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Protein

Zona pellucida sperm-binding protein 3

Gene

Zp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • acrosin binding Source: MGI
  • carbohydrate binding Source: UniProtKB
  • manganese ion transmembrane transporter activity Source: UniProtKB
  • signal transducer activity Source: UniProtKB
  • store-operated calcium channel activity Source: MGI

GO - Biological processi

  • binding of sperm to zona pellucida Source: UniProtKB
  • blastocyst formation Source: UniProtKB
  • calcium ion transmembrane transport Source: MGI
  • egg coat formation Source: UniProtKB
  • humoral immune response mediated by circulating immunoglobulin Source: UniProtKB
  • intracellular protein transport Source: UniProtKB
  • intracellular signal transduction Source: UniProtKB
  • manganese ion transmembrane transport Source: GOC
  • manganese ion transport Source: UniProtKB
  • negative regulation of binding of sperm to zona pellucida Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • oocyte development Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: UniProtKB
  • positive regulation of acrosomal vesicle exocytosis Source: UniProtKB
  • positive regulation of acrosome reaction Source: UniProtKB
  • positive regulation of antral ovarian follicle growth Source: UniProtKB
  • positive regulation of calcium ion import Source: UniProtKB
  • positive regulation of humoral immune response Source: UniProtKB
  • positive regulation of inflammatory response Source: UniProtKB
  • positive regulation of interferon-gamma production Source: UniProtKB
  • positive regulation of interleukin-4 production Source: UniProtKB
  • positive regulation of leukocyte migration Source: UniProtKB
  • positive regulation of ovarian follicle development Source: UniProtKB
  • positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • positive regulation of T cell proliferation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of type IV hypersensitivity Source: UniProtKB
  • protein kinase C signaling Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiREACT_301180. Interaction With The Zona Pellucida.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Zp3
Synonyms:Zp-3, Zpc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:99215. Zp3.

Subcellular locationi

Processed zona pellucida sperm-binding protein 3 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 387365ExtracellularAdd
BLAST
Transmembranei388 – 40821HelicalSequence AnalysisAdd
BLAST
Topological domaini409 – 42416CytoplasmicAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • multivesicular body Source: UniProtKB
  • outer acrosomal membrane Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
  • secretory granule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi111 – 1111Y → C: Reduces protein solubility and causes formation of an abnormal disulfide bond between C-111 and C-139 in approximately half of the molecules. 1 Publication
Mutagenesisi111 – 1111Y → F: Causes a mild reduction of protein solubility. 1 Publication
Mutagenesisi111 – 1111Y → L or V: Strongly reduces protein solubility. 1 Publication
Mutagenesisi111 – 1111Y → S: Reduces protein solubility. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 351329Zona pellucida sperm-binding protein 3PRO_0000041715Add
BLAST
Chaini23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304572
Propeptidei352 – 42473Removed in mature form1 PublicationPRO_0000041716Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Pyrrolidone carboxylic acid1 Publication
Glycosylationi32 – 321O-linked (GalNAc...)Curated
Glycosylationi34 – 341O-linked (GalNAc...)Curated
Glycosylationi39 – 391O-linked (GalNAc...)Curated
Disulfide bondi46 ↔ 1391 Publication
Disulfide bondi78 ↔ 981 Publication
Glycosylationi146 – 1461N-linked (GlcNAc...)1 Publication
Glycosylationi155 – 1551O-linked (GalNAc...)Curated
Glycosylationi162 – 1621O-linked (GalNAc...)Curated
Disulfide bondi216 ↔ 2831 Publication
Disulfide bondi240 ↔ 3011 Publication
Glycosylationi273 – 2731N-linked (GlcNAc...)1 Publication
Glycosylationi304 – 3041N-linked (GlcNAc...)1 Publication
Glycosylationi327 – 3271N-linked (GlcNAc...)1 Publication
Glycosylationi330 – 3301N-linked (GlcNAc...)1 Publication

Post-translational modificationi

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

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiP10761.

PTM databases

PhosphoSiteiP10761.

Expressioni

Tissue specificityi

Oocytes.

Developmental stagei

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

Gene expression databases

BgeeiP10761.
CleanExiMM_ZP3.
GenevisibleiP10761. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000005073.

