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P42098

- ZP3_PIG

UniProt

P42098 - ZP3_PIG

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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

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
Complete GO annotation...

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-KW
  12. secretory granule Source: UniProtKB
Complete GO annotation...

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.
InParanoidiP42098.

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

« Hide

        10         20         30         40         50
MAPSWRFFVC FLLWGGTELC SPQPVWQDEG QRLRPSKPPT VMVECQEAQL
60 70 80 90 100
VVIVSKDLFG TGKLIRPADL SLGPAKCEPL VSQDTDAVVR FEVGLHECGS
110 120 130 140 150
SLQVTDDALV YSTFLRHDPR PAGNLSILRT NRAEVPIECH YPRQGNVSSW
160 170 180 190 200
AILPTWVPFR TTVFSEEKLV FSLRLMEENW SAEKMTPTFQ LGDRAHLQAQ
210 220 230 240 250
VHTGSHVPLR LFVDHCVATL TPDWNTSPSH TIVDFHGCLV DGLTEASSAF
260 270 280 290 300
KAPRPGPETL QFTVDVFHFA NDSRNTIYIT CHLKVTPADR VPDQLNKACS
310 320 330 340 350
FSKSSNRWSP VEGPAVICRC CHKGQCGTPS LSRKLSMPKR QSAPRSRRHV
360 370 380 390 400
TDEADVTVGP LIFLGKTSDH GVEGSTSSPT SVMVGLGLAT VVTLTLATIV
410 420
LGVPRRRRAA AHLVCPVSAS Q
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.
InParanoidi P42098.

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 29, 2014
This is version 93 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