P10761 (ZP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	Zp-3, Zpc

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Subcellular location	Processed zona pellucida sperm-binding protein 3: Secreted › extracellular space › extracellular matrix Ref.8. Cell membrane; Single-pass type I membrane protein Ref.8.
Tissue specificity	Oocytes.
Developmental stage	Expressed during the 2-week growth phase of oogenesis, prior to ovulation.
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. O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy. Ref.7 Cys-320, Cys-322, Cys-323 and Cys-328 are involved in two additional disulfide bonds.
Sequence similarities	Belongs to the ZP domain family. ZPC subfamily. Contains 1 ZP domain.

Ontologies

Keywords
Cellular component	Cell membrane Extracellular matrix Membrane Secreted
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	binding of sperm to zona pellucida Inferred from mutant phenotype PubMed 11417900. Source: UniProtKB blastocyst formation Inferred from mutant phenotype PubMed 20382503. Source: UniProtKB egg coat formation Inferred from mutant phenotype PubMed 14645511PubMed 18420282. Source: UniProtKB humoral immune response mediated by circulating immunoglobulin Inferred from direct assay PubMed 20382503. Source: UniProtKB intracellular protein transport Inferred from mutant phenotype PubMed 14645511PubMed 17047254. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 18667753. Source: UniProtKB oocyte development Inferred from mutant phenotype PubMed 18420282. Source: UniProtKB phosphatidylinositol-mediated signaling Inferred from mutant phenotype PubMed 17258189. Source: UniProtKB positive regulation of T cell proliferation Inferred from direct assay PubMed 15579591. Source: UniProtKB positive regulation of acrosomal vesicle exocytosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of acrosome reaction Inferred from direct assay PubMed 10793136. Source: UniProtKB positive regulation of antral ovarian follicle growth Inferred from mutant phenotype PubMed 18420282PubMed 20382503. Source: UniProtKB positive regulation of calcium ion import Inferred from direct assay PubMed 10793136. Source: UniProtKB positive regulation of humoral immune response Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of interferon-gamma production Inferred from direct assay PubMed 15579591. Source: UniProtKB positive regulation of interleukin-4 production Inferred from direct assay PubMed 15579591. Source: UniProtKB positive regulation of leukocyte migration Inferred from direct assay PubMed 18667753. Source: UniProtKB positive regulation of ovarian follicle development Inferred from direct assay PubMed 18667753. Source: UniProtKB positive regulation of phosphatidylinositol biosynthetic process Inferred from direct assay PubMed 17258189. Source: UniProtKB positive regulation of protein kinase B signaling cascade Inferred from mutant phenotype PubMed 17258189. Source: UniProtKB positive regulation of protein kinase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 18667753. Source: UniProtKB positive regulation of type IV hypersensitivity Inferred from direct assay PubMed 15579591. Source: UniProtKB protein kinase C signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 11906903PubMed 14645511. Source: UniProtKB endoplasmic reticulum Inferred from direct assay PubMed 14645511PubMed 17047254. Source: UniProtKB extracellular matrix Inferred from direct assay PubMed 11906903Ref.8. 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 direct assay PubMed 17047254. Source: UniProtKB outer acrosomal membrane Inferred from direct assay PubMed 11417900. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay PubMed 14645511. Source: UniProtKB plasma membrane Inferred from direct assay PubMed 11417900PubMed 14645511Ref.8. Source: UniProtKB proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carbohydrate binding Inferred from sequence or structural similarity. Source: UniProtKB manganese ion transmembrane transporter activity Inferred from direct assay PubMed 10793136. Source: UniProtKB signal transducer activity Inferred from direct assay PubMed 10793136. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Chain

23 – 351

329

Zona pellucida sperm-binding protein 3

PRO_0000041715

Chain

23 – ?

Processed zona pellucida sperm-binding protein 3

PRO_0000304572

Propeptide

352 – 424

73

Removed in mature form

PRO_0000041716

Regions

Topological domain

23 – 387

365

Extracellular

Transmembrane

388 – 408

21

Helical; Potential

Topological domain

409 – 424

16

Cytoplasmic

Domain

45 – 308

264

ZP

Amino acid modifications

Modified residue

23

1

Pyrrolidone carboxylic acid

Glycosylation

32

1

O-linked (GalNAc...) Probable

Glycosylation

34

1

O-linked (GalNAc...) Probable

Glycosylation

39

1

O-linked (GalNAc...) Probable

Glycosylation

146

1

N-linked (GlcNAc...) Ref.7

Glycosylation

155

1

O-linked (GalNAc...) Probable

Glycosylation

162

1

O-linked (GalNAc...) Probable

Glycosylation

273

1

N-linked (GlcNAc...) Ref.7

Glycosylation

304

1

N-linked (GlcNAc...) Ref.7

Glycosylation

327

1

N-linked (GlcNAc...) Ref.7

Glycosylation

330

1

N-linked (GlcNAc...) Ref.7

Disulfide bond

46 ↔ 139

Ref.8

Disulfide bond

78 ↔ 98

Ref.8

Disulfide bond

216 ↔ 283

Ref.8

Disulfide bond

240 ↔ 301

Ref.8

Experimental info

Mutagenesis

111

1

Y → C: Reduces protein solubility and causes formation of an abnormal disulfide bond between C-111 and C-139 in approximately half of the molecules. Ref.8

Mutagenesis

111

1

Y → F: Causes a mild reduction of protein solubility. Ref.8

Mutagenesis

111

1

Y → L or V: Strongly reduces protein solubility. Ref.8

Mutagenesis

111

1

Y → S: Reduces protein solubility. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

424

Helix Strand Turn

Details...