Structurei

Secondary structure

1
424
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 465Combined sources
Beta strandi48 – 5811Combined sources
Beta strandi60 – 634Combined sources
Helixi68 – 703Combined sources
Beta strandi71 – 755Combined sources
Beta strandi81 – 844Combined sources
Beta strandi86 – 949Combined sources
Helixi95 – 984Combined sources
Beta strandi100 – 1045Combined sources
Beta strandi106 – 11712Combined sources
Beta strandi133 – 14210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D4CX-ray2.90A42-143[»]
3D4GX-ray2.30A/B/C/D/E/F/G/H42-143[»]
3EF7X-ray3.10A/B42-143[»]
ProteinModelPortaliP10761.
SMRiP10761. Positions 42-143.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10761.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 308264ZPPROSITE-ProRule annotationAdd
BLAST

Domaini

The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.

Sequence similaritiesi

Belongs to the ZP domain family. ZPC subfamily.Curated
Contains 1 ZP domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43042.
GeneTreeiENSGT00530000063482.
HOGENOMiHOG000220813.
HOVERGENiHBG007985.
InParanoidiP10761.
OMAiNRRHVTE.
OrthoDBiEOG773XG3.
PhylomeDBiP10761.
TreeFamiTF331369.

Family and domain databases

InterProiIPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00023. ZPELLUCIDA.
SMARTiSM00241. ZP. 1 hit.
[Graphical view]
PROSITEiPS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10761-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSYFLFLC LLLCGGPELC NSQTLWLLPG GTPTPVGSSS PVKVECLEAE
60 70 80 90 100
LVVTVSRDLF GTGKLVQPGD LTLGSEGCQP RVSVDTDVVR FNAQLHECSS
110 120 130 140 150
RVQMTKDALV YSTFLLHDPR PVSGLSILRT NRVEVPIECR YPRQGNVSSH
160 170 180 190 200
PIQPTWVPFR ATVSSEEKLA FSLRLMEENW NTEKSAPTFH LGEVAHLQAE
210 220 230 240 250
VQTGSHLPLQ LFVDHCVATP SPLPDPNSSP YHFIVDFHGC LVDGLSESFS
260 270 280 290 300
AFQVPRPRPE TLQFTVDVFH FANSSRNTLY ITCHLKVAPA NQIPDKLNKA
310 320 330 340 350
CSFNKTSQSW LPVEGDADIC DCCSHGNCSN SSSSQFQIHG PRQWSKLVSR
360 370 380 390 400
NRRHVTDEAD VTVGPLIFLG KANDQTVEGW TASAQTSVAL GLGLATVAFL
410 420
TLAAIVLAVT RKCHSSSYLV SLPQ
Length:424
Mass (Da):46,304
Last modified:November 1, 1997 - v4
Checksum:i9089903FBD268365
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19749.1.
PIRiA30334.
RefSeqiNP_035906.1. NM_011776.1.
UniGeneiMm.1381.

Genome annotation databases

EnsembliENSMUST00000005073; ENSMUSP00000005073; ENSMUSG00000004948.
GeneIDi22788.
KEGGimmu:22788.
UCSCiuc008zzl.1. mouse.

Cross-referencesi

Web resourcesi

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19749.1.
PIRiA30334.
RefSeqiNP_035906.1. NM_011776.1.
UniGeneiMm.1381.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D4CX-ray2.90A42-143[»]
3D4GX-ray2.30A/B/C/D/E/F/G/H42-143[»]
3EF7X-ray3.10A/B42-143[»]
ProteinModelPortaliP10761.
SMRiP10761. Positions 42-143.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000005073.

PTM databases

PhosphoSiteiP10761.

Proteomic databases

PRIDEiP10761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005073; ENSMUSP00000005073; ENSMUSG00000004948.
GeneIDi22788.
KEGGimmu:22788.
UCSCiuc008zzl.1. mouse.

Organism-specific databases

CTDi7784.
MGIiMGI:99215. Zp3.

Phylogenomic databases

eggNOGiNOG43042.
GeneTreeiENSGT00530000063482.
HOGENOMiHOG000220813.
HOVERGENiHBG007985.
InParanoidiP10761.
OMAiNRRHVTE.
OrthoDBiEOG773XG3.
PhylomeDBiP10761.
TreeFamiTF331369.

Enzyme and pathway databases

ReactomeiREACT_301180. Interaction With The Zona Pellucida.

Miscellaneous databases

EvolutionaryTraceiP10761.
NextBioi303371.
PROiP10761.
SOURCEiSearch...

Gene expression databases

BgeeiP10761.
CleanExiMM_ZP3.
GenevisibleiP10761. MM.

Family and domain databases

InterProiIPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00023. ZPELLUCIDA.
SMARTiSM00241. ZP. 1 hit.
[Graphical view]
PROSITEiPS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiZP3_MOUSE
AccessioniPrimary (citable) accession number: P10761
Secondary accession number(s): Q4FZI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: July 22, 2015
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.