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Reviewed, UniProtKB/Swiss-Prot P10761 (ZP3_MOUSE)

Last modified January 19, 2010. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Zona pellucida sperm-binding protein 3
Alternative name(s):
    Zona pellucida glycoprotein ZP3
    Zona pellucida protein C
    Sperm receptor
Cleaved into the following chain:
    1- Recommended name:
            Processed zona pellucida sperm-binding protein 3
Gene names
Name: Zp3
Synonyms: Zp-3, Zpc
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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 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.

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 – 40821 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
P10761-1 [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: 3378665] [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: 2541416] [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: 2842770] [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: 15489334] [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: 1330788] [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: 12799386] [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, 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: 19052627] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 42-143, 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.
IPIIPI00114128.
PIRA30334.
RefSeqNP_035906.1.
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[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP10761.

Proteomic databases

PRIDEP10761.

Genome annotation databases

EnsemblENSMUST00000005073; ENSMUSP00000005073; ENSMUSG00000004948; Mus musculus. [Genome view]
GeneID22788.
KEGGmmu:22788.
UCSCuc008zzl.1. mouse.

Organism-specific databases

CTD22788.
MGIMGI:99215. Zp3.

Phylogenomic databases

eggNOGroNOG17165.
HOGENOMHBG444650.
HOVERGENP10761.
InParanoidP10761.
OMATNRAEVP.
OrthoDBEOG9N8TR9.
PhylomeDBP10761.

Gene expression databases

ArrayExpressP10761.
BgeeP10761.
CleanExMM_ZP3.
GenevestigatorP10761.
GermOnlineENSMUSG00000004948. Mus musculus.

Family and domain databases

InterProIPR001507. Endoglin/CD105.
IPR017977. Endoglin/CD105_CS.
IPR017976. Endoglin/CD105_subgr.
[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 Resources

NextBio303371.
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: January 19, 2010
This is version 88 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents