Zona pellucida sperm-binding protein 3 precursor

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Reviewed, UniProtKB/Swiss-Prot P10761 (ZP3_MOUSE)

Last modified January 19, 2010. Version 88. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Zona pellucida sperm-binding protein 3
Alternative name(s):
    Zona pellucida glycoprotein ZP3
    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:	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

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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.

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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.

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Ontologies

Keywords
Cellular component	Cell membrane Extracellular matrix Membrane Secreted
Domain	Signal Transmembrane
Molecular function	Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	binding of sperm to zona pellucida Inferred from direct assay. Source: MGI
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 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

Removed in mature form

PRO_0000041716

Regions

Topological domain

23 – 387

365

Extracellular

Transmembrane

388 – 408

Potential

Topological domain

409 – 424

Cytoplasmic

Domain

45 – 308

264

Amino acid modifications

Modified residue

Pyrrolidone carboxylic acid

Glycosylation

O-linked (GalNAc...) Probable

Glycosylation

O-linked (GalNAc...) Probable

Glycosylation

O-linked (GalNAc...) Probable

Glycosylation

146

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

Glycosylation

155

O-linked (GalNAc...) Probable

Glycosylation

162

O-linked (GalNAc...) Probable

Glycosylation

273

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

Glycosylation

304

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

Glycosylation

327

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

Glycosylation

330

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

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Experimental info

Mutagenesis

111

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

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

Mutagenesis

111

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

Mutagenesis

111

Y → S: Reduces protein solubility. Ref.8

Secondary structure

424

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P10761-1 [UniParc].

Last modified November 1, 1997. Version 4.
Checksum: 9089903FBD268365
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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

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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: 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]	"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: 15489334] [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: 1330788] [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: 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.
[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: 19052627] [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.

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Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

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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.

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P10761.

Proteomic databases

PRIDE

P10761.

Genome annotation databases

Ensembl

ENSMUST00000005073; ENSMUSP00000005073; ENSMUSG00000004948; Mus musculus. [Genome view]

GeneID

22788.

KEGG

mmu:22788.

UCSC

uc008zzl.1. mouse.

Organism-specific databases

CTD

22788.

MGI

MGI:99215. Zp3.

Phylogenomic databases

eggNOG

roNOG17165.

HOGENOM

HBG444650.

HOVERGEN

P10761.

InParanoid

P10761.

OMA

TNRAEVP.

OrthoDB

EOG9N8TR9.

PhylomeDB

P10761.

Gene expression databases

ArrayExpress

P10761.

Bgee

P10761.

CleanEx

MM_ZP3.

Genevestigator

P10761.

GermOnline

ENSMUSG00000004948. Mus musculus.

Family and domain databases

InterPro

IPR001507. Endoglin/CD105.
IPR017977. Endoglin/CD105_CS.
IPR017976. Endoglin/CD105_subgr.
[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 Resources

NextBio

303371.

SOURCE

Search...

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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:	January 19, 2010
This is version 88 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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