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P23491 (ZP3_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length422 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: Secreted › extracellular space › extracellular matrix.

Cell membrane; Single-pass type I membrane protein.

Tissue specificity

Oocytes.

Developmental stage

Growing 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

negative regulation of binding of sperm to zona pellucida

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-dependent

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 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 cascade

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-dependent

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 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

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 to 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

   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 – 349327Zona pellucida sperm-binding protein 3
PRO_0000041713
Chain23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304571
Propeptide350 – 42273Removed in mature form By similarity
PRO_0000041714

Regions

Topological domain23 – 386364Extracellular Potential
Transmembrane387 – 40721Helical; Potential
Topological domain408 – 42215Cytoplasmic Potential
Domain45 – 306262ZP
Compositional bias119 – 15840Pro-rich
Compositional bias208 – 25750Pro-rich

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid By similarity
Glycosylation321O-linked (GalNAc...) By similarity
Glycosylation341O-linked (GalNAc...) By similarity
Glycosylation1461N-linked (GlcNAc...) By similarity
Glycosylation1551O-linked (GalNAc...) By similarity
Glycosylation1611O-linked (GalNAc...) By similarity
Glycosylation1621O-linked (GalNAc...) By similarity
Glycosylation2711N-linked (GlcNAc...) By similarity
Glycosylation3021N-linked (GlcNAc...) By similarity
Disulfide bond46 ↔ 139 By similarity
Disulfide bond78 ↔ 98 By similarity
Disulfide bond216 ↔ 281 By similarity
Disulfide bond238 ↔ 299 By similarity

Sequences

Sequence LengthMass (Da)Tools
P23491 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: D0F95BE7FF8E7E01

FASTA42245,827
        10         20         30         40         50         60 
MGLSYQLLLC LLLCGGAKQC CSQPLWLLPG GTPTPGKLTS SVEVECLEAE LVVTVSRDLF 

        70         80         90        100        110        120 
GTGKLIQPED LTLGSENCRP LVSVATDVVR FKAQLHECSN RVQVTEDALV YSTVLLHQPR 

       130        140        150        160        170        180 
PVPGLSILRT NRADVPIECR YPRQGNVSSH AIRPTWVPFS TTVSSEEKLV FSLRLMEENW 

       190        200        210        220        230        240 
NTEKLSPTSH LGEVAYLQAE VQTGSHLPLL LFVDRCVPTP SPDQTASPYH VIVDFHGCLV 

       250        260        270        280        290        300 
DGLSESFSAF QVPRPRPETL QFTVDVFHFA NSSRNTIYIT CHLKVTPANQ TPDELNKACS 

       310        320        330        340        350        360 
FNRSSKSWSP VEGDAEVCGC CSSGDCGSSS RSRYQAHGVS QWPKSASRRR RHVRDEADVT 

       370        380        390        400        410        420 
VGPLIFLGKA SDQAVEGWAS SAQTSLALGL GLAAVAFLTL AAIVLGVTRS CHTPSHVVSL 


SQ

« Hide

References

[1]"Genomic organization and polypeptide primary structure of zona pellucida glycoprotein hZP3, the hamster sperm receptor."
Kinloch R.A., Ruiz-Seller B., Wassarman P.M.
Dev. Biol. 142:414-421(1990) [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		M63629 mRNA. Translation: AAA37079.1.
PIRA60503.

3D structure databases

ProteinModelPortalP23491.
ModBaseSearch...

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_MESAU
AccessionPrimary (citable) accession number: P23491
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 71 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents