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P97708

- ZP3_RAT

UniProt

P97708 - ZP3_RAT

Protein

Zona pellucida sperm-binding protein 3

Gene

Zp3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (01 Jun 1998)
      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):
    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620606. 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.

    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 – 351329Zona pellucida sperm-binding protein 3PRO_0000041721Add
    BLAST
    Chaini23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304575
    Propeptidei352 – 42473Removed in mature form1 PublicationPRO_0000041722Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei23 – 231Pyrrolidone carboxylic acid1 Publication
    Glycosylationi32 – 321O-linked (GalNAc...)By similarity
    Glycosylationi34 – 341O-linked (GalNAc...)By similarity
    Glycosylationi39 – 391O-linked (GalNAc...)By similarity
    Disulfide bondi46 ↔ 139By similarity
    Disulfide bondi78 ↔ 981 Publication
    Glycosylationi146 – 1461N-linked (GlcNAc...)2 Publications
    Glycosylationi155 – 1551O-linked (GalNAc...)By similarity
    Glycosylationi162 – 1621O-linked (GalNAc...)By similarity
    Disulfide bondi216 ↔ 2831 Publication
    Disulfide bondi240 ↔ 3011 Publication
    Glycosylationi273 – 2731N-linked (GlcNAc...)2 Publications
    Glycosylationi304 – 3041N-linked (GlcNAc...)2 Publications
    Glycosylationi327 – 3271N-linked (GlcNAc...)By similarity
    Glycosylationi330 – 3301N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
    N-glycosylated; N-linked glycans are of high mannose/hybrid type, as well as bi-, tri- and tetra-antennary complex types.
    O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy.

    Keywords - PTMi

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

    Proteomic databases

    PRIDEiP97708.

    Expressioni

    Tissue specificityi

    Oocytes.

    Gene expression databases

    GenevestigatoriP97708.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP97708.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 387365ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini409 – 42416CytoplasmicSequence AnalysisAdd
    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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi329 – 3346Poly-Ser

    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.
    HOGENOMiHOG000220813.
    HOVERGENiHBG007985.
    InParanoidiP97708.
    PhylomeDBiP97708.

    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.

    P97708-1 [UniParc]FASTAAdd to Basket

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    MGPSCLLFLC LLLCGGPELC YPQTQWLLPG GTPTPAGSSS PVEVECKEAE    50
    LVVTVRRDLF GTGKLVQPGD LTLGSEGCQP LVAVDTDVVR LNAQLHECSS 100
    GVQVTEDALV YNTFLLHDPR PVNGLSILRT NRVEVPIECR YPRQGNVSSH 150
    PIQPTWVPFS ATVSSEEKLA FSLRLMEEDW NTEKSSPTFH LGEVAHLQAE 200
    VQTGSHLPLQ LFVDHCVATP SPLPGQNSSP HHFIVDSHGC LVDGLSESFS 250
    AFQVPRPRPE TLQFTVDVFH FANSSRNTVY ITCHLKVAPA NQIPDKLNKA 300
    CSFNKTSQSW LPVEGDADIC DCCSNGNCSN SSSSEFETHE PAQWSTLVSR 350
    NRRHVTDEAD VTVGPLIFLG KANDQAVEGW TSSAQTSVAL GLGLATVAFL 400
    TLAAIVLGVT RKCHTSSYLV SLPQ 424
    Length:424
    Mass (Da):45,901
    Last modified:June 1, 1998 - v2
    Checksum:i2AB42CBB14DE8701
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551V → A in BAA24456. (PubMed:9820205)Curated
    Sequence conflicti112 – 1121N → S in BAA24456. (PubMed:9820205)Curated
    Sequence conflicti412 – 4121K → M in BAA24456. (PubMed:9820205)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10823 mRNA. Translation: CAA71787.1.
    D78482 mRNA. Translation: BAA24456.1.
    RefSeqiNP_446214.1. NM_053762.1.
    UniGeneiRn.10892.

    Genome annotation databases

    GeneIDi114639.
    KEGGirno:114639.
    UCSCiRGD:620606. rat.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Molecular chastity - Issue 93 of April 2008

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10823 mRNA. Translation: CAA71787.1 .
    D78482 mRNA. Translation: BAA24456.1 .
    RefSeqi NP_446214.1. NM_053762.1.
    UniGenei Rn.10892.

    3D structure databases

    ProteinModelPortali P97708.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P97708.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 114639.
    KEGGi rno:114639.
    UCSCi RGD:620606. rat.

    Organism-specific databases

    CTDi 7784.
    RGDi 620606. Zp3.

    Phylogenomic databases

    eggNOGi NOG43042.
    HOGENOMi HOG000220813.
    HOVERGENi HBG007985.
    InParanoidi P97708.
    PhylomeDBi P97708.

    Miscellaneous databases

    NextBioi 618829.
    PROi P97708.

    Gene expression databases

    Genevestigatori P97708.

    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 characterisation of zona pellucida protein 3 (ZP3) in the rat."
      MacDuff P.E., Kerr L.E., Aitken R.J.
      J. Reprod. Fertil. Abstr. Ser. 18:86-86(1996)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Ovary.
    2. "Rat zona pellucida glycoproteins: molecular cloning and characterization of the three major components."
      Akatsuka K., Yoshida-Komiya H., Tulsiani D.R.P., Orgebin-Crist M.-C., Hiroi M., Araki Y.
      Mol. Reprod. Dev. 51:454-467(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-63, GLYCOSYLATION.
      Strain: Sprague-Dawley.
      Tissue: Ovary.
    3. "Structural conservation of mouse and rat zona pellucida glycoproteins. Probing the native rat zona pellucida proteome by mass spectrometry."
      Boja E.S., Hoodbhoy T., Garfield M., Fales H.M.
      Biochemistry 44:16445-16460(2005) [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 AND ASN-330, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiZP3_RAT
    AccessioniPrimary (citable) accession number: P97708
    Secondary accession number(s): O55084
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    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