Q05996 · ZP2_HUMAN
- ProteinZona pellucida sperm-binding protein 2
- GeneZP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids745 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 172-173 | Cleavage; by ASTL | |||
Site | 640-641 | Cleavage | |||
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | egg coat | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular region | |
Cellular Component | multivesicular body | |
Cellular Component | plasma membrane | |
Molecular Function | acrosin binding | |
Molecular Function | coreceptor activity | |
Molecular Function | identical protein binding | |
Molecular Function | structural constituent of egg coat | |
Biological Process | binding of sperm to zona pellucida | |
Biological Process | prevention of polyspermy |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZona pellucida sperm-binding protein 2
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ05996
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Processed zona pellucida sperm-binding protein 2
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Topological domain | 39-716 | Extracellular | |||
Transmembrane | 717-736 | Helical | |||
Topological domain | 737-745 | Cytoplasmic | |||
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Oocyte/zygote/embryo maturation arrest 6 (OZEMA6)
- Note
- DescriptionAn autosomal recessive infertility disorder characterized by oocyte fertilization failure, due to defective sperm-binding to an abnormally thin zona pellucida in patient oocytes.
- See alsoMIM:618353
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Natural variant | VAR_024705 | 36 | in dbSNP:rs2075520 | ||
Variants
![](/variants.8e7f84.jpg)
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.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, propeptide.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-38 | ||||
Chain | PRO_0000304559 | 39-? | Processed zona pellucida sperm-binding protein 2 | ||
Chain | PRO_0000041689 | 39-640 | Zona pellucida sperm-binding protein 2 | ||
Disulfide bond | 55↔138 | ||||
Disulfide bond | 88↔106 | ||||
Glycosylation | 105 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 122 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 372↔465 | ||||
Disulfide bond | 403↔424 | ||||
Glycosylation | 462 | O-linked (GalNAc...) threonine | |||
Disulfide bond | 545↔615 | ||||
Disulfide bond | 566↔634 | ||||
Disulfide bond | 620↔630 | ||||
Propeptide | PRO_0000041690 | 641-745 | Removed 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
- PTM
Proteomic databases
PTM 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).
Interacts with ZP3 (PubMed:28886344).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | Q05996 | ACR P10323 | 4 | EBI-1755919, EBI-21280149 | |
BINARY | Q05996 | VDAC2 P45880-3 | 2 | EBI-1755919, EBI-11614013 | |
BINARY | Q05996 | ZP2 Q05996 | 6 | EBI-1755919, EBI-1755919 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 371-637 | ZP | |||
Region | 469-491 | Disordered | |||
Region | 673-708 | Disordered | |||
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe 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.
- Name1
- Length745
- Mass (Da)82,357
- Last updated1994-02-01 v1
- MD5 Checksum6013B57DE3AE0175ADF8916EBEC05A15
Q05996-2
- Name2
- Differences from canonical
- 460-468: Missing
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Alternative sequence | VSP_054508 | 460-468 | in isoform 2 | ||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |