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P10761

- ZP3_MOUSE

UniProt

P10761 - ZP3_MOUSE

Protein

Zona pellucida sperm-binding protein 3

Gene

Zp3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 4 (01 Nov 1997)
      Previous versions | rss
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    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

    1. carbohydrate binding Source: UniProtKB
    2. manganese ion transmembrane transporter activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. signal transducer activity Source: UniProtKB

    GO - Biological processi

    1. binding of sperm to zona pellucida Source: UniProtKB
    2. blastocyst formation Source: UniProtKB
    3. egg coat formation Source: UniProtKB
    4. humoral immune response mediated by circulating immunoglobulin Source: UniProtKB
    5. intracellular protein transport Source: UniProtKB
    6. intracellular signal transduction Source: UniProtKB
    7. manganese ion transmembrane transport Source: GOC
    8. manganese ion transport Source: UniProtKB
    9. negative regulation of transcription, DNA-templated Source: UniProtKB
    10. oocyte development Source: UniProtKB
    11. phosphatidylinositol-mediated signaling Source: UniProtKB
    12. positive regulation of acrosomal vesicle exocytosis Source: UniProtKB
    13. positive regulation of acrosome reaction Source: UniProtKB
    14. positive regulation of antral ovarian follicle growth Source: UniProtKB
    15. positive regulation of calcium ion import Source: UniProtKB
    16. positive regulation of humoral immune response Source: UniProtKB
    17. positive regulation of inflammatory response Source: UniProtKB
    18. positive regulation of interferon-gamma production Source: UniProtKB
    19. positive regulation of interleukin-4 production Source: UniProtKB
    20. positive regulation of leukocyte migration Source: UniProtKB
    21. positive regulation of ovarian follicle development Source: UniProtKB
    22. positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
    23. positive regulation of protein kinase activity Source: UniProtKB
    24. positive regulation of protein kinase B signaling Source: UniProtKB
    25. positive regulation of T cell proliferation Source: UniProtKB
    26. positive regulation of transcription, DNA-templated Source: UniProtKB
    27. positive regulation of type IV hypersensitivity Source: UniProtKB
    28. protein kinase C signaling Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_199072. 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: Chromosome 5

    Organism-specific databases

    MGIiMGI:99215. Zp3.

    Subcellular locationi

    Chain 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.
    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB
    3. extracellular matrix Source: UniProtKB
    4. extracellular space Source: UniProtKB
    5. Golgi apparatus Source: UniProtKB
    6. integral component of membrane Source: UniProtKB-KW
    7. multivesicular body Source: UniProtKB
    8. outer acrosomal membrane Source: UniProtKB
    9. perinuclear region of cytoplasm Source: UniProtKB
    10. plasma membrane Source: UniProtKB
    11. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    12. secretory granule Source: UniProtKB

    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 ↔ 139
    Disulfide bondi78 ↔ 98
    Glycosylationi146 – 1461N-linked (GlcNAc...)1 Publication
    Glycosylationi155 – 1551O-linked (GalNAc...)Curated
    Glycosylationi162 – 1621O-linked (GalNAc...)Curated
    Disulfide bondi216 ↔ 283
    Disulfide bondi240 ↔ 301
    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.
    GenevestigatoriP10761.

    Interactioni

    Subunit structurei

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

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei388 – 40821HelicalSequence AnalysisAdd
    BLAST

    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.
    InParanoidiQ4FZI2.
    OMAiLMEEDWG.
    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

    MASSYFLFLC LLLCGGPELC NSQTLWLLPG GTPTPVGSSS PVKVECLEAE    50
    LVVTVSRDLF GTGKLVQPGD LTLGSEGCQP RVSVDTDVVR FNAQLHECSS 100
    RVQMTKDALV YSTFLLHDPR PVSGLSILRT NRVEVPIECR YPRQGNVSSH 150
    PIQPTWVPFR ATVSSEEKLA FSLRLMEENW NTEKSAPTFH LGEVAHLQAE 200
    VQTGSHLPLQ LFVDHCVATP SPLPDPNSSP YHFIVDFHGC LVDGLSESFS 250
    AFQVPRPRPE TLQFTVDVFH FANSSRNTLY ITCHLKVAPA NQIPDKLNKA 300
    CSFNKTSQSW LPVEGDADIC DCCSHGNCSN SSSSQFQIHG PRQWSKLVSR 350
    NRRHVTDEAD VTVGPLIFLG KANDQTVEGW TASAQTSVAL GLGLATVAFL 400
    TLAAIVLAVT RKCHSSSYLV SLPQ 424
    Length:424
    Mass (Da):46,304
    Last modified:November 1, 1997 - v4
    Checksum:i9089903FBD268365
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS19749.1.
    PIRi A30334.
    RefSeqi NP_035906.1. NM_011776.1.
    UniGenei Mm.1381.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3D4C X-ray 2.90 A 42-143 [» ]
    3D4G X-ray 2.30 A/B/C/D/E/F/G/H 42-143 [» ]
    3EF7 X-ray 3.10 A/B 42-143 [» ]
    ProteinModelPortali P10761.
    SMRi P10761. Positions 42-143.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P10761.

    Proteomic databases

    PRIDEi P10761.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005073 ; ENSMUSP00000005073 ; ENSMUSG00000004948 .
    GeneIDi 22788.
    KEGGi mmu:22788.
    UCSCi uc008zzl.1. mouse.

    Organism-specific databases

    CTDi 7784.
    MGIi MGI:99215. Zp3.

    Phylogenomic databases

    eggNOGi NOG43042.
    GeneTreei ENSGT00530000063482.
    HOGENOMi HOG000220813.
    HOVERGENi HBG007985.
    InParanoidi Q4FZI2.
    OMAi LMEEDWG.
    OrthoDBi EOG773XG3.
    PhylomeDBi P10761.
    TreeFami TF331369.

    Enzyme and pathway databases

    Reactomei REACT_199072. Interaction With The Zona Pellucida.

    Miscellaneous databases

    EvolutionaryTracei P10761.
    NextBioi 303371.
    PROi P10761.
    SOURCEi Search...

    Gene expression databases

    Bgeei P10761.
    CleanExi MM_ZP3.
    Genevestigatori P10761.

    Family and domain databases

    InterProi IPR001507. ZP_dom.
    IPR017977. ZP_dom_CS.
    [Graphical view ]
    Pfami PF00100. Zona_pellucida. 1 hit.
    [Graphical view ]
    PRINTSi PR00023. ZPELLUCIDA.
    SMARTi SM00241. ZP. 1 hit.
    [Graphical view ]
    PROSITEi PS00682. ZP_1. 1 hit.
    PS51034. ZP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 122 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