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P42098

- ZP3_PIG

UniProt

P42098 - ZP3_PIG

Protein

Zona pellucida sperm-binding protein 3

Gene

ZP3

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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 zona matrix formation. In pig, does not seem to have a sperm-binding activity by itself but may increase sperm-binding activity of ZPB.

    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 glycoprotein 3-beta
    Short name:
    Zp-3-beta
    Short name:
    Zp3-beta
    Zona pellucida protein C
    Cleaved into the following chain:
    Gene namesi
    Name:ZP3
    Synonyms:ZP3B, ZPC
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    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 – 22221 PublicationAdd
    BLAST
    Chaini23 – 332310Zona pellucida sperm-binding protein 3PRO_0000041717Add
    BLAST
    Chaini23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304573
    Propeptidei333 – 42189Removed in mature form1 PublicationPRO_0000041718Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei23 – 231Pyrrolidone carboxylic acid1 Publication
    Disulfide bondi45 ↔ 139By similarity
    Disulfide bondi77 ↔ 98By similarity
    Glycosylationi124 – 1241N-linked (GlcNAc...)1 PublicationCAR_000151
    Glycosylationi146 – 1461N-linked (GlcNAc...)1 PublicationCAR_000152
    Glycosylationi155 – 1551O-linked (GalNAc...)1 Publication
    Glycosylationi161 – 1611O-linked (GalNAc...)1 Publication
    Glycosylationi162 – 1621O-linked (GalNAc...)1 Publication
    Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi216 ↔ 281By similarity
    Disulfide bondi238 ↔ 299By similarity
    Glycosylationi271 – 2711N-linked (GlcNAc...)1 PublicationCAR_000153

    Post-translational modificationi

    Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.1 Publication
    O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy.By similarity
    All cysteine residues are involved in disulfide bonds.

    Keywords - PTMi

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

    PTM databases

    UniCarbKBiP42098.

    Expressioni

    Tissue specificityi

    Oocytes.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000008213.

    Structurei

    3D structure databases

    ProteinModelPortaliP42098.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 381359ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini403 – 42119CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei382 – 40221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini44 – 306263ZPPROSITE-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.
    HOGENOMiHOG000220813.
    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.

    P42098-1 [UniParc]FASTAAdd to Basket

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    MAPSWRFFVC FLLWGGTELC SPQPVWQDEG QRLRPSKPPT VMVECQEAQL    50
    VVIVSKDLFG TGKLIRPADL SLGPAKCEPL VSQDTDAVVR FEVGLHECGS 100
    SLQVTDDALV YSTFLRHDPR PAGNLSILRT NRAEVPIECH YPRQGNVSSW 150
    AILPTWVPFR TTVFSEEKLV FSLRLMEENW SAEKMTPTFQ LGDRAHLQAQ 200
    VHTGSHVPLR LFVDHCVATL TPDWNTSPSH TIVDFHGCLV DGLTEASSAF 250
    KAPRPGPETL QFTVDVFHFA NDSRNTIYIT CHLKVTPADR VPDQLNKACS 300
    FSKSSNRWSP VEGPAVICRC CHKGQCGTPS LSRKLSMPKR QSAPRSRRHV 350
    TDEADVTVGP LIFLGKTSDH GVEGSTSSPT SVMVGLGLAT VVTLTLATIV 400
    LGVPRRRRAA AHLVCPVSAS Q 421
    Length:421
    Mass (Da):46,239
    Last modified:November 1, 1995 - v1
    Checksum:iDC97D760E985213A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011Missing in BAA08093. 1 PublicationCurated
    Sequence conflicti107 – 1071D → V in BAA08093. 1 PublicationCurated
    Sequence conflicti163 – 1642VF → GV in BAA08093. 1 PublicationCurated
    Sequence conflicti404 – 4041P → A in BAA08093. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22169 mRNA. Translation: AAA31145.1.
    D45065 mRNA. Translation: BAA08093.1.
    PIRiS70433.
    RefSeqiNP_999058.1. NM_213893.1.
    UniGeneiSsc.80359.

    Genome annotation databases

    GeneIDi396927.
    KEGGissc:396927.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Molecular chastity - Issue 93 of April 2008

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22169 mRNA. Translation: AAA31145.1 .
    D45065 mRNA. Translation: BAA08093.1 .
    PIRi S70433.
    RefSeqi NP_999058.1. NM_213893.1.
    UniGenei Ssc.80359.

    3D structure databases

    ProteinModelPortali P42098.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000008213.

    PTM databases

    UniCarbKBi P42098.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 396927.
    KEGGi ssc:396927.

    Organism-specific databases

    CTDi 7784.

    Phylogenomic databases

    eggNOGi NOG43042.
    HOGENOMi HOG000220813.
    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. "Cloning and characterization of zona pellucida genes and cDNAs from a variety of mammalian species: the ZPA, ZPB and ZPC gene families."
      Harris J.D., Hibler D.W., Fontenot G.K., Hsu K.T., Yurewicz E.C., Sacco A.G.
      DNA Seq. 4:361-393(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.
    2. Okazaki Y., Sugimoto M.
      Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.
    3. "Localization of epitopes for monoclonal antibodies at the N-terminus of the porcine zona pellucida glycoprotein pZPC."
      Gupta S.K., Yurewicz E.C., Afzalpurkar A., Rao K.V., Gage D.A., Wu H., Sacco A.G.
      Mol. Reprod. Dev. 42:220-225(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-23, IDENTIFICATION BY MASS SPECTROMETRY.
    4. "Identification of the carboxyl termini of porcine zona pellucida glycoproteins ZPB and ZPC."
      Yonezawa N., Nakano M.
      Biochem. Biophys. Res. Commun. 307:877-882(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    5. "Porcine oocyte zona pellucida M(r) 55,000 glycoproteins: identification of O-glycosylated domains."
      Yurewicz E.C., Pack B.A., Sacco A.G.
      Mol. Reprod. Dev. 33:182-188(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.

    Entry informationi

    Entry nameiZP3_PIG
    AccessioniPrimary (citable) accession number: P42098
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 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