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P42098 (ZP3_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Processed zona pellucida sperm-binding protein 3
Gene names
Name:ZP3
Synonyms:ZP3B, ZPC
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

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; Single-pass type I membrane protein.

Tissue specificity

Oocytes.

Domain

The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.

Post-translational modification

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida. Ref.4

O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy By similarity. Ref.5

All cysteine residues are involved in disulfide bonds.

Sequence similarities

Belongs to the ZP domain family. ZPC subfamily.

Contains 1 ZP domain.

Ontologies

Keywords
   Biological processFertilization
   Cellular componentCell membrane
Extracellular matrix
Membrane
Secreted
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbinding of sperm to zona pellucida

Inferred from sequence or structural similarity. Source: UniProtKB

blastocyst formation

Inferred from sequence or structural similarity. Source: UniProtKB

egg coat formation

Inferred from sequence or structural similarity. Source: UniProtKB

humoral immune response mediated by circulating immunoglobulin

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

manganese ion transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

manganese ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of binding of sperm to zona pellucida

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

oocyte development

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of T cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of acrosomal vesicle exocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of acrosome reaction

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of antral ovarian follicle growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of calcium ion import

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of humoral immune response

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interferon-gamma production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-4 production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of leukocyte migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ovarian follicle development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of type IV hypersensitivity

Inferred from direct assay PubMed 15579591. Source: UniProtKB

protein kinase C signaling

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

multivesicular body

Inferred from sequence or structural similarity. Source: UniProtKB

outer acrosomal membrane

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

secretory granule

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncarbohydrate binding

Inferred from sequence or structural similarity. Source: UniProtKB

manganese ion transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

signal transducer activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.3
Chain23 – 332310Zona pellucida sperm-binding protein 3
PRO_0000041717
Chain23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304573
Propeptide333 – 42189Removed in mature form
PRO_0000041718

Regions

Topological domain23 – 381359Extracellular Potential
Transmembrane382 – 40221Helical; Potential
Topological domain403 – 42119Cytoplasmic Potential
Domain44 – 306263ZP

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid
Glycosylation1241N-linked (GlcNAc...)
CAR_000151
Glycosylation1461N-linked (GlcNAc...)
CAR_000152
Glycosylation1551O-linked (GalNAc...)
Glycosylation1611O-linked (GalNAc...)
Glycosylation1621O-linked (GalNAc...)
Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...)
CAR_000153
Disulfide bond45 ↔ 139 By similarity
Disulfide bond77 ↔ 98 By similarity
Disulfide bond216 ↔ 281 By similarity
Disulfide bond238 ↔ 299 By similarity

Experimental info

Sequence conflict1011Missing in BAA08093. Ref.2
Sequence conflict1071D → V in BAA08093. Ref.2
Sequence conflict163 – 1642VF → GV in BAA08093. Ref.2
Sequence conflict4041P → A in BAA08093. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P42098 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: DC97D760E985213A

FASTA42146,239
        10         20         30         40         50         60 
MAPSWRFFVC FLLWGGTELC SPQPVWQDEG QRLRPSKPPT VMVECQEAQL VVIVSKDLFG 

        70         80         90        100        110        120 
TGKLIRPADL SLGPAKCEPL VSQDTDAVVR FEVGLHECGS SLQVTDDALV YSTFLRHDPR 

       130        140        150        160        170        180 
PAGNLSILRT NRAEVPIECH YPRQGNVSSW AILPTWVPFR TTVFSEEKLV FSLRLMEENW 

       190        200        210        220        230        240 
SAEKMTPTFQ LGDRAHLQAQ VHTGSHVPLR LFVDHCVATL TPDWNTSPSH TIVDFHGCLV 

       250        260        270        280        290        300 
DGLTEASSAF KAPRPGPETL QFTVDVFHFA NDSRNTIYIT CHLKVTPADR VPDQLNKACS 

       310        320        330        340        350        360 
FSKSSNRWSP VEGPAVICRC CHKGQCGTPS LSRKLSMPKR QSAPRSRRHV TDEADVTVGP 

       370        380        390        400        410        420 
LIFLGKTSDH GVEGSTSSPT SVMVGLGLAT VVTLTLATIV LGVPRRRRAA AHLVCPVSAS 


Q 

« Hide

References

[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.

Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L22169 mRNA. Translation: AAA31145.1.
D45065 mRNA. Translation: BAA08093.1.
PIRS70433.
RefSeqNP_999058.1. NM_213893.1.
UniGeneSsc.80359.

3D structure databases

ProteinModelPortalP42098.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000008213.

PTM databases

UniCarbKBP42098.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396927.
KEGGssc:396927.

Organism-specific databases

CTD7784.

Phylogenomic databases

eggNOGNOG43042.
HOGENOMHOG000220813.
HOVERGENHBG007985.

Family and domain databases

InterProIPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamPF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSPR00023. ZPELLUCIDA.
SMARTSM00241. ZP. 1 hit.
[Graphical view]
PROSITEPS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameZP3_PIG
AccessionPrimary (citable) accession number: P42098
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries