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P48830 (ZP3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 74. 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 3B
Short name=Zp-3B
Zona pellucida protein C

Cleaved into the following chain:

  1. Processed zona pellucida sperm-binding protein 3
Gene names
Name:ZP3
Synonyms:ZPC
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length421 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
Transmembrane helix
   Molecular functionReceptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processbinding of sperm to zona pellucida

Inferred from physical interaction. 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 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 calcium ion transport via store-operated calcium channel activity

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 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 functionmanganese ion transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: UniProtKB

receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

signal transducer activity

Inferred from sequence or structural similarity. Source: UniProtKB

sugar binding

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 – 346324Zona pellucida sperm-binding protein 3
PRO_0000041701
Chain23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304565
Propeptide347 – 42175Removed in mature form By similarity
PRO_0000041702

Regions

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

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
P48830 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 905C4722B7BA11DC

FASTA42146,545
        10         20         30         40         50         60 
MGPCSRLFVC FLLWGSTELC SPQPFWDDET ERFRPSKPPA VMVECQEAQL VVTVDKDLFG 

        70         80         90        100        110        120 
TGKLIRPADL TLGPDNCEPL ASADTDGVVR FAVGLHECGN ILQVTDNALV YSTFLLHNPR 

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

       190        200        210        220        230        240 
SAEKMTPTFQ LGDRAHLQAQ VHTGSHVPLR LFVDHCVASL TPDWSTSPYH TIVDFHGCLV 

       250        260        270        280        290        300 
DGLTDASSAF KAPRPRPEIL QFTVDVFRFA NDSRNMIYIT CHLKVTPVDR VPDQLNKACS 

       310        320        330        340        350        360 
FSKSSNRWSP VEGPTDICRC CSKGRCGISG RSMRLSHREG RPVPRSRRHV TEEADVTVGP 

       370        380        390        400        410        420 
LIFLRKMNDR GVEGPTSSPP LVMLGLGLAT VMTLTLAAIV LGLTGRLRAA SHPVCPVSAS 


Q 

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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.

Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U05775 mRNA. Translation: AAA74385.1.
IPIIPI00703432.
PIRS70402.
RefSeqNP_776399.1. NM_173974.2.
UniGeneBt.511.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP48830.

Proteomic databases

PRIDEP48830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID280964.
KEGGbta:280964.

Organism-specific databases

CTD7784.

Phylogenomic databases

eggNOGmaNOG06569.
HOVERGENHBG007985.
InParanoidP48830.
OrthoDBEOG437RFK.

Family and domain databases

InterProIPR017977. Endoglin/CD105_CS.
IPR017976. Endoglin/CD105_subgr.
IPR001507. Zona_pellucida_Endoglin/CD105.
[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_BOVIN
AccessionPrimary (citable) accession number: P48830
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 16, 2011
This is version 74 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