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Reviewed, UniProtKB/Swiss-Prot P42098 (ZP3_PIG)

Last modified November 24, 2009. Version 65. 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 protein 3-beta
    Zona pellucida glycoprotein ZP3-beta
    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: ZP3B, ZPC
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length421 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 zona matrix formation. In pig, does not seem to have a sperm-binding activity by itself but may increase sperm-binding activity of ZPB.

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. Ref.4

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

All cysteine residues are involved in disulfide bonds.

Sequence similarities

Belongs to the ZP domain family. ZPC subfamily.

Contains 1 ZP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 332310Zona pellucida sperm-binding protein 3
PRO_0000041717
Chain23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304573
Propeptide333 – 42189Removed in mature form
PRO_0000041718

Regions

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

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid
Glycosylation1241N-linked (GlcNAc...)
CAR_000151
Glycosylation1461N-linked (GlcNAc...)
CAR_000152
Glycosylation1551O-linked (GalNAc...)
Glycosylation1611O-linked (GalNAc...)
Glycosylation1621O-linked (GalNAc...)
Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...)
CAR_000153
Disulfide bond45 ↔ 139 By similarity
Disulfide bond77 ↔ 98 By similarity
Disulfide bond216 ↔ 281 By similarity
Disulfide bond238 ↔ 299 By similarity

Experimental info

Sequence conflict1011Missing in BAA08093. Ref.2
Sequence conflict1071D → V in BAA08093. Ref.2
Sequence conflict163 – 1642VF → GV in BAA08093. Ref.2
Sequence conflict4041P → A in BAA08093. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P42098-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: DC97D760E985213A

FASTA42146,239
        10         20         30         40         50         60 
MAPSWRFFVC FLLWGGTELC SPQPVWQDEG QRLRPSKPPT VMVECQEAQL VVIVSKDLFG 

        70         80         90        100        110        120 
TGKLIRPADL SLGPAKCEPL VSQDTDAVVR FEVGLHECGS SLQVTDDALV YSTFLRHDPR 

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

       190        200        210        220        230        240 
SAEKMTPTFQ LGDRAHLQAQ VHTGSHVPLR LFVDHCVATL TPDWNTSPSH TIVDFHGCLV 

       250        260        270        280        290        300 
DGLTEASSAF KAPRPGPETL QFTVDVFHFA NDSRNTIYIT CHLKVTPADR VPDQLNKACS 

       310        320        330        340        350        360 
FSKSSNRWSP VEGPAVICRC CHKGQCGTPS LSRKLSMPKR QSAPRSRRHV TDEADVTVGP 

       370        380        390        400        410        420 
LIFLGKTSDH GVEGSTSSPT SVMVGLGLAT VVTLTLATIV LGVPRRRRAA AHLVCPVSAS 


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.
[2]Okazaki Y., Sugimoto M.
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[3]"Localization of epitopes for monoclonal antibodies at the N-terminus of the porcine zona pellucida glycoprotein pZPC."
Gupta S.K., Yurewicz E.C., Afzalpurkar A., Rao K.V., Gage D.A., Wu H., Sacco A.G.
Mol. Reprod. Dev. 42:220-225(1995) [PubMed: 8562067] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-23, MASS SPECTROMETRY.
[4]"Identification of the carboxyl termini of porcine zona pellucida glycoproteins ZPB and ZPC."
Yonezawa N., Nakano M.
Biochem. Biophys. Res. Commun. 307:877-882(2003) [PubMed: 12878193] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[5]"Porcine oocyte zona pellucida M(r) 55,000 glycoproteins: identification of O-glycosylated domains."
Yurewicz E.C., Pack B.A., Sacco A.G.
Mol. Reprod. Dev. 33:182-188(1992) [PubMed: 1418987] [Abstract]
Cited for: GLYCOSYLATION.

Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Cross-references

Sequence databases

L22169 mRNA. Translation: AAA31145.1.
D45065 mRNA. Translation: BAA08093.1.
PIRS70433.
RefSeqNP_999058.1.
UniGeneSsc.14525

3D structure databases

ModBaseSearch...

PTM databases

GlycoSuiteDBP42098.

Genome annotation databases

EnsemblENSSSCT00000008432; ENSSSCP00000008213; ENSSSCG00000007691; Sus scrofa. [Genome view]
GeneID396927.
KEGGssc:396927.

Organism-specific databases

CTD396927.

Phylogenomic databases

HOVERGENP42098.

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_PIG
AccessionPrimary (citable) accession number: P42098
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 24, 2009
This is version 65 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