Reviewed,
UniProtKB/Swiss-Prot P42098 (ZP3_PIG)
Last modified
November 24, 2009.
Version 65.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Zona pellucida sperm-binding protein 3 Alternative name(s): Zona pellucida protein 3-beta Zona pellucida glycoprotein ZP3-beta Zona pellucida protein C Sperm receptor Cleaved into the following chain: 1- Recommended name: Processed zona pellucida sperm-binding protein 3 | ||||
| Gene names |
| ||||
| Organism | Sus scrofa (Pig) | ||||
| Taxonomic identifier | 9823 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 421 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein 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 zona matrix formation. In pig, does not seem to have a sperm-binding activity by itself but may increase sperm-binding activity of ZPB. |
| 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. Ref.4 O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy By similarity. All cysteine residues are involved in disulfide bonds. |
| Sequence similarities | Belongs to the ZP domain family. ZPC subfamily. Contains 1 ZP domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fertilization |
| Cellular component | Cell membrane Extracellular matrix Membrane Secreted |
| Domain | Signal Transmembrane |
| Molecular function | Receptor |
| PTM | Cleavage on pair of basic residues Disulfide bond Glycoprotein Pyrrolidone carboxylic acid |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW proteinaceous extracellular matrixInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | receptor activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | |||||||||
| Chain | 23 – 332 | 310 | Zona pellucida sperm-binding protein 3 | PRO_0000041717 | |||||||
| Chain | 23 – ? | Processed zona pellucida sperm-binding protein 3 | PRO_0000304573 | ||||||||
| Propeptide | 333 – 421 | 89 | Removed in mature form | PRO_0000041718 | |||||||
Regions | |||||||||||
| Topological domain | 23 – 381 | 359 | Extracellular Potential | ||||||||
| Transmembrane | 382 – 402 | 21 | Potential | ||||||||
| Topological domain | 403 – 421 | 19 | Cytoplasmic Potential | ||||||||
| Domain | 44 – 306 | 263 | ZP | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 23 | 1 | Pyrrolidone carboxylic acid | ||||||||
| Glycosylation | 124 | 1 | N-linked (GlcNAc...) | CAR_000151 | |||||||
| Glycosylation | 146 | 1 | N-linked (GlcNAc...) | CAR_000152 | |||||||
| Glycosylation | 155 | 1 | O-linked (GalNAc...) | ||||||||
| Glycosylation | 161 | 1 | O-linked (GalNAc...) | ||||||||
| Glycosylation | 162 | 1 | O-linked (GalNAc...) | ||||||||
| Glycosylation | 179 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 271 | 1 | N-linked (GlcNAc...) | CAR_000153 | |||||||
| Disulfide bond | 45 ↔ 139 | By similarity | |||||||||
| Disulfide bond | 77 ↔ 98 | By similarity | |||||||||
| Disulfide bond | 216 ↔ 281 | By similarity | |||||||||
| Disulfide bond | 238 ↔ 299 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 101 | 1 | Missing in BAA08093. Ref.2 | ||||||||
| Sequence conflict | 107 | 1 | D → V in BAA08093. Ref.2 | ||||||||
| Sequence conflict | 163 – 164 | 2 | VF → GV in BAA08093. Ref.2 | ||||||||
| Sequence conflict | 404 | 1 | P → A in BAA08093. Ref.2 | ||||||||
Sequences
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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: 7841460] [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. |
| [3] | "Localization of epitopes for monoclonal antibodies at the N-terminus of the porcine zona pellucida glycoprotein pZPC." Gupta S.K., Yurewicz E.C., Afzalpurkar A., Rao K.V., Gage D.A., Wu H., Sacco A.G. Mol. Reprod. Dev. 42:220-225(1995) [PubMed: 8562067] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-23, MASS SPECTROMETRY. |
| [4] | "Identification of the carboxyl termini of porcine zona pellucida glycoproteins ZPB and ZPC." Yonezawa N., Nakano M. Biochem. Biophys. Res. Commun. 307:877-882(2003) [PubMed: 12878193] [Abstract] Cited for: PROTEOLYTIC PROCESSING. |
| [5] | "Porcine oocyte zona pellucida M(r) 55,000 glycoproteins: identification of O-glycosylated domains." Yurewicz E.C., Pack B.A., Sacco A.G. Mol. Reprod. Dev. 33:182-188(1992) [PubMed: 1418987] [Abstract] Cited for: GLYCOSYLATION. |
Cross-references
Sequence databases | |
|---|---|
| L22169 mRNA. Translation: AAA31145.1. D45065 mRNA. Translation: BAA08093.1. | |
| PIR | S70433. |
| RefSeq | NP_999058.1. |
| UniGene | Ssc.14525 |
3D structure databases | |
| ModBase | Search... |
PTM databases | |
| GlycoSuiteDB | P42098. |
Genome annotation databases | |
| Ensembl | ENSSSCT00000008432; ENSSSCP00000008213; ENSSSCG00000007691; Sus scrofa. [Genome view] |
| GeneID | 396927. |
| KEGG | ssc:396927. |
Organism-specific databases | |
| CTD | 396927. |
Phylogenomic databases | |
| HOVERGEN | P42098. |
Family and domain databases | |
| InterPro | IPR001507. Endoglin/CD105. IPR017977. Endoglin/CD105_CS. IPR017976. Endoglin/CD105_subgr. [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_PIG | ||||||||
| Accession | Primary (citable) accession number: P42098 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Protein Spotlight Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


