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P48832 (ZP3_FELCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. 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
OrganismFelis catus (Cat) (Felis silvestris catus) [Reference proteome]
Taxonomic identifier9685 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis

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
   Technical termComplete proteome
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 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

store-operated calcium channel activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 348326Zona pellucida sperm-binding protein 3
PRO_0000041707
Chain23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304568
Propeptide349 – 42476Removed in mature form By similarity
PRO_0000041708

Regions

Topological domain23 – 383361Extracellular Potential
Transmembrane384 – 40421Helical; Potential
Topological domain405 – 42420Cytoplasmic Potential
Domain43 – 305263ZP

Amino acid modifications

Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation1231N-linked (GlcNAc...) By similarity
Glycosylation1451N-linked (GlcNAc...) By similarity
Glycosylation1541O-linked (GalNAc...) By similarity
Glycosylation1601O-linked (GalNAc...) By similarity
Glycosylation1611O-linked (GalNAc...) By similarity
Disulfide bond44 ↔ 138 By similarity
Disulfide bond76 ↔ 97 By similarity
Disulfide bond215 ↔ 280 By similarity
Disulfide bond237 ↔ 298 By similarity

Experimental info

Sequence conflict721G → W in BAA08096. Ref.2
Sequence conflict2641D → Y in BAA08096. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P48832 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: CFC62F35F9AAFC0D

FASTA42446,854
        10         20         30         40         50         60 
MGLSYGLFIC FLLWAGTGLC YPPTTTEDKT HPSLPSSPSV VVECRHAWLV VNVSKNLFGT 

        70         80         90        100        110        120 
GRLVRPADLT LGPENCEPLI SGDSDDTVRF EVELHKCGNS VQVTEDALVY STFLLHNPRP 

       130        140        150        160        170        180 
MGNLSILRTN RAEVPIECRY PRHSNVSSEA ILPTWVPFRT TMLSEEKLAF SLRLMEEDWG 

       190        200        210        220        230        240 
SEKQSPTFQL GDLAHLQAEV HTGRHIPLRL FVDYCVATLT PDQNASPHHT IVDFHGCLVD 

       250        260        270        280        290        300 
GLSDASSAFK APRPRPETLQ FTVDTFHFAN DPRNMIYITC HLKVTPASRV PDQLNKACSF 

       310        320        330        340        350        360 
IKSSNRWFPV EGPADICNCC NKGSCGLQGR SWRLSHLDRP WHKMASRNRR HVTEEADITV 

       370        380        390        400        410        420 
GPLIFLGKAA DRGVEGSTSP HTSVMVGIGL ATVLSLTLAT IVLGLARRHH TASRPMICPV 


SASQ 

« 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.

Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U05778 mRNA. Translation: AAA74390.1.
D45068 mRNA. Translation: BAA08096.1.
PIRS70399.
RefSeqNP_001009330.1. NM_001009330.2.

3D structure databases

ProteinModelPortalP48832.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSFCAT00000013478; ENSFCAP00000012496; ENSFCAG00000013474.
GeneID493925.
KEGGfca:493925.

Organism-specific databases

CTD7784.

Phylogenomic databases

GeneTreeENSGT00530000063482.
HOVERGENHBG007985.
OMALMEEDWG.

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_FELCA
AccessionPrimary (citable) accession number: P48832
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 86 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