P48832 (ZP3_FELCA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 79.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Zona pellucida sperm-binding protein 3 Alternative name(s): Sperm receptor Zona pellucida glycoprotein 3 Short name=Zp-3 Zona pellucida protein C Cleaved into the following chain: | ||||
| Gene names |
| ||||
| Organism | Felis catus (Cat) (Felis silvestris catus) [Complete proteome] | ||||
| Taxonomic identifier | 9685 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis![]() |
Protein attributes
| Sequence length | 424 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | The mammalian zona pellucida, which mediates species-specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation. |
| Subunit structure | Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers By similarity. |
| Subcellular location | Processed zona pellucida sperm-binding protein 3: Secreted › extracellular space › extracellular matrix. |
| Tissue specificity | Oocytes. |
| Domain | The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida. |
| Post-translational modification | Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida. N-glycosylated By similarity. O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy By similarity. |
| Sequence similarities | Belongs to the ZP domain family. ZPC subfamily. Contains 1 ZP domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | By similarity | ||||||||
| Chain | 23 – 348 | 326 | Zona pellucida sperm-binding protein 3 | PRO_0000041707 | |||||||
| Chain | 23 – ? | Processed zona pellucida sperm-binding protein 3 | PRO_0000304568 | ||||||||
| Propeptide | 349 – 424 | 76 | Removed in mature form By similarity | PRO_0000041708 | |||||||
Regions | |||||||||||
| Topological domain | 23 – 383 | 361 | Extracellular Potential | ||||||||
| Transmembrane | 384 – 404 | 21 | Helical; Potential | ||||||||
| Topological domain | 405 – 424 | 20 | Cytoplasmic Potential | ||||||||
| Domain | 43 – 305 | 263 | ZP | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 52 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 123 | 1 | N-linked (GlcNAc...) By similarity | ||||||||
| Glycosylation | 145 | 1 | N-linked (GlcNAc...) By similarity | ||||||||
| Glycosylation | 154 | 1 | O-linked (GalNAc...) By similarity | ||||||||
| Glycosylation | 160 | 1 | O-linked (GalNAc...) By similarity | ||||||||
| Glycosylation | 161 | 1 | O-linked (GalNAc...) By similarity | ||||||||
| Disulfide bond | 44 ↔ 138 | By similarity | |||||||||
| Disulfide bond | 76 ↔ 97 | By similarity | |||||||||
| Disulfide bond | 215 ↔ 280 | By similarity | |||||||||
| Disulfide bond | 237 ↔ 298 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 72 | 1 | G → W in BAA08096. Ref.2 | ||||||||
| Sequence conflict | 264 | 1 | D → Y in BAA08096. Ref.2 | ||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning and characterization of zona pellucida genes and cDNAs from a variety of mammalian species: the ZPA, ZPB and ZPC gene families." Harris J.D., Hibler D.W., Fontenot G.K., Hsu K.T., Yurewicz E.C., Sacco A.G. DNA Seq. 4:361-393(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary. |
| [2] | Okazaki Y., Sugimoto M. Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary. |
Web resources
| Protein Spotlight Molecular chastity - Issue 93 of April 2008 |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U05778 mRNA. Translation: AAA74390.1. D45068 mRNA. Translation: BAA08096.1. |
| PIR | S70399. |
| RefSeq | NP_001009330.1. NM_001009330.2. |
3D structure databases | |
| ProteinModelPortal | P48832. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSFCAT00000013478; ENSFCAP00000012496; ENSFCAG00000013474. |
| GeneID | 493925. |
| KEGG | fca:493925. |
Organism-specific databases | |
| CTD | 7784. |
Phylogenomic databases | |
| HOVERGEN | HBG007985. |
Family and domain databases | |
| InterPro | IPR001507. ZP_dom. IPR017977. ZP_dom_CS. [Graphical view] |
| Pfam | PF00100. Zona_pellucida. 1 hit. [Graphical view] |
| PRINTS | PR00023. ZPELLUCIDA. |
| SMART | SM00241. ZP. 1 hit. [Graphical view] |
| PROSITE | PS00682. ZP_1. 1 hit. PS51034. ZP_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ZP3_FELCA | ||||||||
| Accession | Primary (citable) accession number: P48832 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Protein Spotlight Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries |

Clusters with