Beta strand

42 – 46

5

Beta strand

48 – 58

11

Beta strand

60 – 63

4

Helix

68 – 70

3

Beta strand

71 – 75

5

Beta strand

81 – 84

4

Beta strand

86 – 94

9

Helix

95 – 98

4

Beta strand

100 – 104

5

Beta strand

106 – 117

12

Beta strand

133 – 142

10

Sequences

	Sequence		Length	Mass (Da)
	P10761 [UniParc]. Last modified November 1, 1997. Version 4. Checksum: 9089903FBD268365	FASTA	424	46,304
	10 20 30 40 50 60 MASSYFLFLC LLLCGGPELC NSQTLWLLPG GTPTPVGSSS PVKVECLEAE LVVTVSRDLF 70 80 90 100 110 120 GTGKLVQPGD LTLGSEGCQP RVSVDTDVVR FNAQLHECSS RVQMTKDALV YSTFLLHDPR 130 140 150 160 170 180 PVSGLSILRT NRVEVPIECR YPRQGNVSSH PIQPTWVPFR ATVSSEEKLA FSLRLMEENW 190 200 210 220 230 240 NTEKSAPTFH LGEVAHLQAE VQTGSHLPLQ LFVDHCVATP SPLPDPNSSP YHFIVDFHGC 250 260 270 280 290 300 LVDGLSESFS AFQVPRPRPE TLQFTVDVFH FANSSRNTLY ITCHLKVAPA NQIPDKLNKA 310 320 330 340 350 360 CSFNKTSQSW LPVEGDADIC DCCSHGNCSN SSSSQFQIHG PRQWSKLVSR NRRHVTDEAD 370 380 390 400 410 420 VTVGPLIFLG KANDQTVEGW TASAQTSVAL GLGLATVAFL TLAAIVLAVT RKCHSSSYLV SLPQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular analysis of cDNA coding for ZP3, a sperm binding protein of the mouse zona pellucida." Ringuette M.J., Chamberlin M.E., Baur A.W., Sobieski D.A., Dean J. Dev. Biol. 127:287-295(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Dean J. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 387.
[3]	"Nucleotide sequence of the gene encoding zona pellucida glycoprotein ZP3 -- the mouse sperm receptor." Kinloch R.A., Wassarman P.M. Nucleic Acids Res. 17:2861-2863(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CD-1. Tissue: Liver.
[4]	"Primary structure of the mouse sperm receptor polypeptide determined by genomic cloning." Kinloch R.A., Roller R.J., Fimiani C.M., Wassarman D.A., Wassarman P.M. Proc. Natl. Acad. Sci. U.S.A. 85:6409-6413(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Identification of a region of mouse zona pellucida glycoprotein mZP3 that possesses sperm receptor activity." Rosiere T.K., Wassarman P.M. Dev. Biol. 154:309-317(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 49-63; 197-204; 219-233 AND 261-275. Strain: CD-1.
[7]	"Structural characterization of native mouse zona pellucida proteins using mass spectrometry." Boja E.S., Hoodbhoy T., Fales H.M., Dean J. J. Biol. Chem. 278:34189-34202(2003) [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; ASN-327 AND ASN-330, MASS SPECTROMETRY.
[8]	"Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats." Monne M., Han L., Schwend T., Burendahl S., Jovine L. Nature 456:653-657(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 42-143, MASS SPECTROMETRY, MUTAGENESIS OF TYR-111, SUBCELLULAR LOCATION, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M20026 mRNA. Translation: AAB18629.1.
X14376 Genomic DNA. Translation: CAA32550.1.
BC099465 mRNA. Translation: AAH99465.1.
BC100745 mRNA. Translation: AAI00746.1.
BC103583 mRNA. Translation: AAI03584.1.
BC103584 mRNA. Translation: AAI03585.1.
BC103585 mRNA. Translation: AAI03586.1.

IPI

IPI00114128.

PIR

A30334.

RefSeq

NP_035906.1. NM_011776.1.

UniGene

Mm.1381.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3D4C	X-ray	2.90	A	42-143	[»]
3D4G	X-ray	2.30	A/B/C/D/E/F/G/H	42-143	[»]
3EF7	X-ray	3.10	A/B	42-143	[»]

ProteinModelPortal

P10761.

SMR

P10761. Positions 42-143.

ModBase

Search...

PTM databases

PhosphoSite

P10761.

Proteomic databases

PRIDE

P10761.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000005073; ENSMUSP00000005073; ENSMUSG00000004948.

GeneID

22788.

KEGG

mmu:22788.

UCSC

uc008zzl.1. mouse.

Organism-specific databases

CTD

7784.

MGI

MGI:99215. Zp3.

Phylogenomic databases

eggNOG

NOG43042.

GeneTree

ENSGT00530000063482.

HOGENOM

HOG000220813.

HOVERGEN

HBG007985.

InParanoid

Q4FZI2.

OMA

TPDQNAS.

OrthoDB

EOG437RFK.

Gene expression databases

Bgee

P10761.

CleanEx

MM_ZP3.

Genevestigator

P10761.

GermOnline

ENSMUSG00000004948. Mus musculus.

Family and domain databases

InterPro

IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]

Pfam

PF00100. Zona_pellucida. 1 hit.
[Graphical view]

PRINTS

PR00023. ZPELLUCIDA.

SMART

SM00241. ZP. 1 hit.
[Graphical view]

PROSITE

PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P10761.

NextBio

303371.

SOURCE

Search...

Entry information

Entry name

ZP3_MOUSE

Accession

Primary (citable) accession number: P10761
Secondary accession number(s): Q4FZI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 110 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program