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P23491

- ZP3_MESAU

UniProt

P23491 - ZP3_MESAU

Protein

Zona pellucida sperm-binding protein 3

Gene

ZP3

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      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. 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 binding of sperm to zona pellucida Source: UniProtKB
    10. negative regulation of transcription, DNA-templated Source: UniProtKB
    11. oocyte development Source: UniProtKB
    12. phosphatidylinositol-mediated signaling Source: UniProtKB
    13. positive regulation of acrosomal vesicle exocytosis Source: UniProtKB
    14. positive regulation of acrosome reaction Source: UniProtKB
    15. positive regulation of antral ovarian follicle growth Source: UniProtKB
    16. positive regulation of calcium ion import Source: UniProtKB
    17. positive regulation of humoral immune response Source: UniProtKB
    18. positive regulation of inflammatory response Source: UniProtKB
    19. positive regulation of interferon-gamma production Source: UniProtKB
    20. positive regulation of interleukin-4 production Source: UniProtKB
    21. positive regulation of leukocyte migration Source: UniProtKB
    22. positive regulation of ovarian follicle development Source: UniProtKB
    23. positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
    24. positive regulation of protein kinase activity Source: UniProtKB
    25. positive regulation of protein kinase B signaling Source: UniProtKB
    26. positive regulation of T cell proliferation Source: UniProtKB
    27. positive regulation of transcription, DNA-templated Source: UniProtKB
    28. positive regulation of type IV hypersensitivity Source: UniProtKB
    29. protein kinase C signaling Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Fertilization

    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:ZPC
    OrganismiMesocricetus auratus (Golden hamster)
    Taxonomic identifieri10036 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

    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.

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222By similarityAdd
    BLAST
    Chaini23 – 349327Zona pellucida sperm-binding protein 3PRO_0000041713Add
    BLAST
    Chaini23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304571
    Propeptidei350 – 42273Removed in mature formBy similarityPRO_0000041714Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei23 – 231Pyrrolidone carboxylic acidBy similarity
    Glycosylationi32 – 321O-linked (GalNAc...)By similarity
    Glycosylationi34 – 341O-linked (GalNAc...)By similarity
    Disulfide bondi46 ↔ 139By similarity
    Disulfide bondi78 ↔ 98By similarity
    Glycosylationi146 – 1461N-linked (GlcNAc...)By similarity
    Glycosylationi155 – 1551O-linked (GalNAc...)By similarity
    Glycosylationi161 – 1611O-linked (GalNAc...)By similarity
    Glycosylationi162 – 1621O-linked (GalNAc...)By similarity
    Disulfide bondi216 ↔ 281By similarity
    Disulfide bondi238 ↔ 299By similarity
    Glycosylationi271 – 2711N-linked (GlcNAc...)By similarity
    Glycosylationi302 – 3021N-linked (GlcNAc...)By similarity

    Post-translational modificationi

    Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
    N-glycosylated.By similarity
    O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy.By similarity

    Keywords - PTMi

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

    Expressioni

    Tissue specificityi

    Oocytes.

    Developmental stagei

    Growing oocytes.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP23491.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 386364ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini408 – 42215CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei387 – 40721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 306262ZPPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi119 – 15840Pro-richAdd
    BLAST
    Compositional biasi208 – 25750Pro-richAdd
    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

    HOVERGENiHBG007985.

    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.

    P23491-1 [UniParc]FASTAAdd to Basket

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    MGLSYQLLLC LLLCGGAKQC CSQPLWLLPG GTPTPGKLTS SVEVECLEAE    50
    LVVTVSRDLF GTGKLIQPED LTLGSENCRP LVSVATDVVR FKAQLHECSN 100
    RVQVTEDALV YSTVLLHQPR PVPGLSILRT NRADVPIECR YPRQGNVSSH 150
    AIRPTWVPFS TTVSSEEKLV FSLRLMEENW NTEKLSPTSH LGEVAYLQAE 200
    VQTGSHLPLL LFVDRCVPTP SPDQTASPYH VIVDFHGCLV DGLSESFSAF 250
    QVPRPRPETL QFTVDVFHFA NSSRNTIYIT CHLKVTPANQ TPDELNKACS 300
    FNRSSKSWSP VEGDAEVCGC CSSGDCGSSS RSRYQAHGVS QWPKSASRRR 350
    RHVRDEADVT VGPLIFLGKA SDQAVEGWAS SAQTSLALGL GLAAVAFLTL 400
    AAIVLGVTRS CHTPSHVVSL SQ 422
    Length:422
    Mass (Da):45,827
    Last modified:February 1, 1996 - v2
    Checksum:iD0F95BE7FF8E7E01
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63629 mRNA. Translation: AAA37079.1.
    PIRiA60503.
    RefSeqiNP_001268531.1. NM_001281602.1.

    Genome annotation databases

    GeneIDi101824371.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Molecular chastity - Issue 93 of April 2008

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63629 mRNA. Translation: AAA37079.1 .
    PIRi A60503.
    RefSeqi NP_001268531.1. NM_001281602.1.

    3D structure databases

    ProteinModelPortali P23491.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 101824371.

    Organism-specific databases

    CTDi 7784.

    Phylogenomic databases

    HOVERGENi HBG007985.

    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. "Genomic organization and polypeptide primary structure of zona pellucida glycoprotein hZP3, the hamster sperm receptor."
      Kinloch R.A., Ruiz-Seller B., Wassarman P.M.
      Dev. Biol. 142:414-421(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.

    Entry informationi

    Entry nameiZP3_MESAU
    AccessioniPrimary (citable) accession number: P23491
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 76 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3