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P97708 (ZP3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. 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):
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:Zp-3, Zpc
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

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; N-linked glycans are of high mannose/hybrid type, as well as bi-, tri- and tetra-antennary complex types. Ref.2 Ref.3

O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy. Ref.2 Ref.3

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
Direct protein sequencing
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

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 – 351329Zona pellucida sperm-binding protein 3
PRO_0000041721
Chain23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304575
Propeptide352 – 42473Removed in mature form
PRO_0000041722

Regions

Topological domain23 – 387365Extracellular Potential
Transmembrane388 – 40821Helical; Potential
Topological domain409 – 42416Cytoplasmic Potential
Domain45 – 308264ZP
Compositional bias329 – 3346Poly-Ser

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid
Glycosylation321O-linked (GalNAc...) By similarity
Glycosylation341O-linked (GalNAc...) By similarity
Glycosylation391O-linked (GalNAc...) By similarity
Glycosylation1461N-linked (GlcNAc...) Ref.3
Glycosylation1551O-linked (GalNAc...) By similarity
Glycosylation1621O-linked (GalNAc...) By similarity
Glycosylation2731N-linked (GlcNAc...) Ref.3
Glycosylation3041N-linked (GlcNAc...) Ref.3
Glycosylation3271N-linked (GlcNAc...) By similarity
Glycosylation3301N-linked (GlcNAc...) Ref.3
Disulfide bond46 ↔ 139 By similarity
Disulfide bond78 ↔ 98
Disulfide bond216 ↔ 283
Disulfide bond240 ↔ 301

Experimental info

Sequence conflict551V → A in BAA24456. Ref.2
Sequence conflict1121N → S in BAA24456. Ref.2
Sequence conflict4121K → M in BAA24456. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P97708 [UniParc].

Last modified June 1, 1998. Version 2.
Checksum: 2AB42CBB14DE8701

FASTA42445,901
        10         20         30         40         50         60 
MGPSCLLFLC LLLCGGPELC YPQTQWLLPG GTPTPAGSSS PVEVECKEAE LVVTVRRDLF 

        70         80         90        100        110        120 
GTGKLVQPGD LTLGSEGCQP LVAVDTDVVR LNAQLHECSS GVQVTEDALV YNTFLLHDPR 

       130        140        150        160        170        180 
PVNGLSILRT NRVEVPIECR YPRQGNVSSH PIQPTWVPFS ATVSSEEKLA FSLRLMEEDW 

       190        200        210        220        230        240 
NTEKSSPTFH LGEVAHLQAE VQTGSHLPLQ LFVDHCVATP SPLPGQNSSP HHFIVDSHGC 

       250        260        270        280        290        300 
LVDGLSESFS AFQVPRPRPE TLQFTVDVFH FANSSRNTVY ITCHLKVAPA NQIPDKLNKA 

       310        320        330        340        350        360 
CSFNKTSQSW LPVEGDADIC DCCSNGNCSN SSSSEFETHE PAQWSTLVSR NRRHVTDEAD 

       370        380        390        400        410        420 
VTVGPLIFLG KANDQAVEGW TSSAQTSVAL GLGLATVAFL TLAAIVLGVT RKCHTSSYLV 


SLPQ

« Hide

References

[1]"Molecular characterisation of zona pellucida protein 3 (ZP3) in the rat."
MacDuff P.E., Kerr L.E., Aitken R.J.
J. Reprod. Fertil. Abstr. Ser. 18:86-86(1996)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Ovary.
[2]"Rat zona pellucida glycoproteins: molecular cloning and characterization of the three major components."
Akatsuka K., Yoshida-Komiya H., Tulsiani D.R.P., Orgebin-Crist M.-C., Hiroi M., Araki Y.
Mol. Reprod. Dev. 51:454-467(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-63, GLYCOSYLATION.
Strain: Sprague-Dawley.
Tissue: Ovary.
[3]"Structural conservation of mouse and rat zona pellucida glycoproteins. Probing the native rat zona pellucida proteome by mass spectrometry."
Boja E.S., Hoodbhoy T., Garfield M., Fales H.M.
Biochemistry 44:16445-16460(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF C-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-23, DISULFIDE BOND FORMATION AT 78-CYS--CYS-98; 216-CYS--CYS-283 AND 240-CYS--CYS-301, GLYCOSYLATION AT ASN-146; ASN-273; ASN-304 AND ASN-330, MASS SPECTROMETRY.

Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y10823 mRNA. Translation: CAA71787.1.
D78482 mRNA. Translation: BAA24456.1.
IPIIPI00326649.
RefSeqNP_446214.1. NM_053762.1.
UniGeneRn.10892.

3D structure databases

ProteinModelPortalP97708.
ModBaseSearch...

Proteomic databases

PRIDEP97708.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID114639.
KEGGrno:114639.
UCSCRGD:620606. rat.

Organism-specific databases

CTD7784.
RGD620606. Zp3.

Phylogenomic databases

eggNOGNOG43042.
HOGENOMHOG000220813.
HOVERGENHBG007985.
InParanoidP97708.
OrthoDBEOG437RFK.

Gene expression databases

ArrayExpressP97708.
GenevestigatorP97708.
GermOnlineENSRNOG00000001434. Rattus norvegicus.

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...

Other

NextBio618829.

Entry information

Entry nameZP3_RAT
AccessionPrimary (citable) accession number: P97708
Secondary accession number(s): O55084
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 1998
Last modified: April 3, 2013
This is version 85 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