Reviewed, UniProtKB/Swiss-Prot P10761 (ZP3_MOUSE)

Names and origin

Protein names

Recommended name:
    Zona pellucida sperm-binding protein 3
Alternative name(s):
    Zona pellucida glycoprotein ZP3
    Sperm receptor
    Zona pellucida protein C
Cleaved into the following 1 chains:
    1- Recommended name:
            Processed zona pellucida sperm-binding protein 3

Gene names

Name:	Zp3
Synonyms:	Zp-3, Zpc

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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. Cell membrane; Single-pass type I membrane protein.
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. 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
Molecular function	Receptor
PTM	Cleavage on pair of basic residues Glycoprotein Pyrrolidone carboxylic acid
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	binding of sperm to zona pellucida Inferred from direct assay. Source: MGI
Molecular function	protein binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Signal peptide	1 – 22	22
	Chain	23 – 351	329	Zona pellucida sperm-binding protein 3
	Chain	23 – ?		Processed zona pellucida sperm-binding protein 3
	Propeptide	352 – 424	73	Removed in mature form
Regions
	Topological domain	23 – 387	365	Extracellular
	Transmembrane	388 – 408	21	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...)
	Glycosylation	155	1	O-linked (GalNAc...) Probable
	Glycosylation	162	1	O-linked (GalNAc...) Probable
	Glycosylation	273	1	N-linked (GlcNAc...)
	Glycosylation	304	1	N-linked (GlcNAc...)
	Glycosylation	327	1	N-linked (GlcNAc...)
	Glycosylation	330	1	N-linked (GlcNAc...)
	Disulfide bond	78 ↔ 98
	Disulfide bond	216 ↔ 283
	Disulfide bond	240 ↔ 301

Sequences

	Sequence		Length	Mass (Da)
	P10761-1 [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

[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: 3378665] [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: 2541416] [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: 2842770] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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: 1330788] [Abstract] Cited for: PROTEIN SEQUENCE OF 49-63; 197-204; 219-233 AND 261-275. Strain: CD-1.
[6]	"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: 12799386] [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.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Cross-references

Sequence databases
EMBLGenBankDDBJ	M20026 mRNA. Translation: AAB18629.1. X14376 Genomic DNA. Translation: CAA32550.1.
PIR	A30334.
RefSeq	NP_035906.1.
UniGene	Mm.1381
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000004948. Mus musculus. [Contig view]
GeneID	22788.
KEGG	mmu:22788.
Organism-specific databases
MGI	MGI:99215. Zp3.
Phylogenomic databases
HOGENOM	P10761.
HOVERGEN	P10761.
Gene expression databases
ArrayExpress	P10761.
CleanEx	MM_ZP3.
GermOnline	ENSMUSG00000004948. Mus musculus.
Family and domain databases
InterPro	IPR001507. Endoglin/CD105. [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]
ProDom	P10761. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

ZP3_MOUSE

Accession

Primary (citable) accession number: P10761

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1997
Last modified:	July 22, 2008
This is version 73 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)