[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0012-1606(88)90315-6; PubMed=3378665 [NCBI, ExPASy, EBI, Israel, Japan] Ringuette M.J., Chamberlin M.E., Baur A.W., Sobieski D.A., Dean J.; "Molecular analysis of cDNA coding for ZP3, a sperm binding protein of the mouse zona pellucida."; Dev. Biol. 127:287-295(1988).
[2]	SEQUENCE REVISION TO 387. Dean J.; Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=CD-1; TISSUE=Liver; DOI=10.1093/nar/17.7.2861; PubMed=2541416 [NCBI, ExPASy, EBI, Israel, Japan] Kinloch R.A., Wassarman P.M.; "Nucleotide sequence of the gene encoding zona pellucida glycoprotein ZP3 -- the mouse sperm receptor."; Nucleic Acids Res. 17:2861-2863(1989).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2842770 [NCBI, ExPASy, EBI, Israel, Japan] Kinloch R.A., Roller R.J., Fimiani C.M., Wassarman D.A., Wassarman P.M.; "Primary structure of the mouse sperm receptor polypeptide determined by genomic cloning."; Proc. Natl. Acad. Sci. U.S.A. 85:6409-6413(1988).
[5]	PROTEIN SEQUENCE OF 49-63; 197-204; 219-233 AND 261-275. STRAIN=CD-1; DOI=10.1016/0012-1606(92)90070-W; PubMed=1330788 [NCBI, ExPASy, EBI, Israel, Japan] Rosiere T.K., Wassarman P.M.; "Identification of a region of mouse zona pellucida glycoprotein mZP3 that possesses sperm receptor activity."; Dev. Biol. 154:309-317(1992).
[6]	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, AND MASS SPECTROMETRY. DOI=10.1074/jbc.M304026200; PubMed=12799386 [NCBI, ExPASy, EBI, Israel, Japan] Boja E.S., Hoodbhoy T., Fales H.M., Dean J.; "Structural characterization of native mouse zona pellucida proteins using mass spectrometry."; J. Biol. Chem. 278:34189-34202(2003).

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: 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.
SUBCELLULAR LOCATION: 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.
PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
PTM: O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy.
PTM: Cys-320, Cys-322, Cys-323 and Cys-328 are involved in two additional disulfide bonds.
SIMILARITY: Belongs to the ZP domain family. ZPC subfamily.
SIMILARITY: Contains 1 ZP domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M20026; AAB18629.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X14376; CAA32550.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A30334; A30334.

NP_035906.1; -.

3D structure databases

ModBase

P10761.

Organism-specific databases

MGI

MGI:99215; Zp3.

GeneLynx

Zp3; Mus musculus.

Gene expression databases

ArrayExpress

P10761; -.

CleanEx

MM_ZP3; -.

GermOnline

ENSMUSG00000004948; Mus musculus.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0007339;	Biological process: binding of sperm to zona pellucida (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001507; Endoglin/CD105.
Graphical view of domain structure.

Pfam

PF00100; Zona_pellucida; 1.
Pfam graphical view of domain structure.

PRINTS

PR00023; ZPELLUCIDA.

SMART

SM00241; ZP; 1.
SMART graphical view of domain structure.

PROSITE

PS00682; ZP_1; 1.
PS51034; ZP_2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P10761.

Genome annotation databases

Ensembl

ENSMUSG00000004948; Mus musculus. [Contig view]

GeneID

22788; -.

KEGG

mmu:22788; -.

Other

Zp3; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cleavage on pair of basic residues; Direct protein sequencing; Extracellular matrix; Glycoprotein; Membrane; Pyrrolidone carboxylic acid; Receptor; Secreted; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`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`
`PROPEP`	`352 424`	`73`	`Removed in mature form.`	`PRO_0000041716`
`TOPO_DOM`	`23 387`	`365`	`Extracellular.`
`TRANSMEM`	`388 408`	`21`	`Potential.`
`TOPO_DOM`	`409 424`	`16`	`Cytoplasmic.`
`DOMAIN`	`45 308`	`264`	`ZP.`
`MOD_RES`	`23 23`		`Pyrrolidone carboxylic acid.`
`CARBOHYD`	`32 32`		`O-linked (GalNAc...) (Probable).`
`CARBOHYD`	`34 34`		`O-linked (GalNAc...) (Probable).`
`CARBOHYD`	`39 39`		`O-linked (GalNAc...) (Probable).`
`CARBOHYD`	`146 146`		`N-linked (GlcNAc...).`
`CARBOHYD`	`155 155`		`O-linked (GalNAc...) (Probable).`
`CARBOHYD`	`162 162`		`O-linked (GalNAc...) (Probable).`
`CARBOHYD`	`273 273`		`N-linked (GlcNAc...).`
`CARBOHYD`	`304 304`		`N-linked (GlcNAc...).`
`CARBOHYD`	`327 327`		`N-linked (GlcNAc...).`
`CARBOHYD`	`330 330`		`N-linked (GlcNAc...).`
`DISULFID`	`78 98`
`DISULFID`	`216 283`
`DISULFID`	`240 301`

Sequence information

Length: 424 AA [This is the length of the unprocessed precursor]

Molecular weight: 46304 Da [This is the MW of the unprocessed precursor]

CRC64: 9089903FBD268365 [This is a checksum on the sequence]

        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

P10761 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools