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P10761 (ZP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Processed zona pellucida sperm-binding protein 3
Gene names
Name:Zp3
Synonyms:Zp-3, Zpc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 sperm binding and zona matrix formation.

Subunit structure

Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers.

Subcellular location

Processed zona pellucida sperm-binding protein 3: Secretedextracellular spaceextracellular matrix. Note: The glycoproteinaceous translucent extracellular matrix that surrounds the mammalian oocyte is called zona pellucida. Ref.8

Cell membrane; Single-pass type I membrane protein Ref.8.

Tissue specificity

Oocytes.

Developmental stage

Expressed during the 2-week growth phase of oogenesis, prior to ovulation.

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.

O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy. Ref.7

Cys-320, Cys-322, Cys-323 and Cys-328 are involved in two additional disulfide bonds.

Sequence similarities

Belongs to the ZP domain family. ZPC subfamily.

Contains 1 ZP domain.

Ontologies

Keywords
   Cellular componentCell membrane
Extracellular matrix
Membrane
Secreted
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbinding of sperm to zona pellucida

Inferred from mutant phenotype PubMed 11417900. Source: UniProtKB

blastocyst formation

Inferred from mutant phenotype PubMed 20382503. Source: UniProtKB

egg coat formation

Inferred from mutant phenotype PubMed 14645511PubMed 18420282. Source: UniProtKB

humoral immune response mediated by circulating immunoglobulin

Inferred from direct assay PubMed 20382503. Source: UniProtKB

intracellular protein transport

Inferred from mutant phenotype PubMed 14645511PubMed 17047254. Source: UniProtKB

intracellular signal transduction

Inferred from direct assay PubMed 10793136. Source: UniProtKB

manganese ion transmembrane transport

Inferred from direct assay PubMed 10793136. Source: GOC

manganese ion transport

Inferred from direct assay PubMed 10793136. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18667753. Source: UniProtKB

oocyte development

Inferred from mutant phenotype PubMed 18420282. Source: UniProtKB

phosphatidylinositol-mediated signaling

Inferred from mutant phenotype PubMed 17258189. Source: UniProtKB

positive regulation of T cell proliferation

Inferred from direct assay PubMed 15579591. Source: UniProtKB

positive regulation of acrosomal vesicle exocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of acrosome reaction

Inferred from direct assay PubMed 10793136. Source: UniProtKB

positive regulation of antral ovarian follicle growth

Inferred from mutant phenotype PubMed 18420282PubMed 20382503. Source: UniProtKB

positive regulation of calcium ion import

Inferred from direct assay PubMed 10793136. Source: UniProtKB

positive regulation of humoral immune response

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of inflammatory response

Inferred from direct assay PubMed 18667753. Source: UniProtKB

positive regulation of interferon-gamma production

Inferred from direct assay PubMed 15579591. Source: UniProtKB

positive regulation of interleukin-4 production

Inferred from direct assay PubMed 15579591. Source: UniProtKB

positive regulation of leukocyte migration

Inferred from direct assay PubMed 18667753. Source: UniProtKB

positive regulation of ovarian follicle development

Inferred from direct assay PubMed 18667753. Source: UniProtKB

positive regulation of phosphatidylinositol biosynthetic process

Inferred from direct assay PubMed 17258189. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 17258189. Source: UniProtKB

positive regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18667753. Source: UniProtKB

positive regulation of type IV hypersensitivity

Inferred from direct assay PubMed 15579591. Source: UniProtKB

protein kinase C signaling

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 11906903PubMed 14645511. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 9609824. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 14645511PubMed 17047254. Source: UniProtKB

extracellular matrix

Inferred from direct assay PubMed 11906903Ref.8. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

multivesicular body

Inferred from direct assay PubMed 17047254. Source: UniProtKB

outer acrosomal membrane

Inferred from direct assay PubMed 11417900. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 14645511. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 11417900PubMed 14645511Ref.8. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

secretory granule

Inferred from direct assay PubMed 11906903. Source: UniProtKB

   Molecular_functioncarbohydrate binding

Inferred from sequence or structural similarity. Source: UniProtKB

manganese ion transmembrane transporter activity

Inferred from direct assay PubMed 10793136. Source: UniProtKB

signal transducer activity

Inferred from direct assay PubMed 10793136. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 351329Zona pellucida sperm-binding protein 3
PRO_0000041715
Chain23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304572
Propeptide352 – 42473Removed in mature form
PRO_0000041716

Regions

Topological domain23 – 387365Extracellular
Transmembrane388 – 40821Helical; Potential
Topological domain409 – 42416Cytoplasmic
Domain45 – 308264ZP

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid
Glycosylation321O-linked (GalNAc...) Probable
Glycosylation341O-linked (GalNAc...) Probable
Glycosylation391O-linked (GalNAc...) Probable
Glycosylation1461N-linked (GlcNAc...) Ref.7
Glycosylation1551O-linked (GalNAc...) Probable
Glycosylation1621O-linked (GalNAc...) Probable
Glycosylation2731N-linked (GlcNAc...) Ref.7
Glycosylation3041N-linked (GlcNAc...) Ref.7
Glycosylation3271N-linked (GlcNAc...) Ref.7
Glycosylation3301N-linked (GlcNAc...) Ref.7
Disulfide bond46 ↔ 139 Ref.8
Disulfide bond78 ↔ 98 Ref.8
Disulfide bond216 ↔ 283 Ref.8
Disulfide bond240 ↔ 301 Ref.8

Experimental info

Mutagenesis1111Y → C: Reduces protein solubility and causes formation of an abnormal disulfide bond between C-111 and C-139 in approximately half of the molecules. Ref.8
Mutagenesis1111Y → F: Causes a mild reduction of protein solubility. Ref.8
Mutagenesis1111Y → L or V: Strongly reduces protein solubility. Ref.8
Mutagenesis1111Y → S: Reduces protein solubility. Ref.8

Secondary structure

..................... 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10761 [UniParc].

