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Reviewed, UniProtKB/Swiss-Prot P48832 (ZP3_FELCA)

Last modified October 13, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Zona pellucida sperm-binding protein 3
Alternative name(s):
    Zona pellucida glycoprotein ZP3
    Zona pellucida protein C
    Sperm receptor
Cleaved into the following chain:
    1- Recommended name:
            Processed zona pellucida sperm-binding protein 3
Gene names
Name: ZP3
Synonyms: ZPC
OrganismFelis catus (Cat) (Felis silvestris catus)
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.

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
   Molecular functionReceptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processsingle fertilization

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionreceptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

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 – 40421 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
P48832-1 [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: 7841460] [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

U05778 mRNA. Translation: AAA74390.1.
D45068 mRNA. Translation: BAA08096.1.
PIRS70399.
RefSeqNP_001009330.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP48832.

Genome annotation databases

GeneID493925.

Organism-specific databases

CTD493925.

Phylogenomic databases

HOVERGENP48832.

Family and domain databases

InterProIPR001507. Endoglin/CD105.
IPR017977. Endoglin/CD105_CS.
IPR017976. Endoglin/CD105_subgr.
[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: October 13, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents