P53786 · ZP3_CALSQ
- ProteinZona pellucida sperm-binding protein 3
- GeneZP3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids424 (go to sequence)
- Protein existenceEvidence at transcript 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. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.
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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Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameZona pellucida sperm-binding protein 3
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Platyrrhini > Cebidae > Callitrichinae > Callithrix > Callithrix
Accessions
- Primary accessionP53786
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Processed zona pellucida sperm-binding protein 3
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-387 | Extracellular | ||||
Sequence: QPLRLLQGGTSHPETALQPVVVECQEATLVVTVSKDLFGTRKLIRAVDLTLGPEGCEPLVSTDTEDVVRFEVGLHECGNSMQVTDDALVYSTFLLHDPRPVGNLSIVRTNRAEIPIECRYPRRGNVSSQAILPTWLPFRTTVFSEEKLTFSLRLMEENWSTEKRTPTFHLGDVAHLQAEIHTGSHVPLRLFVDHCVATPTPDQNASPYHTIVDFHGCLVDGLTDASSAFQAPRPRPDTLQFTVDVFHFANDSRNMIYITCHLKVTLAEQDPDELNKACSFSKASNSWFPVEGPADICQCCSKGDCGTPSHARRQPHVVSLGSGSPARDRRHVTEEADVTVGPLIFLDRTGDHEMEQWALPADTSL | ||||||
Transmembrane | 388-408 | Helical | ||||
Sequence: LLLGTGLAVVALLTLTAVILV | ||||||
Topological domain | 409-424 | Cytoplasmic | ||||
Sequence: LTRRCRTASLPVSASE |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, modified residue, glycosylation, disulfide bond, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MELSYRLFICLLLWGSTELCYP | ||||||
Chain | PRO_0000304566 | 23-? | Processed zona pellucida sperm-binding protein 3 | |||
Sequence: MELSYRLFICLLLWGSTELCYP | ||||||
Modified residue | 23 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000041703 | 23-350 | Zona pellucida sperm-binding protein 3 | |||
Sequence: QPLRLLQGGTSHPETALQPVVVECQEATLVVTVSKDLFGTRKLIRAVDLTLGPEGCEPLVSTDTEDVVRFEVGLHECGNSMQVTDDALVYSTFLLHDPRPVGNLSIVRTNRAEIPIECRYPRRGNVSSQAILPTWLPFRTTVFSEEKLTFSLRLMEENWSTEKRTPTFHLGDVAHLQAEIHTGSHVPLRLFVDHCVATPTPDQNASPYHTIVDFHGCLVDGLTDASSAFQAPRPRPDTLQFTVDVFHFANDSRNMIYITCHLKVTLAEQDPDELNKACSFSKASNSWFPVEGPADICQCCSKGDCGTPSHARRQPHVVSLGSGSPARD | ||||||
Glycosylation | 32 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Disulfide bond | 46↔140 | |||||
Sequence: CQEATLVVTVSKDLFGTRKLIRAVDLTLGPEGCEPLVSTDTEDVVRFEVGLHECGNSMQVTDDALVYSTFLLHDPRPVGNLSIVRTNRAEIPIEC | ||||||
Disulfide bond | 78↔99 | |||||
Sequence: CEPLVSTDTEDVVRFEVGLHEC | ||||||
Glycosylation | 125 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 147 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 156 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 162 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 163 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 180 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 217↔282 | |||||
Sequence: CVATPTPDQNASPYHTIVDFHGCLVDGLTDASSAFQAPRPRPDTLQFTVDVFHFANDSRNMIYITC | ||||||
Disulfide bond | 239↔300 | |||||
Sequence: CLVDGLTDASSAFQAPRPRPDTLQFTVDVFHFANDSRNMIYITCHLKVTLAEQDPDELNKAC | ||||||
Glycosylation | 272 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Propeptide | PRO_0000041704 | 351-424 | Removed in mature form | |||
Sequence: RRHVTEEADVTVGPLIFLDRTGDHEMEQWALPADTSLLLLGTGLAVVALLTLTAVILVLTRRCRTASLPVSASE |
Post-translational modification
Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
N-glycosylated.
O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy.
Keywords
- PTM
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 ZP1 and ZP2.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 45-307 | ZP | ||||
Sequence: ECQEATLVVTVSKDLFGTRKLIRAVDLTLGPEGCEPLVSTDTEDVVRFEVGLHECGNSMQVTDDALVYSTFLLHDPRPVGNLSIVRTNRAEIPIECRYPRRGNVSSQAILPTWLPFRTTVFSEEKLTFSLRLMEENWSTEKRTPTFHLGDVAHLQAEIHTGSHVPLRLFVDHCVATPTPDQNASPYHTIVDFHGCLVDGLTDASSAFQAPRPRPDTLQFTVDVFHFANDSRNMIYITCHLKVTLAEQDPDELNKACSFSKASN |
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. ZPC subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length424
- Mass (Da)46,809
- Last updated1996-10-01 v1
- Checksum1DACBD03026C2739