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P53785 (ZP3_MACRA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. 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 protein C

Cleaved into the following chain:

  1. Processed zona pellucida sperm-binding protein 3
Gene names
Name:ZP3
Synonyms:ZPC
OrganismMacaca radiata (Bonnet macaque)
Taxonomic identifier9548 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 sperm binding and zona matrix formation.

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.

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.

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
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 sequence or structural similarity. 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 By similarity
Chain23 – 350328Zona pellucida sperm-binding protein 3
PRO_0000041711
Chain23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304570
Propeptide351 – 42474Removed in mature form By similarity
PRO_0000041712

Regions

Topological domain23 – 387365Extracellular Potential
Transmembrane388 – 40821Helical; Potential
Topological domain409 – 42416Cytoplasmic Potential
Domain45 – 307263ZP

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid By similarity
Glycosylation1251N-linked (GlcNAc...) By similarity
Glycosylation1471N-linked (GlcNAc...) By similarity
Glycosylation1561O-linked (GalNAc...) By similarity
Glycosylation1621O-linked (GalNAc...) By similarity
Glycosylation1631O-linked (GalNAc...) By similarity
Glycosylation2721N-linked (GlcNAc...) By similarity
Disulfide bond46 ↔ 140 By similarity
Disulfide bond78 ↔ 99 By similarity
Disulfide bond217 ↔ 282 By similarity
Disulfide bond239 ↔ 300 By similarity

Sequences

Sequence LengthMass (Da)Tools
P53785 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 3B41C4CFA3792331

FASTA42447,040
        10         20         30         40         50         60 
MELSYRLFIC LLLWGSTELC YPQPFWLLQG GASRAETSVQ PVLVECREAT LLVTVSKDLF 

        70         80         90        100        110        120 
GTGKLIRAAD LTLGPEACEP LVSMDTEDVV RFEVGLHECG SSMQVTDDAL VYSTFLLHDP 

       130        140        150        160        170        180 
RPVGNLSIVR TNRAEIPIEC RYPRQGNVSS QAILPTWLPF RTTVFSEEKL TFSLRLMEEN 

       190        200        210        220        230        240 
WNAEKRSPTF HLGDAAHLQA EIHTGSHVPL RLFVDHCVAT PTPDQNASPY HTIVDFHGCL 

       250        260        270        280        290        300 
VDGLTDASSA FKVPRPGPDT LQFTVDVFHF ANDSRNMIYI TCHLKAIPAE QEPDELNKAC 

       310        320        330        340        350        360 
SFSKSSNSWF PVEGPADICQ CCSKGDCGTP SHSRRQPHVV SQWSRSASRN RRHVTEEADI 

       370        380        390        400        410        420 
TVGPLIFLDR SADYEVEQWA LPADTSVLLL GIGLAVVASL TLTAVILIFT RRWRTASRPV 


SASE 

« Hide

References

[1]"Nucleotide sequence of cDNA encoding bonnet monkey (Macaca radiata) zona pellucida glycoprotein-ZP3."
Kolluri S.K., Kaul R., Banerjee K., Gupta S.K.
Reprod. Fertil. Dev. 7:1209-1212(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.

Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82639 mRNA. Translation: CAA57961.1.

3D structure databases

ProteinModelPortalP53785.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

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_MACRA
AccessionPrimary (citable) accession number: P53785
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 69 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