Last modified November 1, 1997. Version 4.
Checksum: 9089903FBD268365

FASTA42446,304
        10         20         30         40         50         60 
MASSYFLFLC LLLCGGPELC NSQTLWLLPG GTPTPVGSSS PVKVECLEAE LVVTVSRDLF 

        70         80         90        100        110        120 
GTGKLVQPGD LTLGSEGCQP RVSVDTDVVR FNAQLHECSS RVQMTKDALV YSTFLLHDPR 

       130        140        150        160        170        180 
PVSGLSILRT NRVEVPIECR YPRQGNVSSH PIQPTWVPFR ATVSSEEKLA FSLRLMEENW 

       190        200        210        220        230        240 
NTEKSAPTFH LGEVAHLQAE VQTGSHLPLQ LFVDHCVATP SPLPDPNSSP YHFIVDFHGC 

       250        260        270        280        290        300 
LVDGLSESFS AFQVPRPRPE TLQFTVDVFH FANSSRNTLY ITCHLKVAPA NQIPDKLNKA 

       310        320        330        340        350        360 
CSFNKTSQSW LPVEGDADIC DCCSHGNCSN SSSSQFQIHG PRQWSKLVSR NRRHVTDEAD 

       370        380        390        400        410        420 
VTVGPLIFLG KANDQTVEGW TASAQTSVAL GLGLATVAFL TLAAIVLAVT RKCHSSSYLV 


SLPQ 

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of cDNA coding for ZP3, a sperm binding protein of the mouse zona pellucida."
Ringuette M.J., Chamberlin M.E., Baur A.W., Sobieski D.A., Dean J.
Dev. Biol. 127:287-295(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Dean J.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 387.
[3]"Nucleotide sequence of the gene encoding zona pellucida glycoprotein ZP3 -- the mouse sperm receptor."
Kinloch R.A., Wassarman P.M.
Nucleic Acids Res. 17:2861-2863(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CD-1.
Tissue: Liver.
[4]"Primary structure of the mouse sperm receptor polypeptide determined by genomic cloning."
Kinloch R.A., Roller R.J., Fimiani C.M., Wassarman D.A., Wassarman P.M.
Proc. Natl. Acad. Sci. U.S.A. 85:6409-6413(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Identification of a region of mouse zona pellucida glycoprotein mZP3 that possesses sperm receptor activity."
Rosiere T.K., Wassarman P.M.
Dev. Biol. 154:309-317(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 49-63; 197-204; 219-233 AND 261-275.
Strain: CD-1.
[7]"Structural characterization of native mouse zona pellucida proteins using mass spectrometry."
Boja E.S., Hoodbhoy T., Fales H.M., Dean J.
J. Biol. Chem. 278:34189-34202(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF C-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-23, DISULFIDE BOND FORMATION AT 78-CYS--CYS-98; 216-CYS--CYS-283 AND 240-CYS--CYS-301, GLYCOSYLATION AT ASN-146; ASN-273; ASN-304; ASN-327 AND ASN-330, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats."
Monne M., Han L., Schwend T., Burendahl S., Jovine L.
Nature 456:653-657(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 42-143, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF TYR-111, SUBCELLULAR LOCATION, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20026 mRNA. Translation: AAB18629.1.
X14376 Genomic DNA. Translation: CAA32550.1.
BC099465 mRNA. Translation: AAH99465.1.
BC100745 mRNA. Translation: AAI00746.1.
BC103583 mRNA. Translation: AAI03584.1.
BC103584 mRNA. Translation: AAI03585.1.
BC103585 mRNA. Translation: AAI03586.1.
PIRA30334.
RefSeqNP_035906.1. NM_011776.1.
UniGeneMm.1381.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3D4CX-ray2.90A42-143[»]
3D4GX-ray2.30A/B/C/D/E/F/G/H42-143[»]
3EF7X-ray3.10A/B42-143[»]
ProteinModelPortalP10761.
SMRP10761. Positions 40-331.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP10761.

Proteomic databases

PRIDEP10761.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005073; ENSMUSP00000005073; ENSMUSG00000004948.
GeneID22788.
KEGGmmu:22788.
UCSCuc008zzl.1. mouse.

Organism-specific databases

CTD7784.
MGIMGI:99215. Zp3.

Phylogenomic databases

eggNOGNOG43042.
GeneTreeENSGT00530000063482.
HOGENOMHOG000220813.
HOVERGENHBG007985.
InParanoidQ4FZI2.
OMALMEEDWG.
OrthoDBEOG773XG3.
PhylomeDBP10761.
TreeFamTF331369.

Gene expression databases

BgeeP10761.
CleanExMM_ZP3.
GenevestigatorP10761.

Family and domain databases

InterProIPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamPF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSPR00023. ZPELLUCIDA.
SMARTSM00241. ZP. 1 hit.
[Graphical view]
PROSITEPS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10761.
NextBio303371.
PROP10761.
SOURCESearch...

Entry information

Entry nameZP3_MOUSE
AccessionPrimary (citable) accession number: P10761
Secondary accession number(s): Q4FZI2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 118 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot