBJ
mRNA
BC096306
EMBL· GenBank· DDBJ
AAH96306.1
EMBL· GenBank· DDBJ
mRNA
BC096307
EMBL· GenBank· DDBJ
AAH96307.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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